AsC~’09 Beijing

Joint Conference of the Asian
Crystallographic Association andChinese Crystallographic Society

Program Book

October 22-25 , 2009 • Beijing , China

AsCA ’09

Content

Welcome Message from Chairmen of Organizing Committee

1

AsCA ’09 Committees Members

2

AsCA ’09 Timetable &Scientific Program

I고

Generallnformation

15

Floor Plan for Exhibition Booths

21

Sponsors and Industrial Companies

22

List of participants

23

Welcome Message

AsCA ’09

DearC이 leagues ，You are cordially invited to Beijing for the Joint Conference of the Asian Crystallographic
Association and Chinese Crystallographic Society, AsCA’ 09 , from October 22-25 2009.
This conference is devoted to crystallography in Asia . The meeting aims to cover all aspects ofcrystallography, ranging from inorganic and organic small molecules to macromolecular proteins ,viruses , and membrane proteins; from crystal growth to protein engineering; from structuralchemistry and material science to nanoscience and nanotechnology; from crystal structure ,proteomics , and genomics , to drug design ; from diffraction physics and ray optics to theapplications of electron , neutron , and synchrotron X-ray photons for structural investigations , andso on .
Beijing , the host city of the 2008 Olympic Games , is the political , educational and cultural capital of
China . It offers an exciting and stimulating blend of rich cultural heritage and thoroughly modern
facilities. The city is home to many beautiful historic sites , including the Great Wall , the Forbidden
City, the Temple of Heaven , and the Summer Palace.

TheAsCA’09 meeting will be held in ‘Ji ngyi Hotel , an elegant conference facility opened prior to the2008 Olympic Games. Boasting excellent meeting , recreation and health facilities , ‘Jingyi Hotel islocated 6 km from downtown Beijing and 40 km from Beijing International Airport. It is within easyreach of many cultural sights , either via taxi or by subway from two nearby subway stations.
We look forward to welcoming you to Beijing in 2009. With your pa 미 cipation ， we have every
confidence that AsCA’ 09 will be a successful meeting , both scientifically and socially.

Zihe Rao
Chairman , AsCA’09
President of Nankai University

Jianhua Li n
Chairman , AsCA'’09
Vice President of Peking University

AsCA ’09

Committees

Intern하ional Program Committee
α1êIirman:. Peter Colman (Australia)

Jacqui Gulbis (Australia)

Pinak Chakrabarti (India)

Shigeyuki Yokoyama (Japan)

AltafHussain (Bangladesh)

Ashwini Nangia (India)

Junje Cho (Korea)

Jianhua Lin (China)

Seiki Kuramitsu (Japan)

Se Won Suh (Korea)

Zihe Rao (China)

Kunio Miki (J apan)

Peter Metcalfe (N ew Zealand)

Ian Williams (HK , China)

Masaki Takata (J apan)

Haiwei Song (Singapore)

Chwan-Deng Hsiao (Chinese Taipei)μ)CéI1 Organizing Committee@홉im홉n: Zihe Rao (N ankai University) , Jianhua Lin (Peking University)

Zhi-Jie Liu (Executive , IBP/CAS)

IShixiong Li때uzhou U)

IJiyang Wang (Shandong U)

lXIaodorlg Su (ExecutIVe, Peking U) Yang Lv (IMM/CAMS)

Mu Wang (N anjing U)!Jijie Chai (NIBS)

Zhenhong Mai (IOP/CAS)

Zheming Wang (Peking U)

Xiaolong Chen (IOP/CAS)

Liwen Niu (USTC)

Yicheng Wu (TIPC/CAS)

Xiaoming Chen (SYS U)

Feng Pan (Tsinghua U)

Ruiming Xu (IBP/CAS)

Jiangping Ding (SIBS/CAS)

Lianmao Peng (Peking U)

Ze Zhang (BUT)

Weimin Gong (IBP/CAS)

Yigong Shi (Tsinghua U)

Weitao Zheng (J ilin U)

Luhua Lai (Peking U)

Dacheng Wang (IBP/CAS)

Intemational Advisory Comm뼈e

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President of AsCA
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Secretarv-eeneral:

Mark Bartlam

Deoutv Secretarv-eeneral:.

Shunyi Wei , Xiaoke Xia, Neil Shaw

Secretariat~ Ke Chen , Yue Wang , Wenli Xu , Chongyun Cheng , Ping Shan , Weihong Zhou

-2-

Scient'뀔ic 띤rog~αm

Timetable

AsCA ’09

Thursday,

Registration
09 :00-21 :00
09:00

Saturday, October 24

Friday, October 23

October 22

Keynote-1 by Joel Sussman

Keynote-3 by David Owen

Meeting Room 1

Plenary lecture

Workshop 1
09 :00 Meeting Room 1

Hongkun Park

Keynote-2 by Matthew

Grand Ball Room

Rosseinsky

Meeting Room 1
Keynote-4 by Thomas Mak
Meeting Room 6

Meeting Room 6! MS-7: Membrane proteinsMS-1: Structural BiologyiGrand Ball RoomI MS-8: Organic crystal-12 :00
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and diffraction

and applications

crystallography

Meeting room 7

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Rigaku Lunchon Seminar

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Meeting

Poster Session!

Poster Session

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Meeting room 1

nano-materials

Meetíng room 6

13:30 iI

engineering andMS-3 : Neutron and

12:00

FaBr eakMS-13 : Hot structures

Meeting room 1

in diseaseMS-2 : Inorganic andWorkshop 1?

Tea BreakConference photo

09:50

10:00

Sunday, October 25

15:45

Rising Stars Symposium
Grand ball room

Workshop 2
13:30-17:00

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Meeting Room Q i MS-6: Advanced“”리

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13:30-17:00

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AsCA ’09

Scientific Program

T'h ursdav. October 22
09:00-12:00

Meeting Room 1 (2ndfloor)

Workshop 1: Macromolecular crystallization, data collection and dataprocessing techniques
13:30-17:00

Meeting Room 1 (2ndfloor)、.vorkshop 2: Direct-method SAD phasing and dual-space model completion

13:30-17:00

MeetingRoom6 (2ndfloor)

Workshop 3: Publication of Small Molecule Structures in IUCr Journals

18:00-19:00

Opening and Welcome -lUCr Plenary (Grand Ball Room , 2nd

f1 oor)Celebrating Crystallography
Ted Baker
Chair: Jianhua Lin

F 'ridav. October 23
09:00-09:50

Grand Ball Room뭔델욕표lVertical Nanowire Arrays: a Universal Platform for Interfacing with
Li ving Cells
Hongkun Park
Chair: Jing-Tai Zhao
09:50-10:10

Conference Photo

October 23. 10:00-12:0Q (Grand Ball Room)MS-l Structural Biolo휠 in disease
Chairs: Michael Parker, Xiao-Dong Su
10:00-10:25

Arms race between host and pathogen
꾀쁘드밸i

10:25-10:50

Structural studies of the Glutathione Transferases and their involvement
in resistance to chemotherapy treatment.
Lorien J Parke!, Paul J Dyson , Mario Lo Bello , Michael W Parker

10:50-11: 15

Structural Study of PA subunit from an Avian Influenza Virus RNA
polymerase
Yingfang Liu

11 : 15-11 :40

Li gand recognition by the TLR4-MD-2 complex

Jie-Oh Lee-4-

AsCA ’09

11 :40-12: 00

Scientific Program

Scaffold-based discovery of a novel selective inhibitor of oncogenic B-Raf
kinase with potent anti-melanoma activity
Kam Y1 Zhang

October 23. 10:00-12:0!L (Meeting Room 1, 2nd floor)
MS-2 Inorganic and nano-materials

Chairs: Ian Williams , Stephen S-Y Chui
10:00-10:30

Metal Organic Frameworks for Proton Conduction and C02 Uptake
1effHurd, Ramanathan Vaidhyanathan , 1ared Taylor, Simon Iremonger, Karl
Dawson , George Shimizu

10:30-11 :00

Homoleptic Metal Organothiolate and -selenolate Coordination Polymers[M(SR)n1 ∞ (n = 1-3): Structural Determination using Powder X-ray
Diffraction and Their Materials Properties
Stephen Sin-Yin Chu!, Kam-Hung Low, Roy VAL, Chi-Ming Che

11 :00-11 :20

Ionothermal Synthesis of Metal Organic Framework Materials
Zhu이 ia Li!!, Linna Huang , Ming-Liang Tong , Russell E Morris

11 :20-11 :4 0

To bridge or not to bridge - carbonylligand configurations in some
phosphine and arsine substituted tricobalt carbon cluster systems
Jim Simpsor1, C 10hn McAdam , Brian H Robinson , Roderick G Stanley

11: 40-12:00

Crystal Engineering of Chiral Metal Organic Frameworks (MOFs) fromTartrates and N-Donor Spacer Ligands
PokkaK-C Pang, Herman H-Y Sung , Ian D Williams

October 23 , 10:00-12:00 (Meeting Room 6, 2nd floor)

MS-3 Neutron and synchrotron sources and applications
Chairs: Richard Garrett , Hongjie Xu

10:00-10:20

Current status and future development of neutron scattering at China
Advance Research Reactor
Dongfeng Che!!, Yuntao Liu , Hongli Wang, Kai Sun, Meimei Wu

10:20-10 :4 0

Current Status of Shanghai Synchrotron Radiation Facility
hanhua H~， Zhentang Zhao , Hongjie Xu

10:40-11 :00

Crystallography and Materials Science at the J-P ARC pulsed sp 쩌 lation
neutron facility
Takashi Kamivama

11 :00-11 :20

The Current Status of Taiwan Photon SourceX브쁘효rrg， Mau-Tsu Tang , Gwo-Huei Luo , Yaw-Wen Yang , Keng S Liang

11 :20-11 :40

Cold Neutron Research Facility at HANARO
Kve Hong Le~， Young Ki Kim-5-

Scientific Program

AsCA ’09

11:40-12:00

New Facilities for Australian Research:
The Australian Synchrotron and the OP AL Research Reactor
Ri chard F Garrett

October 23. 12:00-13:3!!_Ri gaku Lunchon Seminar (Grand ball room)
October 23. 14:00-16:00
14:00-16:00

nd
Poster Session !_(Poster room and corridor on the 2 f1 oor)

October 23.16:00-18:30 (Meeting room 1)

MS-4 Macromolecular assemblies (viruses, proteins, protein-nucleic acid complexes)
Chairs: Peter Metca1f, Tomitake Tsukihara

16:00-16:30

Structure of the bacterial flagellum and the mechanism of its self-assembly
Katsumi Imada

16:30-17:00

Understanding cytokine receptor signaling
Guide Hansen , Tim R Hercus , Jack Kn g Scott, Angel F Lopez , Michael W
Parker

17:00-17:30

Effector recognition ofRab and Arffamily small G proteins in vesicletransport and membrane remodelling
Soichi Wakatsuki

17:30-17:50

Structural Basis of Transcription: Backtracked RNA Polymerase 11
Don 2: Wang , Roger D Komberg

17:50-18: 10

Structure of RNA-guided RNA Modification Enzymes
KeQion 2: Y~， Ling Li , Jingqi Duan , Ru Jia, Jinzhong Lin, Minghua Ju , Jin Peng ,Anbi Xu , Liman Zhang

18:10-18:30

RNA-protein interactions in the core domain ofspliceosomal U4 snRNP
Ade1aine K W Leung, 갤de Li , Ki yoshi Nagai

October 23. 16:00-18:30 (Meeting Room 6)

MS-5 Charge density studies
Chairs: Masaki Takata , Yu Wang

16:00-16:30

Recent Progress in X-ray Charge Density Studies of Advanced Materials
Bo B Iversen

16:30-16:55

Non-linear Optical Properties and Spin Densities from X-ray Charge
Density Measurements
Dvlan Javatilaka

16:55-17:20

Exploring Halogen -Halogen interactions via charge density analysis
Guru Row-6-

A sCA ’09

Scientific Program

17:20-17 :4 5

ChaUenge to Atomic Orbital Visualization by 0.2A Resolution
Synchrotron Radiation Single Crystal Experiment
Hiroshi Saw~， E니 i Nishibori , Shinobu Aoyagi

17:45-18:10

MEM Electrostatic Potential Imaging
Hiroshi Tanaka

18:10-18:30

Photo-induced Structure Determination and Electron Density Study by
MEM of Spin Crossover Complex [Fe(abpt)2(NCS)2]
Che Hsiu Shih, Chou Fu Sheu, Kunihisa Sugimoto , Jungeun Kim , Kenichi
Kato , Yu Wang , Masaki Takata

October 23 , 16:00-18:30 (Meeting Room 7, 2 nd floor)

MS-6 Advanced X-ray/neutronlelectron imaging techniques
Chairs: Steve Will이ns ， Mau-Tsu Tang

16:00-16:30

Recent Developments in Coherent Diffractive
Imaging Instrumentation and Applications
Andrew G Peele

16:30-17:00

Visualization ofBio-Structures Using Coherent X-Ray Diffraction
Yoshinori NishinQ, Kazuhiro Maeshima, Naoko Imamoto , Ryuta Hirohata,
Eiichiro Matsubara, Yukio Takahashi , Tetsuya Ishikawa

17:00-17:30

Phase imaging using a liquid ce lI in a transmission x-ray microscope
Gun!.!-Chian Yin

17:30-17:50

Improved Accuracy Laue Neutron Diffraction
Ross Pilt~， Alison Edwards

17:50-18: 10

Development and AppIication of Neutron 2D-Counter for Crystal andMagnetic Structure Analysis
YN으da， C-H Lee , M-K Moon , S-A Kim , Y Ishikawa , H Ki mura , R Ki yanagi

18:10-18 :30

State-of-the-art Mu ItiI ayer Optics for Modern X-ray Analysis
J Wiesmann, T Samtleben , C Michaelsen, B Hasse , J Graf, F Hertlein

S'a turdav. October 24
09:00-09 :50

Meeting Room 1
Kevnote 1
Proteopedia - a Scientific ‘ Wiki ’ Bridging the Ri ft Between 3D Structure
and Function of Biomacromolecules
Joel Sussman
Chair: Jenny Martin

09:00-09:50

Meeting Room 6
Kevnote 2
Reactivity and flexib iIi ty in metal-organic frameworks: amino-acid based
and post-synthetica Ily functiona Ii sed materials-7-

Scientific Program

AsCA ’09
Matthew Rosseinsky
Chair: Gautam Desiraju
October 24. 10:00-12:0!!..._(Meeting Room 1)
MS-7 Membrane proteins
Chairs: Jacqui Gulbis , Kenji lnaba’

10:00-10:25

Structure and mechanism of an amino acid antiporter
Yigong Shi

10:25-10:50

The structure of human connexin 26 gap junction channel
Shoii Maed~， So Nakagawa, Michihiro Suga, Eiki Yamashita , Atsunori Oshima,
Yoshinori Fujiyoshi , Tomitake Tsukihara

10:50-11 : 15

The role of AmtB-GlnK complex in nitrogen reg띠 ation
Xiao-Dan Li, Fritz Wi nk1 er, Mike Merrick

11: 15-11 :40

Structure and function of A-A TPase: combining electron microscopy and
X-ray crystallography to study a transmembrane rotary motor complex
Lawrence K Lee , Alastair G Stewart, Mhairi Donohoe , 01ga Esteban , Ricardo
I-em-a-l띄 anie1a_SJ.Qç_k

1 1: 40-12:00、

Crystal Structure of Bacterial Nitric Oxide Reductase, a Key Enzyme in
the Respiratory Evolution
Yushi Matsumoto , Shingo Nagano , Yoshitsugu Shiro

October 24. 10:00-12:00 (Meeting Room 6)

MS-8 Organic crystal engineering and structure
Chairs: VR Pedireddi , Suresh Valiyaveettil"'

10:00-10: 10

lntroduction by Chairs

10: 10-10:35

Engineering Organic Crystals using Arene-Perfluoroarene Interactions
Todd B Marder

10:35-11 :00

Proton Dynamics in Hydrogen-bonded Organic Solids - from Protonic
Dielectrics to Proton-motor
Tadashi Sugawar~， Kentaro Suzuki

11 :00-11 :20

Structure-property correlations: mechanical properties of molecular
crystals
C Malla ReddY, Michael T Ki rchner, K An antha Padmanabhan ,Gautam R Desiraju

11 :20-11 :40

Polymorph and pseudo-polymorph of co-crystal; controlling formationand structural transition
따i욕으묘브， Xiu-Juan Jiang , Min Tang

11 :4 0-12:00

Towards knowledge-based design and control of pharmaceutical crystal
forms
-8-

AsCA ’09

Scientific Program
Colin R Groom , Peter T A Galek , Peter A Wood

October 24‘ 10:00-12:00 (Meeting Room 7)

MS-9 Small angle scattering and soft materials crystallography
Chairs: Naoto Yagi , Monnhor Ree

10:00-10:30

A smalllwide-angle X-ray scattering instrument for structuralcharacterizations with soft matter, nanomaterials, and air- Ii quidinterfaces
U-Ser Jeng~ Chiu Hun Su , Chun-Jen Su , Kuei-Fen Liao , Wei-Tsung Chuang ,Ying-Huang Lai , Je-Wei Chang , Yi-Jiun Chen , Yu-Shan Huang , Ming-Tao Lee ,Kuan-Li Yu , Din-Goa Liu , Zia-Fung Chang , Chin-Yen Liu , Chien-Hung Chang ,Keng S Liang

10:30-11 :00

Surface and flow ordering of complex fluids
WTA HamiltoD_, L Porcar, PD Bu t1 er, GG Warr

11 :00-11 :30

Intimate Relationship between Micro-phase Separation and Crystalline
Phase Transitions in P이yethylene- Poly( ethylene Oxide) Diblock
Copolymer as Viewed by Synchrotron SAXSIWAXD and I RlRaman
Measurements
Kohii TashirQ, Weiyu Cao , Makoto Hanesaka, Hiroyasu Masunaga, Sono
Sasaki , Masaki Takata

11 :30-11 :45

The Quol ka Small Angle Neutron Scattering Instrument at OPAL
Richard F Garret1, Elliot P Gilbert , William A Hamilton , Kathleen Wood

11 :45-12:00

The effect of interface on the crystallization behavior of poly(3hydroxybutyrate) uIt ra-thin film revealed by grazing incident X-ray
dffraction
Xiaoli SuD_, Harumi , Sato , Yukihiro Ozaki , Shouke Yan , Isao Takahashi‘

AsCA Council Meeting (Meeting room 3)
October 24‘ 14:00-16:00
14:00-16:00

Poster Session ~(Poster room and corridor on the 2 nd floor)

October 2416:00-18:30 (Meeting Room 1)

MS-l0 New tools for macromolecular crystallography (including structural genomics)
Chairs: Kunio Miki , Joel Sussman

16:00-16:25

Tracking ligand migration pathways in carbonmonoxy myoglobin at
cryogenic temperatures
Shin-ichi Adachi

16:25-16:50

Exploring the conformational energy landscape of acetylch 이 inesterase by
kinetic crystallography-9-AsCA ’09

Scientific Program
Jacques-Philippe Colletier , Benoît Sanson , Didier Foumier, Joel L Su ssman ,Israel Silman , Dominique Bourgeois , Martin Weik

16:50-17:10

Structure ofHIV-l Protease in Complex with Inhibitor KNI-272
Determined by Neutron Crystallography
Motovasu Adach!, Ryota Kuroki

17: 10-17:30

Taking the edge off: The softer side of in-house SAD phasing
Joseoh D. Ferrar~， James W. Pt1 ugrath , Cheng Yang

17:30-17:50

Reductive methylation of surface lysines assists crystallization of proteins
T'lJ'eil Shaw, Chongyun Cheng , Zhi-Jie Liu

17:50-18: 10

Improvement of a new rotation function for molecular replacement by
designing new scoring functions such as relative entropy and dynamic
correlation coefficientE웰J빡gg， Wei Ding

18:10-18:30

New and Underused Methods for X-ray Crystallography at Low
Resolution
Yong Xiong

October 24 , 16:00-18:30 (Meeting Room 6)

MS-l1 Metal-organic crystal engineering
Chairs: Ian Williams , Jing-tai Zhao

16:00-16:30

Thermoelectric Zintl Compounds in R-T-Sb (R = Ca , Sr, Ba , Eu , Yb; T =Zn , Cd) Systems
XJ Wang , H Zhang , MB Tang , XX Yang , HH Chen, ZY Man ,U Burkhardt, Y Grin , J工ζhao

16:30-17 :00

Solid-state photochemical reactivity of coordination polymers and metal
complexes containing trans-l ,2-bis(4-pyridyl)ethylene
Jagadese J Vitta1, Mangayarkarasi N agarathinam, Abdul Malik Puthan
Peedikakkal

17 :00-17 :25

Anatomy of a void in an aluminium-copper-tin aUoy
Laure Bourgeoi~， Matthew Weyland, Philip NH Nakashima, Baπy C Muddle

17 :25-17 :45

SMART X2S - Chemical Structures at the Touch of a Button
Eric Hovestrevd1, Michael Ruf, Holger Ott

17:45-18:00 . Rational Design , Synthesis and Properties of Layered Compounds
LnOZnSb (Ln=La , Ce, Pr, Nd)효쁘흐브으， Hao-Hong Chen , Zhen-Yong Man, Mei-Bo Tang , Xin-Xin Yang ,Xiang-Xin Guo , Jing-Tai Zhao
18:00-18:15

Cation ... Cation Supramolec비 ar Interactions in Zinc-ImidazoleOxovanadate Compounds
Samroeng Krachodnok, Kenneth J Haller, Ian 0 WilliamsmAsCA ’09

18:15-18:30

Scientific Program

Synthesis and X-ray Structures ofDiorganotin Complexes with
Tris{ (hydroxymethyl)aminomethane Schiff baseSee Mun Le~， Hapipah Mohd Ali , Kong Mun Lo

October 24 , 16:00-18:30 (Meeting Room 7)

MS-12 Powder diffraction
Chairs: Xiaolong Chen , Takashi Ida

16:00-16:25

Precise Structure Analysis of Ceramic Materials up to 1830 K
Masatomo Yashima

16:25-16:50

Structural analysis of zeolites and related functional materials
Yingxia Wang

16:50-17: 10

Spinner-Scan Method for Evaluation of Particle Statistics in Powder
Diffractometry
TakashiId~， Taishi Goto , Hisashi Hibino

17: 10-17 :30

Structural and magnetic properties of doped wide bandgap
semiconductors
Gang Wang

17:30-17:50

Vanadium substituted potassium tungsten bronzes - synthesis andcharacterization
A M Abdullah, A Hussain

17:50-18:10

Charge density study from high resolution powder diffraction data
Eiii Nishibori, Shinobu Aoyagi, Hiroshi Sawa

18:10-18:30

Interplay between the crystalline and magne디c structures in lightly
Cr-doped Bio.37CaO.63Mno.96CrO.04 O 2.9
Wén-Hsien L i, Chun-Chuen Yang , Chun-Ming Wu , Jirong Sun, Jeffrey W Lynn

S undav. October 25
09:00-09:50

Meeting Room 1
Kevnote 3
Cargo recognition during clathrin-coated vesicle formation
David Owen
Chair: Soichi Wakatsuki

09:00-09:50

Meeting Room 6
Kevnote 4
Crystalline silver(I) complexes containing all-carbon and carbon-richanionic ligands
Thomas Mak
Chair: JJ Vittal-11-

Scientific Program

AsCA ’09
October 25. 10:00-12:0!! (Meeting Room 1)

MS-13 Hot structures
Chairs: Se-Won Suh , Yigong Shi
10:00-10:25

The structure of rat liver vault
Hideaki Tanaka, Koji Kato , Eiki Yamashita, Tomoyuki Sumizawa, Yong Zhou ,Min Yao , Kenji Iwasaki , Masato Yoshirnura, Iornitake Tsukihara

10:25-10 :50

Recognition ofNuclear Export Signal by CRM1
Yuh Min Chook

10:50-1 1: 15

NEMO regulates NF-KB activation by specific recognition of linear
ubiquitin chains
Sirnin Rahighi , Fumiyo Ikeda, Masato Kawasaki , Masato Akutsu , Nobuhiro
Suzuki , Ryuichi Kato , Tobias Kensche , Tarnarni Uejirna, Stuart Bloor, David
Kornander, Felix Randow , Ivan Dikic , Soichi Wakatsuki

11: 15-11 :40

The atomic structure of granulovirus polyhein at 1.8Á resolution
Elaine Chiu , Shin-Mei Yeh, Ri chard Bunker, Clernens Schulze-Briese , r.학학
Metcalf

11 :40-12:00

Crystal structure of human REV7 in complex with REV3 fragment
Kodai Hara, Toshiyuki Shirnizu, Yoshiki Murakumo , Shunsuke Kobayashi ,Toshiaki Kogame , Satoko Ak ashi , Satoru Unzai , Torno Hanafusa , Haruo
Ohrnori , Shunichi Takeda, Marnoru Sato , Hiroshi Hashirnoto

October 25 , 10:00-12:00 (Meeting Room 6)
MS-14 Superconductivity and crystal properties
Chairs: Mohana Yethiraj , Xian-Hui Chen
10:00-10:40

High Pressure Synthesis and Superconducting Properties of Oxygendeficient Oxypnictide Superconductors LnFeAs0 1_y묘￡샌 aki ， K Miyazawa, M Nakajirna , S Ishida, M Ishikado , K Kihou , P M
Shirage , C H Lee , N Takeshita, R Kumai , Y Tornioka, H Kito , K M K이 ima， T
Ito, S Sharnoto , S Uchida , A Iyo

10 :40-11 :20

Diffraction Study of the Fe-based High Temperature Superconductors
Wei Bao

11 :20-11 :40

Electric Polarisation Flop and Magnetic Phase Transition Induced
Magnetic Field in Multiferroic RMn20S (R=Tm , Yb)
Hirovuki Kirnur~， Yuma Sakarnoto , Marnoru F따cunaga， yl따이 o Noda,
Nobuyuki Abe , Kouji Taniguchi , Taka-hisa Ar ima, Shuichi W;따이 rnoto ，Kazuhisa Kakurai

11 :40-12:00

Effect of Ga3+ Substitution for Mn3+ on Magnetic and Dielectric
Properties in Multiferroic YMn20S
Yurna SakarnotQ, Hiroyuki Kirnura , Satoru Horio , Arn o Fey, Mamoru
Fukunaga, Ryoji Ki yanagi , Yukio Noda, Hiraka Haruhiro
-12-

by

AsCA ’09

Scientific Program

October 25 , 16:00-18:30 (Meeting Room 7)
MS-15 Electron microscopy and diffraction

Chairs: Laure Bourgeois , Koh Saitoh
10:00-10:30

Electron Microscopy ofLow-Dimensional Nanomaterials
Fangfang Xu

10:30-11 :00

3 Dimensional Coherent Electron Diffractive Imaging of a N anoparticle
Fu-Rong Cheg, Roman Dronyak, Keng S Liang

11 :00-11 :30

High Resolution Structural Analysis of Membrane Proteins by Electron
Crystallography
Kaoru Mitsuoka

11 :30-11 :45

Strain Mapping near Si/SiGe Interfaces Using HOLZ Line CBEDPatterns
Koh Saitoh, Maiko Hamabe , Nobuo Tanaka

11 :4 5-12 :00

Visualisation of the Orbital-ordered State of FeCr204 using the CBED
MethodDaisuke Morikaw~， Kenji Tsuda, Shintaro Ohtani , Takahisa Ar ima

October 25 -12:00-13:3!!_ CCrS Council Meeting (Meeting room 3)
October 25 -13:30-16:3~ (Grand Ball Room)
13:30-15:30

Ri sing Stars Symposium

Chair: Mitchell Guss
15 :4 5-16 :35

뀐댄ill}'__으

Structural physiology based on electron crystallography
Yoshinori Fujiyoshi
Chair: Zhi-Jie Liu-13-çene1jα {Informα，tion

AsCAJ’'09

Generallnformation

Conference Venue
The AsCA’ 09 conference , including poster presentations and company exhibitions , will beheld on the 2nd f1 00r ofthe Jing-Yi hotel from Oct. 22 to 25 , 2009. The Jingyi Hotel is located
11 km from downtown Beijing and 30 km from Be너 ing Intemational Airport. It is within easyreach of many cultural sights , either via taxi or by subway from 1\νo nearby subway stations.

Registration Desk
The registration desk will be located in the lobby of Jingyi hotel on Oc t. 22. From Oct.
nd23- 25 , the registration and information desk will be moved to the 2 f1 00r near the Grand
Ball Room. The registration desk will be open during the following days and times:
Oct. 22 (Lobby of the Jingyi Hotel): 9:00 - 21 :00
Oct. 23 - 25 (2 nd floor, near the grand ball room): 09:00-11:30 , 13:30-17:30
Any inquiries about the registration , social events , tours , etc. may be answered byapproaching any of the staff at the registration desk. Participants may pick up their
Conference kits , badges and invitations/tickets at the registration des k.
On-site Registration Fees
Full Registration
Full-time Student Registration
Accompanying Person
One Day Registration

USD $500 or RMB341 0
USD $350 or RMB2387
USD $200 or RMB 1364
USD $150 or RMB 1023

Payment On-site
Cash and credit cards (Master, Visa and American Express) are acceptable. No personal checkand traveler ’ s check are accepted for the payments. All bank charges will be bome by thepartlclpant.

Instructions for Presentations
CDPresentation facilities:
Powerpoint presentations are encouraged for oral presentations. Laptop Computers and data
If you would like to use your own
pr이 ectors will be made available in the meeting rooms.
computeζ please send it to our staff at least 20 minutes before the session ofyour speech.
@Speakers' Information Desk
There will be a designated computer located at the Speakers ' Information Desk. This desk will
be somewhere near the registration desk. The speakers are encouraged to copy their files tothe computer at your earliest convenient time , or are kindly requested to copy yourpresentation files into this computer at least 20 minutes before the session of your speech.
Speakers are advised to preview their presentations before the start of each session.
@Poster session:-15-

Generallnformation

AsCA'09

1) A display board measuring 90cm wide by 120cm high will be provided for each poster.
Poster boards are numbered according to the same numbering scheme in the abstractbook.
2) The poster presentations will be in the room next to the grand ball room on the second
f1 oor. The posters will be divided into hνo sessions during the conference. The firstsession of the posters with odd numbers are requested to be set up in the aftemoon of
Oc t. 22 and its presentation is scheduled at 13:30-15:30 on Oct. 23. The second session of
the posters with even numbers are requested to be set up in the same poster room at
20:00-2 1: 30 on Oc t. 23 and the poster presentation is scheduled at 13:30-15:30 on Oct.
24.

1) During the two poster displays , presenters are requested to remain in front of theirposter boards to meet with other attendees.
2) Please note that the frrst session of the poster presenters are advised to take down theposters before 19:00 on Oc t. 23 and the second session ofthe poster presenters shouldtake down the posters before 12:00 on the Oc t. 25.
All posters left uncollected at the end 01 its session will be disposed 01 by the staff.
‘

3) The schedule for poster presentation:
A. Ri sing Star Symposium : 13:30-15:30 on Oct. 25
The candidates of Ri sing Star Award are advised to prepare a 15 minutes talk. Sixof the candidates will be selected for presentations in the Ri sing Star Symposium.
B. Posters of first session:
The time for setting up poster: from 14:00 on Oc t. 22
Poster Presentation: 13:30-15:30 on Oct. 23
C. Posters of second session: Oc t. 23-24
The time for setting up poster: 20:00-21 :30 on Oc t. 23
Poster Presentation: 13 :30-15:30 on Oc t. 24

Exhibition
A scientific exhibition will be held during the AsCA"09 to highlight recent developments intechnology and to demonstrate new products for the crystallography research and related
fields. The exhibition will be on the 2nd f1 oor, where is in front of the grand ball room andnear the poster session area. The exhibition will be open from 9:00-18:00 from Oc t. 23 - 25.

Tea breaks
Moming and aftemoon tea breaks will be served daily adjacent to the grand ball room wheremineral water, tea, coffee and snacks will be provided ..

Internet
Intemet access is available in each guest room of the Jingyi Hotel with free of charge.

-16-

AsCA ’'09

Generallnformalion

Meals
CDLunches:
1) There are three restaurants and two bars inside Jingyi Hote l.
are within walk distance from hote l.

A few more restaurants. 2) Lunchon Seminar: Ri gaku Corporation will organize a seminar at lunch time on Oc t. 23.
The participants are welcome to attend and the lunch will be provided. The seminar
vouchers are available at the registration desk or Rigaku ’ exhibition booth.

s@Dinners:
The dinners for registered participants will be provided in the Chinese Restaurant and Rose
Cafe located on the first floor of Jingyi hotel on Oct. 23 and Oc t. 25 . The coupons will beplaced in your registration package.

@Welcome reception and conference banquet
The welcome reception (Oc t. 22) and conference banquet (Oc t. 24) will be held in the grandball room ofthe second floor. The coupons will be placed in your registration package.

Breakfast:

7:30 - 8:30
51
Participants who stay in Jingyi hotel will have breakfast on the 1 floor of the hote l.
remembεr to show your room card when having breakfas t.

PleaseSmoking
Please be advised that smoking is not permitted inside the meeting rooms .

Social Events
Oct. 22nd(Thursdav):

9:00-12:00: Workshop 1: Macromolecu/ar crystallization, data collection and data processing
techniquesndMeeting room 1 (2 floor)
13:30-17:00: Workshop 2: Direct-method SAD phasing and dual-space model completion
Meeting room 1 (2 nd floor)
14:00-1 ’7:00: Workshop 3: P ublication ofSmall Molecule Structures in l UCr J ournals
Meeting room 6 (2ndfloor)

18:00 -19:00: Opening Ceremony & IUCr Plenary Lecture
Grand Ball Room (2ndfloor)-17-

AsCA ’'09

Generallnformation

19:00 -20:30: Welcome Reception for registered participants
Grand Ball Room (2 nd floor)
Oct. 23 rd (Friday):

09:50-10:10: Picture taking for all paπicipants will be in the lobby of the hote l. Please don ’t
miss it!
12:00-13:30: Lunchon Seminar by Rigaku Corporation
Oct. 24 th (Saturday):

19:00 -21:00: Conference Banquet for registered participantsAwards Ceremony: AsCA Travel Awards , IUCr Travel Awards , Rising Star
and Poster Awards
Grand Ball Room (2 nd floor)
Oct. 25 th (Sunday):

13:30 -15:30: Ri sing Star Symposium
Grand Ball Room (2 nd floor)

Business Meetings
Oct. 22 nd (Monday):

09:00 -18:00: Ri gaku Corporation Meeting
Meeting room 3 (2 nd floor)
Oct. 24 t \Saturday):

12:30 -13:30: AsCA Council Meeting
Meeting room 3 (2 nd floor)
Oct. 25 th (Sunday):

12:30 -13:30: CCrS Council Meeting
Meeting room 3 (2 nd floor)

Weather
The optimal season to visit Beijing is Autumn. Late October in B 며 ing is sunny andcomfortable with a little bit cold. The average daily temperature is about 12 oC /53 0 F , withhighs of around 18 0 C /64 0 F and lows of around 6 0 C /43 0 F. It is an ideal time for tourists to
enj oy the beautiful sites of Beij ing-18-

Generallnformalion

AsCA'09

NameBadges
Please do wear your Conference name badge at all times. In addition , tickets issued in yourregistration package must be presented for all social events.
많뱀mαιuμ αm‘ιParticipants:
Exhibitors:
Accompanying persons:
Host staff:

’4L

M

Nm

””‘Z

Public Transportation
Transportation in Beijing is convenient, with buses and subway/light rai l.
••

Bus: The bus ride in Beijing costs about 1 yuan - 3 yuan depending on distance.
Most city buses run from 5:30 ~ 22:00.
Subway/Light rail: The full fare is about 3 yuan.

Taxis
Taxis are everywhere in the city and is the most convenient way to get around. Taxis charge
2.0 yuan per kilometer for the first 10 km , and then 2 .4 yuan for every additional kilometer.
Toll fees are an extra. It costs around 100 yuan from the airport to the Jingyi hotel and about
35 yuan to downtown.

Secretariat
If you need help or have any requirements during AsCa ’ 09 , please contact the conference
secretariat at the registration desk from Oc t. 23 - Oc t. 25 during daytime hours. Alternatively,
the conference secretariat can be reached in the Jingyi Hotel in the evening. The room number
and telephone number of the staff will be available on the information board either in thelobby of the Jingyi hotel or on the information desk near the meeting room area.
Or you can contact the staffs below by cell phone if needed
Mr. Xiaoke Xia:

Ms. Shunyi Wei:
Ms. Ke Chen:

13601365704
13011058198
15901483571

Attention
1. All participants are advised to wear name badge during the conference.
2. Please note that all participants are requested to present the corresponding ticket for themeals during the conference , including Welcome Reception and Conference Banque t.
3. The local organizing committee of AsCA’ 09 will set up receiving stations for theparticipants both in Terminal No. 2 and Terminal No.3 ofthe Be니 ing International Airport
on Oc t. 22. The participants are advised to look for the AsCA’ 09 sign near the exit doors.
The staff will escort you to the taxi stand.
-19-

AsCA’'09

Generallnformation

Taxi service: The cost of the taxi from the airport to the Jingyi Hotel is about RMB 100
yuan. Please show the Taxi Direction Note and map below to the taxi drivers.
Please be advised that you should not accept a taχi service offer anywhere other than at
the taxi stand 01 the airport.

TAXINOTE
Please take me to the Jingyi Hotel. Thank YOu!
i좁 i쏟 我 到 京

1)( 大 酒 店，

얘f 없fAddress of Jingyi Hotel: 北 京海:波 E 大챔 츄末 路 9 융벌 i굶 (Tel): 010-62165588

냐J 훗村

科技
因[츠

후 i좁路

/hO I1l!l)lI nnC lIl1
lunc

맺 i효因 E()1~ mpic 1011ι

Xucqinglu

Icchnolc믿，~때챔-짜:l tR중格|--=톨페톰.~-20-

AsCA ’09

Floor plan for exhibition

1 I 2 I 3 I 4 I 5 I 6!

버￡

내내
!{

Elevator

Booth Number

I

Exhibitor Name

Booth Number

Exhibitor Name

11

」 PDBJ; Pr야만!l. P~t~. . ~.~.~. . I~p~!ll4l1+23l5, Inc!1 GN Blosystems

Se멧응t Scientific Inc

Oxford Diffraction

16

i Microlvtic

17

I Bioray Instruments Limited /‘‘·“·‘·‘.‘.“‘‘‘‘?Ç!~I.Q~~.~t ç<?φData Centre“ “ “ “ · ‘ … “ . __ . .. .

19

i Bruker AXS GmbH20

i TTP LabTech Ltd China Office21

GE Healthcare‘ ‘......... --21-

AsCA ’09

Sponsors and Industrial Companies

5vonsors
Rigaku Corporation
Thermo Fisher Scientific ( China ) Co. , Ltd
Marresearch GmbHGE Healthcare

Exhibitors
Oxford Diffraction
Cambridge Crystallographic Data Centre
Rayonix, LLC
TTP LabTech Ltd China Office
Bioray Instruments Limited / XtalQuest Corp.
Bruker AXS GmbH
Area Detector Systems Corporation
Microlytic
Intemational Union of Crystallography
Oxford Cryosystems LTD
Dawning Information Industry Co. , Ltd
PDBj: Protein Data Bank JapanGN Biosystems , Inc.
Hamilton Bonaduz AG Shanghai Rep. Office
Seajet Scientific Inc.

-22-

AsCA’09 Beijing
Joint Conference of the Asian
Crystallographic Association andChinese Crystallographic Society

Abstract Book

October 22-25, 2009 • Beijing, China

AsCA’09

Content

Plenary and Keynote Lectures
PL-1
PL-2
PL-3

Celebrating Crystallography

2

Edward N. Baker

Vertical Nanowire Arrays: a Universal Platform for Interfacing with Living Cells
Hongkun Park

Structural physiology based on electron crystallography
Yoshinori Fujiyoshi

4
6

Proteopedia - a Scientific ‘Wiki’ Bridging the Rift Between 3D Structure and

KN-1

Function of Biomacromolecules

8

Joel L Sussman, Eran Hodis, Jaime Prilusky, Israel Silman, John Moult , Eric Martz

Reactivity and flexibility in metal-organic frameworks: amino-acid based andKN-2

post-synthetically functionalised materials

10

M.J. Rosseinsky

KN-3

Cargo recognition during clathrin-coated vesicle formation
David Owen

12

Crystalline Silver(I) Complexes containing All-carbon and Carbon-rich Anionic

KN-4

Ligands

14

Thomas C. W. Mak

MS-1: Structural Biology in disease
1

Arms race between host and pathogen
Jijie Chai

15

Structural studies on the Glutathione Transferases and their involvement in2

resistance to chemotherapy treatment

15

Lorien J. Parker, Paul J. Dyson, Mario Lo Bello , Michael W. Parker

3
4Structural Study of PA subunit from an Avian Influenza Virus RNA polymerase
Yingfang Liu, Zihe Rao

Ligand recognition by the TLR4-MD-2 complex
Jie-Oh Lee

16
17

Scaffold-Based Discovery of a Novel Selective Inhibitor of Oncogenic B-Raf
Kinase with Potent Anti-Melanoma Activity
Kam Y.J. Zhang, James Tsai, John T. Lee, Weiru Wang, Jiazhong Zhang, Hanna Cho, Shumeye5Mamo, Ryan Bremer, Sam Gillette, Jun Kong, Nikolas K. Haass1, Katrin Sproesser, Ling Li, Keiran
S.M. Smalley, Daniel Fong, Yong-Liang Zhu, Adhirai Marimuthu, Hoa Nguyen, Billy Lam, Jennifer

18

Liu, Ivana Cheung, Julie Rice, Yoshihisa Suzuki, Catherine Luu, Calvin Settachatgul, Rafe Shellooe,
John Cantwell, Sung-Hou Kim, Joseph Schlessinger, Brian West, Ben Powell, Gaston Habets, Chao
Zhang, Prabha N. Ibrahim, Peter Hirth, Dean R. Artis, Meenhard Herlyn, Gideon Bollag

MS-2: Inorganic and nano-materials
Metal Organic Frameworks for Proton Conduction and CO2 Uptake

1

Jeff Hurd, Ramanathan Vaidhyanathan, Jared Taylor, Simon Iremonger, Karl Dawson, George
Shimizu-I-

19

AsCA’09

Content
Homoleptic

2

Metal

Organothiolate

andOrganoacetylide

Coordination

Polymers: Structural Determination using Powder X-ray Diffraction and Their
Materials Properties

19

Stephen Sin-Yin, CHUI, Kam-Hung, LOW, Roy V. A. L., Chi-Ming CHE

3

Ionothermal Synthesis of Metal Organic Framework Materials
Zhuojia Lin, Linna Huang, Ming-Liang Tong , Russell E. Morris

20

To bridge or not to bridge – carbonyl ligand configurations in some phosphine4

and arsine substituted tricobalt carbon cluster systems

21

Jim Simpson , C. John McAdam, Brian H. Robinson, Roderick G. Stanley.

Crystal Engineering of Chiral Metal Organic Frameworks (MOFs) from5

Tartrates and N-Donor Spacer Ligands

22

Pokka K-C. Pang, Herman H-Y. Sung, Ian D. Williams

MS-3: Neutron and synchrotron sources and applications
Current status and future development of neutron scattering at China Advance1

22

Research Reactor
Dongfeng Chen, Yuntao Liu, Hongli Wang, Kai Sun, Meimei Wu

2Current Status of Shanghai Synchrotron Radiation Facility
Jianhua He, Zhentang Zhao, Hongjie Xu

23

Crystallography and Materials Science at the J-PARC pulsed spallation

3

24

neutron facility
Takashi Kamiyama

4
5

The Current Status of Taiwan Photon Source
Yu Wang, Mau-Tsu Tang, Gwo-Huei Luo, Yaw-Wen Yang, Keng S. Liang

Cold Neutron Research Facility at HANARO
Kye Hong LEE, Young Ki KIM

25
25

New Facilities for Australian Research: The Australian Synchrotron and the

626

OPAL Research Reactor
Richard F. Garrett

MS-4: Macromolecular assemblies (viruses, proteins, protein-nucleic acid complexes)
12Structure of the bacterial flagellum and the mechanism of its self-assembly
Katsumi Imada

Understanding Cytokine Receptor Signalling
Guido Hansen, Tim R. Hercus, Jack King-Scott, Angel F. Lopez, Michael W. Parker

27
27

Effector recognition of Rab and Arf family small GTPases in vesicle transport

328

and membrane remodeling
Soichi.Wakatsuki

4Structural Basis of Transcription: Backtracked RNA Polymerase II
Dong Wang, Roger D. Kornberg

29

Structure of RNA-guided RNA Modification Enzymes

5

Keqiong Ye, Ling Li, Jingqi Duan, Ru Jia, Jinzhong Lin, Minghua Ju, Jin Peng, Anbi Xu, Liman

30

Zhang

6

RNA-protein interactions in the core domain of spliceosomal U4 snRNP
Adelaine K.W. Leung, Jade Li, Kiyoshi Nagai

MS-5: Charge density studies- II -

31

AsCA’09

1

Content
Recent Progress in X-ray Charge Density Studies of Advanced Materials
Bo Brummerstedt Iversen

32

Non-linear Optical Properties and Spin Densities from X-ray Charge Density

232

Measurements
Dylan Jayatilaka, P. Munshi, M.J. Turner, J.A.K. Howard, M.A. Spackman

3

Exploring Halogen -Halogen Interactions via Charge Density Analysis
T. N. Guru Row

33

Challenge to Atomic Orbital Visualization by 0.2A Resolution Synchrotron

4

Radiation Single Crystal Experiment

34

Hiroshi Sawa, Eiji Nishibori, Shinobu Aoyagi

5

MEM Electrostatic Potential Imaging
Hiroshi Tanaka

34

Photo-induced structure determination and electron density study by MEM of

6

Spin Crossover complex [Fe(abpt)2(NCS)2]
Che Hsiu Shih, Chou Fu Sheu, Kunihisa Sugimoto, Jungeun Kim, Kenichi Kato, Yu Wang, Masaki

36

TakataMS-6: Advanced X-ray/neutron/electron imaging techniques
Recent Developments in Coherent Diffractive Imaging Instrumentation and1

36

Applications
Andrew G. Peele

Visualization of Bio-Structures Using Coherent X-Ray Diffraction

2

Yoshinori Nishino, Kazuhiro Maeshima, Naoko Imamoto, Ryuta Hirohata, Eiichiro Matsubara, Yukio

38

Takahashi, Tetsuya Ishikawa

3
4

Phase imaging using a liquid cell in a transmission x-ray microscope
Gung-Chian Yin

Improved Accuracy Laue Neutron Diffraction
Ross Piltz, Alison Edwards

39
39

Development and Application of Neutron 2D-Counter for Crystal and Magnetic

539

Structure Analysis
Y. Noda, C-H. Lee, M-K. Moon, S-A. Kim, Y. Ishikawa, H. Kimura , R. Kiyanagi

6

State-of-the-art Multilayer Optics for Modern X-ray Analytics
J. Wiesmann, T. Samtleben, C. Michaelsen, B. Hasse, J. Graf, F. Hertlein

40

MS-7: Membrane proteins
1

Structure and Mechanism of An Amino Acid Antiporter
Xiang Gao, Feiran Lu, Lijun Zhou, Jiawei Wang, and Yigong Shi

41

The structure of human connexin 26 gap junction channel

2

Shoji Maeda, So Nakagawa, Michihiro Suga, Eiki Yamashita, Atsunori Oshima, Yoshinori Fujiyoshi,

42

Tomitake Tsukihara

3

The role of AmtB-GlnK complex in nitrogen regulation
Xiaodan Li, Fritz Winkler, Mike Merrick

42

Structure and function of A-ATPase: combining electron microscopy and4

X-ray crystallography to study a transmembrane rotary motor complex
Lawrence K. Lee, Alastair G. Stewart, Mhairi Donohoe, Olga Esteban, Ricardo A. Bernal , Daniela
Stock- III -

43

AsCA’09

Content
Crystal Structure of Bacterial Nitric-oxide Reductase, a Key Enzyme in the

5

44

Respiratory Evolution
Yushi Matsumoto, Shingo Nagano, Yoshitsugu Shiro

MS-8: Organic crystal engineering and structure
1

Engineering Organic Crystals Using Arene- Perfluoroarene Interactions

44

Todd B. MarderProton Dynamics in Hydrogen-bonded Organic Solids from Protonic

2

45

Dielectrics to Proton-motor
Tadashi Sugawara, Kentaro Suzuki

3Structure–Property Correlations: Mechanical Properties of Molecular Crystals
C. Malla Reddy, Michael T. Kirchner, K. Anantha Padmanabhan, Gautam R. Desiraju

46

Polymorph and Pseudopolymorph of Co-crystal: Controlling Formation and

447Structural Transformation
Miao Du, Xiu-Juan Jiang, Min Tang

5

Towards knowledge-based design & control of pharmaceutical crystal forms
Colin R. Groom, Peter T. A. Galek, Peter A. Wood48

MS-9: Small angle scattering and soft materials crystallography
A small/wide-angle X-ray scattering instrument for structural characterizations
with soft matter, nanomaterials, and air-liquid interfaces

1

U-Ser Jeng, Chiu Hun Su, Chun-Jen Su, Kuei-Fen Liao, Wei-Tsung Chuang, Ying-Huang Lai, Je-Wei

49

Chang, Yi-Jiun Chen, Yu-Shan Huang, Ming-Tao Lee, Kuan-Li Yu, Din-Goa Liu, Zia-Fung Chang,
Chin-Yen Liu, Chien-Hung Chang, Keng S. Liang

2

Surface and flow induced ordering of complex fluids

49

W.A. Hamilton, L. Porcar, P.D. Butler, G.G. Warr

Intimate Relationship between Micro-phase Separation and Crystalline Phase

3

Transitions in Polyethylene- Poly(ethylene Oxide) Diblock Copolymer as
Viewed by Synchrotron SAXS/WAXD and IR/Raman Measurements

50

Kohji Tashiro, Weiyu Cao, Makoto Hanesaka, Hiroyasu Masunaga, Sono Sasaki , Masaki Takata

4

The Quokka Small Angle Neutron Scattering Instrument at OPAL
The

5

51

Richard F. Garrett, Elliot P. Gilbert, William A. Hamilton, Kathleen Woodeffectofinterfaceonthecrystallization

behaviorof

Poly(3-hydroxybutyrate) ultra-thin film revealed by grazing incident X-ray
dffraction

52

Xiaoli Sun, Harumi, Sato,Yukihiro Ozaki, Shouke Yan, Isao Takahashi

MS-10: New tools for macromolecular crystallography (including structural genomics)
Tracking ligand migration pathways in carbonmonoxy myoglobin at cryogenic

1

53

temperatures
Shin-ichi Adachi

Exploring the conformational energy landscape of acetylcholinesterase by2

kinetic crystallography
Jacques-Philippe Colletier, Benoît Sanson, Didier Fournier, Joel L. Sussman, Israel Silman,
Dominique Bourgeois, Martin Weik.

- IV -

53

AsCA’09

Content
Structure of HIV-1 protease in complex with inhibitor KNI-272 determined by

3

54

neutron crystallography
Motoyasu Adachi, Ryota Kuroki

45

Taking the edge off: The softer side of in-house SAD phasing

55

Joseph D. Ferrara, James W. Pflugrath, Cheng Yang

Reductive methylation of surface lysines assists crystallization of proteins
Neil Shaw, Chongyun Cheng, Zhi-Jie Liu

56

Improvement of a new rotation function for molecular replacement by

6

designing new scoring functions such as relative entropy and dynamic
correlation coefficient57

Fan Jiang, Wei Ding

7

New and Underused Methods for X-ray Crystallography at Low Resolution

58

Yong Xiong

MS-11: Metal-organic crystal engineering
Thermoelectric Zintl Compounds in R-T-Sb (R = Ca, Sr, Ba, Eu, Yb; T = Zn, Cd)

1

59

Systems
X.J. Wang, H. Zhang, M.B. Tang, X.X. Yang, H.H. Chen, Z.Y. Man, U. Burkhardt, Y.Grin, J.T. Zhao

Solid-state photochemical reactivity of coordination polymers and metal

260

complexes containing trans-1,2-bis(4-pyridyl)ethylene
Jagadese J. Vittal, Mangayarkarasi Nagarathinam, Abdul Malik Puthan Peedikakkal

3
4

Anatomy of a Void in an Aluminium-Copper-Tin Alloy

60

Laure Bourgeois, Matthew Weyland, Philip N.H. Nakashima, Barry C. Muddle

SMART X2S - Chemical Structures at the Touch of a Button

61

Eric Hovestreydt, Michael Ruf, Holger Ott

Rational Design, Synthesis and Properties of Layered Compounds LnOZnSb

5(Ln=La, Ce, Pr, Nd)
Kai Guo, Hao-Hong Chen, Zhen-Yong Man, Mei-Bo Tang, Xin-Xin Yang, Xiang-Xin Guo, Jing-Tai

62

Zhao

Cation⋅⋅⋅Cation Supramolecular Interactions in Zinc–Imidazole–Oxovanadate

663Compounds
Samroeng Krachodnok, Kenneth J. Haller, Ian D. Williams

Synthesis

7

and

X-ray

StructuresofDiorganotin

Complexeswith

Tris{(hydroxymethyl)aminomethane Schiff base64

See Mun Lee, Hapipah Mohd Ali and Kong Mun Lo

MS-12: Powder diffraction
1
2

Precise Structure Analysis of Ceramic Materials up to 1830 K
Masatomo Yashima

Zeolite Structure Analysis by Powder X-ray Data
Yingxia Wang, Jie Su, Jianhua Lin, Hermann Gies

64
66

Spinner-Scan Method for Evaluation of Particle Statistics in Powder

367

Diffractometry
Takashi Ida, Taishi Goto, Hisashi Hibino

4

Structural and magnetic properties of doped wide bandgap semiconductors
Gang Wang, Bo Song, Hui Li, Liangbao Jiang, Xiaolong Chen, Wenjun Wang, Wanyan Wang

-V-

68

AsCA’09

Content
Vanadium substituted potassium tungsten bronzes – its synthesis and569

characterization
A. M. Abdullah, A. Hussain

6

Charge Density study from high-resolution powder diffraction data

70

Eiji Nishibori, Shinobu Aoyagi, Hiroshi Sawa

Interplay between the crystalline and magnetic structures in lightly Cr-doped

771

Bi0.37Ca0.63Mn0.96Cr0.04O2.9
Wen-Hsien Li, Chun-Chuen Yang, Chun-Ming Wu, Jirong Sun, Jeffrey W. Lynn

MS-13: Hot structures
The structure of rat liver vault

1

Hideaki Tanaka,Koji Kato, Eiki Yamashita, Tomoyuki Sumizawa, Yong Zhou, Min Yao, Kenji

72

Iwasaki, Masato Yoshimura, Tomitake Tsukihara

Recognition of Nuclear Export Signal by CRM1

2

Xiuhua Dong, Anindita Biswas, Katherine Suel, Laurie Jackson, Hongmei Gu, Rita Martinez, Yuh

73

Min Chook

NEMO regulates NF-κB activation by specific recognition of linear ubiquitin
chains3

Simin Rahighi , Fumiyo Ikeda, Masato Kawasaki, Masato Akutsu, Nobuhiro Suzuki, Ryuichi Kato,
Tobias Kensche, Tamami Uejima, Stuart Bloor, David Komander, Felix Randow, Ivan Dikic,

73

Soichi

Wakatsuki

4

The atomic structure of granulovirus polyhedrin at 1.8Å resolution
Elaine Chiu, Shin-Mei Yeh, Richard Bunker, Clemens Schulze-Briese, Peter Metcalf

74

Crystal structure of human REV7 in complex with REV3 fragment

5

Kodai Hara, Toshiyuki Shimizu, Yoshiki Murakumo, Shunsuke Kobayashi, Toshiaki Kogame, Satoko
Akashi, Satoru Unzai, Tomo Hanafusa, Haruo Ohmori, Shunichi Takeda, Mamoru Sato, Hiroshi

74

HashimotoMS-14: Superconductivity and crystal properties
High-Pressure Synthesis and Superconducting Properties of Oxygen-deficient

1

Oxypnictide Superconductors LnFeAsO1-y
H. Eisaki, K. Miyazawa, M. Nakajima, S. Ishida, M. Ishikado, K. Kihou, P. M. Shirage, C. H. Lee, N.

75

Takeshita, R. Kumai, Y. Tomioka, H. Kito, K. M. Kojima, T. Ito, S. Shamoto, S. Uchida, A. Iyo

2

Diffraction study on the Fe-based high temperature superconductors
Wei Bao76

Electric Polarization Flop and Magnetic Phase Transition Induced by Magnetic

3

Field in Multiferroic RMn2O5 (R = Tm, Yb)
Hiroyuki Kimura, Yuma Sakamoto, Mamoru Fukunaga, Yukio Noda, Nobuyuki Abe, Kouji

76

Taniguchi, Taka-hisa Arima, Shuichi Wakimoto, Kazuhisa Kakurai

Effect of Ga3+ Substitution for Mn3+ on Magnetic and Dielectric Properties in

4

Multiferroic YMn2O5
Yuma Sakamoto, Hiroyuki Kimura, Satoru Horio, Arno Fey, Mamoru Fukunaga, Ryoji Kiyanagi,

77

Yukio Noda, Hiraka Haruhiro

MS-15: Electron microscopy and diffraction
1

Electron Microscopy of Low-Dimensional Nanomaterials
Fangfang Xu- VI -

78

AsCA’09

2

Content
3 Dimensional Coherent Electron Difractive Imaging of Nanoparticle

79

Fu-Rong Chen, Roman Dronyak, Keng S. Liang

High-resolution Structural Analysis of Membrane Proteins by Electron

380

Crystallography
Kaoru Mitsuoka

45Strain mapping near Si/SiGe interfaces using HOLZ line CBED patterns

82

Koh Saitoh, Maiko Hamabe, Nobuo Tanaka

Visualization of the orbital-ordered state of FeCr2O4 using the CBED method
Daisuke Morikawa, Kenji Tsuda, Shintaro Ohtani, Takahisa Arima

83

Poster Session
Rising Star
RS-1

Synthesis, structures and properties of modulated fresnoites
Structural

RS-2

85

Patryck K. K. Allen, Siegbert Schmid

and

Spin

Phase

Transitions

in

the

PolymericHybridOrganic-Inorganic Materials
Kittipong Chainok, Stuart R. Batten, Keith S. Murray, A. David Rae, Ian D. Williams, Kenneth J.

86

HallerRS-3

Charge Density Study on Metal Complexes with Non-Innocent Ligand
Yu-Chun Chuang, Chou-Fu Sheu, Gene-Hsiang Lee, Yu Wang

87

Topological features of short Cl…Cl contacts via experimental and theoretical

RS-4

87

charge density analysis
Venkatesha R. Hathwar, T. N. Guru Row

RS-5

Three-dimensional structures of Gram-positive bacterial pilins
Hae Joo Kang, Neil G. Paterson, Ton-That Hung, Edward N. Baker

88

Crystal Structure determination of a non-Pfam protein AF1514 by S-SAD using

RS-6

89

a Cr X-ray source
Yang Li, Neil Shaw,Gaojie Song,Chongyun Cheng ,Jie Yin, Zhi-Jie Liu

RS-7
RS-8
RS-9

New Water Clusters Hosted by Diamondoid MOFs
Mohammad Hedayetullah Mir, Jagadese J Vittal

Laser assisted deposition of AgInSe2 films on Si(100)Dinesh Pathak, R. K. Bedi, Davinder Kaur

New Structural Model of Malaria Pigment
Ratchadaporn Puntharod, Bayden R. Wood, Evan G. Robertson, Kenneth J. Haller

90
91
91

Structural insight into acute intermittent porphyria

RS-10

Gaojie Song, Yang Li, Chongyun Cheng, Yu Zhao, Ang Gao, Rongguang Zhang, Andrzej Joachimiak,92

Neil Shaw, Zhi-Jie Liu

Accurate measurements of anomalous dispersion effect shows there is nochloride ion between Fe and Cu ions in the reduction site of oxidized

RS-11

92

Cytochrome c Oxidase
Michihiro Suga, Kazumasa Muramoto, Eiki Yamashita, Masao Mochizuki, Kazunori Maeda, Kyoko
Ito-Shinzawa, Shinya Yoshikawa , Tomitake Tshukihara

Perakine Reductase, The First AKR Superfamily Member Involved In Indole

RS-12

Alkaloids Biosynthesis : Characterization, Crystallization And X-Ray Analysis
Lianli Sun, Meitian Wang, Santosh Panjikar, Joachim Stöckigt- VII -

93

AsCA’09

Content
3-D Structure and Enzymatic Mechanism of Polyneuridine Aldehyde Esterase:

RS-13

95

from C10- to C9- Skeleton in Ajmaline Biosynthesis
Liuqing Yang, Marco Hill, Meitian Wang, Santosh Panjikar, Joachim Stöckigt

Structural

RS-14

Basis

and

Catalytic

Mechanism

for

the

Dual

Functional

96

Endo-β-N-Acetylglucosaminidase A
Jie Yin, Lei Li, Neil Shaw, Yang Li, Lai-Xi Wang, Peng Wang, Zhi-Jie Liu

Structure Biology
P-1
P-2

Structural insights into the chemotactic pathway in Helicobacter pylori

97

Kwok Ho LAM, Thomas King Wah LING , Shannon Wing Ngor AU

Solid-liquid interface method (SLIM): A new crystallization method for proteins
Erik Brostromer, Jie Nan, Lan-Fen Li, Xiao-Dong Su

97Structural Basis for the Nucleotide-dependent Domain Rearrangement of

P-3

98

70-kDa Heat Shock Proteins
Yi-Wei Chang, Yuh-Ju Sun, Chung Wang, Chwan-Deng Hsiao

Complex structure of tarocystatin-papain and characterization of tarocystatin

P-4

98

proposed the role of C-terminal domain of group-2 phytocystatin
Ming-Hung Chu, Kai-Lun Liu, Kai-Wun Yeh, Yi-Sheng Cheng

P-5

Study on Structural Biology in Disease/structure- based Drug Design

99

Ki Joon Cho, Ji-Hye Lee, Intekhab Alam, Yi Ho Park, Kyung Hyun Kim

Crystal Structure of Carboxynorspermidine Decarboxylase from Helicobacter

P-6

99

pyloriChen-Hsi Chu, Chin-Yi Chen, Yuh-Ju Sun

Crystallographic Studies of Manihot esculenta hydroxynitrile lyase mutants

P-7

Charles B.C. Cielo, Mohammad Dadashipour, Tatsuo Hikage, Atsuo Suzuki, Tsunehiro Mizushima,

100

Hidenobu Komeda , Yasuhisa Asano , Takashi Yamane

P-8

The Effects of UV Irradiation of Protein Crystals
Excitation

P-9

101

Angela R. Criswell, Pierre LeMagueres, Bret Simpson

coupling

inbioluminescence:

combined

X-ray

and

NMR

101

determination of the clytin-GFP topology
Yingang Feng, Maxim Titushin，Yang Li，Jinfeng Wang, Eugene Vysotski，Zhi-Jie Liu

P-10
P-11

Structural study of FIH with CQ, HQ inhibitor complex
Sojung Han, Hyunjin Moon, Jungwoo Choe

Structure of Maleylacetate Reductase from Rhizobium sp. strain MTP-10005
Yasuo Hata, Tomomi Fujii, Masahiro Yoshida, Tadao Oikawa

Current

P-12

statusanddevelopments

of

102
102

macromolecular crystallography

beamlines at the Photon Factory
Masahiko Hiraki, Leonard Chavas, Yusuke Yamada, Naohiro Matsugaki, Noriyuki Igarashi and Soichi

104

Wakatsuki

A new beamline at SPring-8 dedicated to protein micro-crystallography

P-13

Kunio Hirata, Go Ueno, Atsushi Nisawa, Nobutaka Shimizu, Takashi Kumasaka, Yoshiaki Kawano,
Takaaki Hikima, Takashi Tanaka, Sunao Takahashi, Kunikazu Takeshita, Hirokatsu Yumoto,Haruhiko Ohashi, Shunji Goto, Hideo Kitamura, Toru Ohata, Yukito Furukawa, Masaki Yamamoto- VIII -105

AsCA’09

Content
Molecular Interplay Between Replicative Helicase DnaC and Its Loader DnaI

P-14

106

from Geobacillus kaustophilus
Chwan-Deng Hsiao, Kuang-Lei Tsai, Yu-Hua Lo, Yuh-Ju Sun

Crystal structure of CRN-4: implications for domain function in apoptotic DNA

P-15

106

degradation
Yu-Yuan Hsiao, Hanna S. Yuan

The Crystal Structures of 2-aminobenzothiazole- based Inhibitors in

P-16

Complexes with the Urokinase-type Plasminogen Activator
Longguang Jiang, Haiyang Yu, Cai Yuan, Jundong Wang, LiQing Chen , Edward J.Meehan, Zixiang

107

Huang, Mingdong Huang

Structural and biochemical characterization of yeast monothiol glutaredoxin

P-17

Grx6/YDL010W
Ming Luo, Yong-Liang Jiang, Xiao-Xiao Ma, Ya-Jun Tang, Yong-Xing He, Jiang Yu, Rong-Guang

108

Zhang, Yuxing Chen, Cong-Zhao Zhou

Structure and Interaction of Ubiquitin-Associated Domain of Human Fas

P-18

Associated Factor 1
Joon Kyu Park, JinSue Song, Jae-Jin Lee, Yun-Seok Choi, Kyoung-Seok Ryu, Jae-Hong Kim,

108

Kong-Joo Lee, Young-Ho Jeon, Eunice EunKyeong Kim

P-19

New design platform for malonyl-CoA-acyl carrier protein transacylase
Seung Kon Hong, Kook Han Kim, Eunice EunKyeong Kim

109

Structural Studies of Two PHP-like Tyrosine Phosphatases, CpsB from

P-20

Streptococcus pneumoniae and YwqE from Bacillus subtilis

109

Hyoun Sook Kim, Sang Jae Lee, Do Jin Kim, Hye-Jin Yoon, Soon-Jong Kim , Se Won Suh

Crystal structure and functional implications of the human Rad9-Hus1-Rad1

P-21

110

DNA damage checkpoint complex
Jin Seok Kim, Sun Young Sohn, Gwang Hyeon Gwon, Yunje Cho

Structural Basis for the Substrate Specificity and Reaction Mechanism of

P-22

111

Bacterial Aminopeptidase
Kyeong Kyu Kim, Minh Hai Ta, HyeJin Park, Sangho Lee

Structural study of Enhanced Intracellular Survival protein, Eis protein from

P-23

Mycobacterium tuberculosis
Kyoung Hoon Kim, Ji Young Yoon, Hyoun Sook Kim, Sang Jae Lee, Do Jin Kim, Hye-Jin Yoon, Se

111

Won Suh

P-24
P-25

Study on Structural biology in disease
Myung-Il Kim, Woo-Suk Jung, Sangkee Rhee

Structural insights into TDP-43, a new player in neurodegenerative diseases
Pan-Hsien Kuo, Lyudmila G. Doudeva, Yi-Ting Wang, Che-Kun James Shen, Hanna S. Yuan

112
113

Pushing low-resolution data to the limit - the structure of the third component

P-26

of the ligand binding site of the human insulin receptor

114

John G. Menting, Brian J. Smith, Colin W. Ward, Michael C. Lawrence

P-27

Crystal structures of aprotinin and its complexs
Ji-Hye Lee, In Seok Yang, Ki Joon Cho, Intekhab Alam, Yi Ho Park, Kyung Hyun Kim- IX -

115

AsCA’09

Content
Crystal Structure of the Glycosyltransferase Domain of Cholesterol-

P-28

α-Glycosyltransferase from Helicobacter pylori
Sang Jae Lee, Hyoun Sook Kim, Do Jin Kim, Kyoung Hoon Kim, Ji Young Yoon, Jun Young Jang,

115

Hye-Jin Yoon, Se Won Suh

A Novel 'in situ' Inhibitor Elongation Strategy Produces a Stable Covalent

P-29

116

Intermediate With Human Pancreatic Alpha-Amylase
Chunmin Li, Ran Zhang, Leslie K. Williams, Brian P. Rempel, Stephen G. Withers, Gary D. Brayer

Crystallization

P-30

and

preliminary

X-ray

crystallographic

studiesof117

O-methyltransferase from the Anabaena Pcc 7120
Guoming Li, Zhenting Tang, Geng Meng, Kesheng Dai, Jindong Zhao, Xiaofeng Zheng

P-31

Crystallographic study of NQO2 and structure-based ligand design

117

Yazhuo Li, Cristina de Matteis

Insights into the Alkyl Peroxide Reduction Pathway of Xanthomonas

P-32

campestris

Bacterioferritin

Comigratory

ProteinfromTrappedIntermediate/Ligand Complex Structures

118

Shu-Ju Liao, Chao-Yu Yang, Ko-Hsin Chin, Andrew H.-J. Wang, Shan-Ho Chou

Crystal Structure of the Cytoplasmic Domain of the Type II Secretion System

P-33

Component EpsL of Vibrio parahaemolyticus

119

Li-Ying Lin, Nien-Tai Hu, Nei-Li Chan

Crystal Optimization of a Secondary Transporter Membrane Protein to 4.5 Å

P-34

119

Resolution
Xiangyu Liu, Pontus Gourdon, Xiaodong Su, Poul Nissen

The crystal structure of a replicative hexameric helicase DnaC and its complex

P-35

121

with single-stranded DNA
Yu-Hua Lo, Kuang-Lei Tsai, Yuh-Ju Sun, Wei-Ti Chen, Cheng-Yang Huang, Chwan-Deng Hsiao

Structures of yeast glutathione S-transferase Gtt2 reveal a new catalytic type

P-36

121

of GST family
Xiao-Xiao Ma, Yong-Liang Jiang, Yong-Xing He, Rui Bao, Yuxing Chen and Cong-Zhao Zhou

Fragment-based screening by X-ray crystallography: discovery of novel

P-37

inhibitors targeting the adrenaline-synthesising enzyme

122

Jennifer L Martin, Nyssa Drinkwater, Gary Grunewald, Michael McLeish

Crystal structure of PACSIN 1 F-BAR domain reveals a novel membrane

P-38

123

curvature sensing mechanism
Geng Meng, Xiaoyun Bai, Guoming Li, Yong Liu, Ming Luo, Xiaofeng Zheng

Stabilization mechanism by Hyp-Thr-Gly sequence in collagen-helix

P-39

Keita Miyama, Tatsuya Morimoto, Koichi Masakiyo, Tatsuya Kawaguchi, Kenji Okuyama, Kazunori

123

Mizuno, Hans Peter Bächinger

Protein Function Annotation from Sequences and Structures with Tools at

P-40

125

PDBj
Daron M. Standley, Mieszko Lis, Akira R. Kinjo, Haruki Nakamura

Structural insights into a pyridoxal 5’-phosphate- dependent fold-type Ⅰ

P-41

racemase, a-amino-e- caprolactam racemase from Achromobacter obae
Seiji Okazaki, Atsuo Suzuki, Koji Suzuki, Hidenobu Komeda, Yasuhisa Asano, Takashi Yamane

-X-

126

AsCA’09

Content
Fluorescence-Based Screening for Soluble Human Proteins by POET in

P-42

Baculovirus-infected Insect Cells for Structural Studies

126

Songying Ouyang, Zhijie Liu

Crystal Structure of the Periplasmic Region of MacB, a Noncanonic ABC

P-43

Transporter
Sun-Hee Park, Yongbin Xu, Se-Hoon Sim, Ki Hyun Nam, Xiao Ling Jin, Hong-Man Kim, Kwang

127

Yeon Hwang, Kangseok Lee, Nam-Chul Ha

Structure of an eIF4A - PDCD4 complex provides insight into the inhibition of

P-44

128

translation
Young Bong Park, Jihye Lee, Jeong Ho Chang , Yunje Cho

Crystal Structure of Bacterial Lysozyme Inhibitor MliC, Complexed with c-type

P-45

128

Lysozyme.
Shunfu Piao, Soohwan Yum and Nam-Chul Ha

P-46

Structural Basis of Transport of Lysophospholipids by Human Serum Albumin
Shihui Guo, Xiaoli Shi, Mingdong Huang

129

Inactivation of Nucleoside Diphosphate Kinase-A through a Conformational

P-47

Change of the C-terminal Loop Induced by Oxidation

129

Mi-Sun Kim, Dong-Hae Shi

Crystal Structure of Stenotrophomonas maltophilia FeoA complexed with

P-48

Zinc: A Unique Procaryotic SH3 Domain-like Protein Possibly Acts as a
Bacterial Ferrous Iron Transport Activating Factor

130

Yi-Che Su, Ko-Hsin Chin, Andrew H.-J. Wang, Shan-Ho Chou

Single-stranded DNA-binding protein complex from Helicobacter pylori

P-49

suggests an ssDNA-binding surface

131

Yuh-Ju Sun and Kun-Wei Chan

A novel pharmaceutical protein, crystal structures of an anti-HIV actinohivin

P-50

from an actinomycete, and its complex with mannobiose
Masaru Tsunoda, Kaoru Suzuki, Tsubasa Sagara, Atsushi Takahashi, Junji Inokoshi, Satoshi Omura,131

Takeshi Sekiguchi, Haruo Tanaka, Akio TakénakaThe SARS-unique domain of SARS-CoV contains two macrodomains that bind

P-51

G-quadruplexes
Jinzhi Tan, Clemens Vonrhein, Oliver S. Smart, Gerard Bricogne, Michela Bollati, Yuri Kusov, Guido

132

Hansen, Jeroen R. Mesters, Christian L. Schmidt, Rolf Hilgenfeld

P-52

A crystallographic study of Tic110C protein from Cyanidioschyzon merolae
Jia-Yin Tsai, Chwan-Den Hsiao

133

Crystal structure of the human FOXO3a-DBD/DNA complex suggests the

P-53

effects of post-translational modification
Kuang-Lei Tsai, Yuh-Ju Sun, Cheng-Yang Huang, Jer-Yen Yang, Mien-Chie Hung, Chwan-Deng

134

Hsiao

Novel crystal structure of Helicobacter pylori neutrophil-activating protein

P-54

134

(HP-NAP)
Osamu Tsuruta, Naoya Akao, Hideshi Yokoyama, Satoshi Fujii

P-55

Structural and function researches on human glutathione transferase kappa
Bing Wang, Yingjie Peng, Jianping Ding

- XI -

136

AsCA’09

Content
HCV Membrane Protein Purification, Characterization and Crystallization

P-56

Liping Wang, Randy Bledsoe, William Burkhart, Annie Hassell, Robert Reid, Derek Parks, Warren

136

Rocque, Michael Thomson, Shawn Williams

An Intramolecular Self-Activation Mechanism of Human Caspase-6

P-57

Xiao-Jun Wang, Xiang Liu, Kai-Tuo Wang, Wei Mi, Yan Zhang, Lan-Fen Li, Andrea C. LeBlanc,

137

Xiao-Dong Su

Redesign of a non-specific endonuclease to yield better DNA-binding activity

P-58

and altered DNA sequence cleavage preference137

Yi-Ting Wang, Jon D. Wright, Lyudmila G. Doudeva, Hua-Ci Jhang, Carmay Lim, Hanna S. Yuan

P-59
P-60

Trapping of Silica Nanoparticles at the Air-Water Interface by Proteins
Joo Chuan Ang, Jhih-Min Lin, Peter N. Yaron and John W. White

Crystal structure of Helicobacter pylori urease accessory protein ureF
Yu Hang Fong, Yu Wai Chen, Kam Bo Wong

138
139

Structural and function researches on two α-isopropylmalate synthases from

P-61

Leptospira biflexa, key enzymes in leucine biosynthesis

139

Jian Wu, Zilong Zhang, Wei Lin, Jun Ma, Peng Zhang, Guoping Zhao, Jianping Ding

Structural basis for a Reciprocating Mechanism of Negative Cooperativity in

P-62

Dimeric Phosphagen kinase Activity

140

Xiaoai Wu, Sheng Ye, Shuyuan Guo, Wupeng Yan, Mark Bartlam, Zihe Rao

Structural and Kinetic Analysis of Raucaffricine Glucosidase (RG) from the

P-63

141

Medicinal Plant Rauvolfia
Liqun Xia, Martin Ruppert, Meitian Wang, Santosh Panjikar, Joachim Stöckigt

Structure and Functional Implications of the Human Rad9-Hus1-Rad1 Cell

P-64

142

Cycle Checkpoint Complex
Min Xu, Lin Bai, Yong Gong, Wei Xie, Haiying Hang, Tao Jiang

In situ proteolysis doubles the success rate in protein crystallization andP-65

structure determination
Xiaohui Xu, Aiping Dong, Hong Cui, Tatiana Skarina, Elena Evdokimova, Aled Edwards, Andrzej

143

Joachimiak, Alexei Savchenko

P-66

A functional Assembly of a Tripartite acrolide-specific Efflux Pump
Yongbin Xu, Hong-Man Kim, Kangseok Lee, Nam-Chul Ha.

144

Homology Modeling of apo-CDK5 and Insights into Structure-Based Inhibitor

P-67

144

DesignKosaraju Vamsi Krishna, Seow Yi Lim, Feng Xue

Xanthomonas campestris PqqD in the Pyrroloquinoline Quinone Biosynthesis

P-68

Operon Adopts a Novel Saddle-Like Fold That Possibly Serves as a PQQ
Carrier

145

Chao-Yu Yang, Tung-Yi Tsai, Andrew H.-J. Wang, Shan-Ho Chou

Dual functions of an exosome component protein Rrp46/CRN-5 in RNA

P-69

degradation and DNA fragmentation

146

Che-Chuan Yang, Yi-Ting Wang, Yu-Yuan Hsiao, Lyudmila G. Doudeva, Hanna S. Yuan

Preliminary X-ray analysis of human Frk kinase domain

P-70

Xiaoyan Yang, Takayoshi Kinoshita, Nao Miyano, Tetsuko Nakaniwa, Koichi Yokota, Masaki Gouda,
Toshiji Tada

- XII -

147

AsCA’09

Content
Crystal structures of human BTG2 and mouse TIS21 involved in suppression

P-71

of CAF1 deadenylase activity.
Xiuna Yang, Masahiro Morita, Hui Wang, Toru Suzuki, Wen Yang, Yunhai Luo, Cong Zhao, Yue Yu,

147

Mark Bartlam, Tadashi Yamamoto, Zihe Rao

Crystal Structure of YqeH, a Circularly Permuted GTPase

P-72

Ji Young Yoon, Hye-Jin Yoon, Hyoun Sook Kim, Kyoung Hoon Kim, Do Jin Kim, Sang Jae Lee, Jun

148

Young Jang, Se Won Suh

Structure and function study of the DUF55 domain of human thymocyte

P-73

nuclear protein 1 and structure determination method study of twinningcrystals

149

Feng Yu, Aixin Song, Chunyan Xu, Lihua Sun, Jian Li, Lin Tang, Hongyu Hu, Jianhua He

P-74

Structure of Catalytic Domain of Matriptase in Complex with SFTI-1
Cai Yuan, Longguang Jiang, Liqing Chen, Mingdong Huang

149

Crystallization and preliminary X-ray crystallographic analysis of Escherichia

P-75

150

coli CusB
Bo-Young Yun, Yongbin Xu and Nam-Chul Ha

Crystallization and preliminary crystallographic analysis of a ribokinase from

P-76

150

Staphylococcus aureus
Lin Wang, Haipeng Wang, Jianbin Ruan, Changlin Tian, Baolin Sun, Jianye Zang

Nucleoside Monophosphate Complex Structures of the Endonuclease Domainfrom the Influenza Polymerase PA Subunit Reveal the Substrate Binding Site

P-77

151

inside the Catalytic Center
Cong Zhao, Zhiyong Lou, Yu Guo, Ming Ma, Yutao Chen, Shuaiyi Liang, Liang Zhang, Shoudeng
Chen, Xuemei Li, Yingfang Liu, Mark Bartlam, Zihe Rao

From peptidic inhibitor leads to non-peptidic drugs: Making use of the

P-78

reversible binding of peptide aldehydes to cysteine proteases in Dynamic
Ligation Screening

152

Lili Zhu, Jinzhi Tan, Marco F. Schmidt, Jörg Rademann, Rolf Hilgenfeld

Molecular ChemistryCo-crystallization of Valproic acid by Co-grinding and Structure Determination

P-79

154

from Powder Diffraction Data
Masahide Aoki, Hidehiro Uekusa, Hiroyuki Kurobe, Etsuo Yonemochi, Katsuhide Terada

The Design of New Bicyclo[3.3.0]octane Lattice Inclusion Hosts and Cocrystal

P-80

155

Partner Molecules
Roger Bishop, Mohan M. Bhadbhade, Isa Y. H. Chan

Zintl

P-81

Phase

Compounds

Yb1-xCaxCd2Sb2 With

TunableThermoelectric

Properties Induced by Cation Substitution
Qigao Cao, Hui Zhang, Meibo Tang, Haohong Chen, Xinxin Yang, Xiangxin Guo, Jingtai Zhao, Grin

156

Yuri

P-82
P-83

Molecular self-assembly – tweezers, forks, and boxes
Christine Cardin, Yu Gan, Zhixue Zhu , Howard Colquhoun

Metal Organic Frameworks from 3,3’-Biphenic Acid
Chun-Lung Choi, Herman H-Y. Sung, M. Gerry J. Lesley, Ian D. Williams- XIII -156
157

AsCA’09

Content
On the quality of data necessary for performing 2nd & 4th moment method of

P-84

evaluating crystallite size & dislocation density

158

Prabal Dasgupta, Bholanath Mondal

Crystal structure of organic compound ethyl-2- amino-5-bromothiazole-

P-85

158

4-carboxylate
K.V.Arjuna Gowda, Ramakrishna Gowda, I.A.Khazi

Local Structure Analysis of an Automobile Catalyst La1.02Fe0.95Pd0.05O3 by Pd

P-86

K-edge XAFSShoshi Higuchi, Daiju Matsumura, Yasuo Nishihata, Jun’iciro Mizuki, Hikaru Terauchi, Isao

159

Takahashi, Masashi Taniguchi, Mari Uenishi, Hirohisa Tanaka, Kimiyoshi Kaneko

Regulation of Anthracene Arrangement and Photoluminescence Properties by

P-87

160

Using Organic Salts
Tomoaki Hinoue, Norimitsu Tohnai, Ichiro Hisaki, Mikiji Miyata

P-88
P-89

X-ray structural study of intercalation compounds BixTiS2
Sho Ikeda , Takuro Kawasaki , Ken-ichi Ohshima

Crystal Structure of Tetracaine Hydrochloride Polymorphs
Sayaka Ina, Hidehiro Uekusa, Naoko Itoda, Etsuo Yonemochi, Katsuhide Terada

161
161

High Resolution X-ray Diffraction Analysis on (Lu2.1,Bi0.9)Fe5O12 Layers Grown

P-90

162

on Gd3Ga5O12 Substrate
Hong Ji , Huaiwu Zhang , Qiye Wen

P-91

Study on Synthesis and Luminescence Properties of LuBO3:Ce3+
Teng-Teng Jin, Jing-Tai Zhao , Hao-Hong Chen, Xin-Xin Yang

163

Structure refinement and electron density distribution of trehalose dihydrate

P-92

164

and anhydarate
Kunimitsu Kataoka, Shota Hasegawa, Takumi Tajima, Takuro Kawasaki , Ken-ichi Ohshima

P-93
P-94

A single-crystal study of hollandite-type BaxTi8O16 and hexagonal BaTiO3-x
Kunimitsu Kataoka, Norihito Kijima, Hiroshi Hayakawa, Junji Akimoto, Ken-ichi Ohshima

Ordered Arrangements of Nb Atoms in Layered Compounds NbxTiS2
Takuro Kawasaki, Yuki Azuma, Ken-ichi Ohshima

165
166

Structure Analysis of CaMoO4 using Energy-filtered Precession Electron

P-95

167

Diffraction
Jin-Gyu Kim, Sung-Woo Lee, Kyung Song, Youn-Joong Kim

Intermolecular interactions in two halogenated Imidazo [2,1-b] [1,3,4]

P-96

168

thiadiazole derivatives
M K Kokila, G N AnilKumar, Puttaraja, S. S. Karki, R. Vinayakumar, S. Kumar

Crystal and molecular structure of 2-amino-N- (2-furylmethyl) -5,6-dihydro-

P-97

4H-cyclopenta[b] thiophene-3-carboxamide’
M K Kokila,

169

K. Chandra Kumar, Puttaraja, S. Mohan ,J. Saravanan

Structures of bioactive compounds: substituted,3,2 –benzoxazaphosphinine

P-98

169

derivatives
Krishnaiah . M , Surendra Babu .V.H.H, Vedavathi G.Puranik

Critical evolution of surface morphology of Quartz (001) surface on

P-99

alpha-incommensurate-beta structural phase transitions
Tsuyoshi Kumagai, Chibon Hyon, Yoshiki Ueno, Hikaru Terauchi and Isao Takahashi- XIV -

170

AsCA’09

Content
Synchrotron radiation X-ray characterization of epitaxial magnetic multilayers

P-100

of yttrium iron garnet/gadolinium gallium garnet

171

Chih-Hao Lee, K.S. Laing, M.Y. Chern

P-101
P-102

Study on Simulation and Preparation of Spherical Diamond Film
Duosheng Li, Xianliang Zhou, Dunwen Zuo, Xiaozhen Hua

The Topological Analysis of Minerals
Li Jia-Ju, Li Hui

172
173

XC6012 from Xanthomonas campestris Adopts a Novel Tetrameric PilZ

P-103

Domain Structure Stabilized by a Central Parallel Four-Stranded Coiled-Coil

174

Tso-Ning Li, Ko-Hsin Chin, Andrew H.-J. Wang, Shan-Ho ChouP-104

New palladium-containing skutterudites BaPd4SnxSb12-x
Ying Liang, Horst Borrmann, Walter Schnelle, Jing-Tai Zhao , Yuri Grin

175

Preparation and Characterization of Ammonium Polyphosphate with Crystal

P-105

176

Form-V
Xinchun Liu, Wenyan Chen, Gousheng Liu

Acid-base approach to Valproic acid co-crystal and the crystal structure

P-106

177

analysis
Takashi Miyamoto, Akiko Sekine, Hidehiro Uekusa, Etsuo Yonemochi, Katsuhide Terada

Hydrogen-bonded Network in Quaternary Ammonium Salts Used as Charge

P-107

178

Control AgentsJin Mizuguchi, Kazuya Uta, Yohei Sato, Osamu Yamate

Suppression of Pseudo-polymorphs by High Temperature Crystallization:

P-108

179

Case Study of Oleanic Acid.
Thanh-ha Nguyen, Alvin W-H. Siu,Herman H-Y. Sung, Henry H-Y. Tong, Ian D. Williams

P-109

Measurement using multiple diffraction with four-circle diffractometer
Koji Okada, Kiyoaki Tanaka, Yasuyuki Takenaka, Isao Kagomiya

179

Electronic spectra of the 1:1 rhodamine B base with ethyl gallate in solution

P-110

180

and in the solid state
Kazuyuki Sato, Hideki Shima, Jin Mizuguchi

P-111

Crystal Structures and Photochromism of Indandione derivatives
Akiko Sekine, Yuji Karakane, Hidehiro Uekusa, Masashi Yokoyama, Yuki Nakai, Koichi Tanaka

181

Structural and Functional Analysis of Nup120 Suggests Ring Formation of the

P-112

Nup84 Complex
Hyuk-Soo Seo, Yingli Ma, Erik W. Debler, Daniel Wacker, Stephan Kutik, Günter Blobel, André

182

Hoelz

P-113
P-114

Gas Pores Formation in Laser Induced Ti Melts for Implant Prototyping
A. A. Shaikh, S. Dudziak, O. Meier , T. M. Gesing

A Study of Tantalum Substituted Potassium Tungsten Bronzes
Md. Mahbubur Rahman Shakil, Altaf Hussain

183
183

Stability and tinctorial strength of black leuco-colorants as viewed from the

P-115

crystal structure of a phenolic developer
Hideki Shima, Kazuyuki Sato, and Jin Mizuguchi- XV -

184

AsCA’09

Content
Crystallographic statistical studies of the decavanadate anion: toward aP-116

prediction of the non-covalent interactions

185

Anne Spasojević – de Biré , Nada Bosnjaković-Pavlović,

Non Photochemical Light Induced Nucleation. A tool to crystallize polymorphs

P-117

on demand ? Application to carbamazepine.

186

David Miret, Janice Aber, Bruce Garetz, Philippe Scouflaire, Anne Spasojević – de Biré

Investigation of Lattice dynamics and Anharmonicity of Raman modes in

P-118

187

BaWO4 crystal
J. Suda, P. G. Zverev, O. Kamishima, J. Kawamura , T.Hattori

P-119

Absolute Structure Determination of Organic Compounds: an Update

Herman H-Y. Sung, Thanh-ha Nguyen, Zoltan Gal, Ian D. Williams

188

Crystal structure and phase transition of a lead-based inorganic-organic

P-120

188

perovskite (C5H10NH2) PbBr3
Kota Takano , Munehiko Nakatsuma , Miwako Takahashi , Ken-ichi Ohshima

P-121

Super accurate structure factor measurement ad PF14A
Kiyoaki Tanaka, Yasuyuki Takenaka, Terutoshi Sakakura, Shirou Fanahashi, Koji Okada

189

Surface Morphology and Crystallinity of Poly(hydroxybutyrate)/Poly(L-lactic

P-122

190

acid) Blends
Akihisa Tokuda, Takashi Asano, Yusuke Oji, Yukihiro Ozaki, Hikaru Terauchi, and Isao Takahashi

Status Report on Super High Resolution Powder Diffractometer at J-PARC

P-123

Shuki Torii, Takashi Kamiyama, Takashi Muroya, Setsuo Sato, Hidenori Sagehashi, Ryoko Oishi,
Takahiro Morishima, Teguh Panca Putra, Junrong Zhang, Kenji Iwase, Masao Yonemura, Akinori

191

Hoshikawa, Toru Ishigaki, Susumu Ikeda

Crystal Structure Comparisons of Tetrakis(4-hydroxyphenyl)alkane Inclusion

P-124

192

Crystals
Kazuyuki Toyota, Hidehiro Uekusa, Natsuki Amanokura, Masami Kaneko, Hiroshi Suzuki

Pharmaceutical Polymorphs and their Phase Transitions Investigated by Ab

P-125

Initio Structure Determination from Powder Diffraction Data

193

Hidehiro Uekusa, Etsuo Yonemochi, Katsuhide Terada

Molecular ordering and orientation in surface region of natural cocoa butter

P-126

and its constituent oils, POP, SOS and POS revealed by X-ray Diffraction

194

Yoshihito Uozaki, Kimihiko Nozaki, Mai Uenaka, Hikaru Terauchi and Isao Takahashi

INTER MOLECULAR INTERACTIONS IN 2 AMINO AND SCHIFF BASES OF

P-127

195

THIOPHENES
Vasu Sriranga , Deepak Chopra

Organo-chelated Borates as Anions for Crystallization and Chiral Resolution

P-128

Lawrence W-Y. Wong, Jack W-H.Kan, Pokka K-C. Pang, Alex S-F. Au Yeung, Thanh-ha Nguyen,

195

Herman H-Y. Sung, Ian D. Williams

P-129

A Unique Approach to Precisely Dispense Chemicals with Diverse Properties
Jian Xu , Matthew Lundy

196

Reversible Transformation and Fluorescent Properties in Polymorphic

P-130

Crystals of n-Butylammonium 2-Naphthalenesulfonate
Atsushi Yamamoto, Masaaki Matsumoto, Tomoaki Hinoue, Yuji Mizobe, Ichiro Hisaki, Mikiji
Miyata, Norimitsu Tohnai- XVI -

197

AsCA’09

Content
NaVO2(IO3)2(H2O): A New 1D Vanadyl Iodate With Very Strong Second

P-131

198

Harmonic Generation
Bing-Ping Yang, Jiang-Gao Mao

P-132

Critical narrowing of glass transition in supported ultrathin polystyrene films
Chunming Yang, Naoki Koyasu, Kohei Ishimoto, Hikaru Terauchi, Isao Takahashi

Zeolitic

P-133

Imidazolate

Framework(ZIF)

Compounds

using

199

Asymmetric200

Imidazoles
Fion T-Y. Yeong, Fanny L-Y. Shek, Herman H-Y. Sung, Ian D. Williams

Modulated structure feature in over-doped manganese oxides

P-134

Xiuzhen Yu, YasuhideTomioka, Yoshio Kaneko, Toru Asaka, Koji Kimoto, Taka-hisa Arima,

201

Yoshinori Tokura, Yoshio Matsui

Structural Studies of Ba2LaIrO6 and La2ZnIrO6 – Two Monoclinic Perovskites

P-135

202

With Different Space Groups
Qingdi Zhou, Brendan J. Kennedy

Specialized Techniques
SMART BREEZE - The affordable high-quality solution for Chemical

P-136

204

Crystallography
Eric Hovestreydt, Michael Ruf, Holger Ott

P-137

Ready, set, screen: X8 PROSPECTOR
Eric Hovestreydt, Matt Benning, Marianna Biadene

204

Focusing Effects in Parabolic Shaped Multi-Plate Crystal Cavity for X-rays

P-138

Y.-Y. Chang, S.-Y. Chen, M.-T. Tang, Yu. Stetsko, M. Yabashi, S.-C. Weng, C.-H. Chu, B.-Y. Shew,

205

S.-L. Chang

P-139
P-140

Bringing the power of synchrotron crystallography to the chemical community
William Clegg, Ross W Harrington, Luca Russo

Optimization of parameters for new rotation function
Wei Ding, FanJiang

206
206

The current status of versatile neutron diffractometer iMATERIA at J-PARC

P-141

Toru Ishigaki, Akinori Hoshikawa, Masao Yonemura, Kenji Iwase, D. S. Adipranoto, Hidetoshi
Oguro, Takahiro Morishima, Takashi Kamiyama, Ryoko Oishi, Kazuhiro Mori, Ryoji Kiyanagi,

207

Kazuya Aizawa, Makoto Hayashi

P-142
P-143

Study on membrane chain-chain packing by grazing incident X-ray diffraction
Ming-Tao Lee

Imposition of multiple F constraints in the maximum entropy method
Koichi Momma, Fujio Izumi

208
208

Synchrotron Radiation Beamline for Macromolecular Assemblies Operated by
the IPR at SPring-8 (BL44XU)

P-144

Eiki yamashita, Masato Yoshimura, Mamoru Suzuki, Kazuya Hasegawa, Yukito Furukawa, Toru

210

Ohata, Takashi Kumasaka, Go Ueno, Masaki Yamamoto, Shinya Yoshikawa, Tomitake Tsukihara,
Atsushi Nakagawa

P-145

X-ray diffraction from crystals in crystallization plates.
Tadeusz Skarzynski- XVII -211

AsCA’09

Content
Electrostatic potential as an experimental or a theoretical tool for a better

P-146

understanding of drug interactions

211

Anne Spasojević – de Biré, Nour Eddine Ghermani

The Effect of Disk Chopper Phasing on Neutron Beam Spectrum of

P-147

SuperHRPD at J-PARC
Teguh Yulius Surya Panca Putra, Shuki Torii, Junrong Zhang, Takashi Muroya, Setsuo Sato, Takashi

212

Kamiyama

A Novel Mounting Tool Using Adhesive for Protein Crystals

P-148

Tomoya Kitatani, Tomokazu Hasegawa, Shigeru Sugiyama, Kensaku Hamada, Hiroaki Adachi,

213

Hiroyoshi Matsumura, Satoshi Murakami, Tsuyoshi Inoue, Yusuke Mori, Kazufumi Takano

P-149

New Possibilities for X-ray Diffractometry: Brighten Up Your Home-Lab
J. Wiesmann T. Samtleben , B. Hasse, J. Graf, C. Michaelsen

214

Desktop Minstrel UV™: A Novel Protein Crystal Monitoring Automation

P-150

System Using UV Fluorescence Microscopy

215

Jian Xu, Craig Sterling and Michael Willis

P-151

SAXS/WAXS Experiments with a Single Detector
Naoto YAGI , Noboru OHTA

215

Fully automated data collection system at macromolecular crystallography

P-152

beamlines in the Photon Factory
Yusuke Yamada, Naohiro Matsugaki, Masahiko Hiraki, Leonard M.G. Chavas, Noriyuki Igarashi,

216

Soichi Wakatsuki

Development of a New Rietveld Code as Powder Diffraction Analysis Suite,
Z-CodeP-153

Masao Yonemura, Takahiro Morishima, Ryoko Oishi, Dyah Sulistyanintyas, Hidetoshi Oguro, Kenji

218

Iwase, Akinori Hoshikawa, Toru Ishigaki, Kazuhiro Mori, Ryoji Kiyanagi, Junrog Zhang, Teguh
Panca, Shuki Torii, Takashi Kamiyama

Study of Time Rebinning for Super High Resolution TOF Neutron Diffraction

P-154

Junrong Zhang, Shuki Torii, Teguh Panca Putra, Takashi Muroya, Takahiro Morishima, Ryoko Oishi,

219

Takashi Kamiyama

OthersEchidna High-Resolution Neutron Powder Diffractometer at OPAL: one year of

P-155

221

experience and experiments
Maxim Avdeev, James Hester

WebCSD – on-line access to the Cambridge Structural Database andP-156

applications in chemical education

221

Gary M. Battle

Enhancing Stability of Enzymes through Modulation of Inter-domain

P-157

222

Interactions: A Case Study
Debi Choudhury, Sumana Roy, Sampa Biswas and J. K. Dattagupta

P-158
P-159

Wide-Angle incidence Waveguides Using X-Ray Diffraction
S.-L. Chang , C.-J. Huang, L.-S. Cai, H.-Y. Chen, C.-H. Chu, M.-T. Tang, Yu. P. Stetsko, B.-Y. Shew

Study on Structural Biology

223
223

Ko-Hsin Chin , Shan-Ho Chou- XVIII -AsCA’09

Content
The Structural analysis of the FAS1 domain 4 of βig-h3 for relationship with

P-160

224

corneal dystrophy
Jiho Yoo, Jongsoo Jeon, Kuglae Kim, Eugkweon Kim, Jongsun Kim, Hyun-Soo Cho

Structural analysis of a prokaryotic Kir channel captured in multiple

P-161

224

conformations
Oliver B. Clarke, Alessandro T. Caputo, Brian J. Smith, Jacqueline M. Gulbis

Crystallization and Preliminary X-ray analysis of PNP 4-mono-oxygenase from

P-162

225

Pseudomonas putida DLL-E4
Zhongli Cui, Weidong Liu , Wenjing Shen

How to interpret the quarterly charged [Ni(dmit)2]-1/4? ⎯ Structure and

P-163

electrical conductivity of (n-Bu4N)[Ni(dmit)2]4MeCN

226

Qi Fang, Wen-Tao Yu, Chun-Li Guo, Wei Xu

The structure of the ribosome with elongation factor G trapped in the

P-164

post-translocational state
Yong-Gui Gao, Maria Selmer, Christine M. Dunham, Albert Weixlbaumer, Ann C. Kelley , V.

227

Ramakrishnan

P-165

Growth and Characterization of α and γ-glycine single crystals
T.P.Srinivasan, S.Anandhi, R.Gopalakrishnan

228

Unusual arrangement of EF hand motifs in Calcium binding protein-1 of

P-166

Entameoba histolytica and its functional implications.

230

Shivesh Kumar, Ruchi Jain, S. Gourinath

P-167
P-168

Crystal structure of human Bfl-1 in complex with BAK BH3 peptide
Rongjin Guan, Rong Xiao, Li Zhao, Eileen White, Celine Gelinas, Guy Montelione

Secondary Extinction and Diffraction Behaviors in Single Crystals
Hua-Chen Hu

230
231

The Development of A “Unified” Microfluidic Technology for Protein

P-169

232

Crystallization
Jiang Huang

ProSeed: A General Method to Introduce Beneficial Nuclei to Promote Protein

P-170

233

Crystallization
Jeff E. Habel, Liwei Hung

P-171

Automated Ligand Identification in PHENIX
Liwei Hung, Thomas C. Terwilliger

233

Crystal Structure of the TNF-α Inducing Protein (Tipα) from Helicobacter

P-172

pylori: Insights into its DNA Binding Activity
Jun Young Jang, Hye-Jin Yoon, Ji Young Yoon, Hyoun Sook Kim, Sang Jae Lee, Kyoung Hoon Kim,

234

Do Jin Kim, Se Won Suh

Determination of structural and magnetic phase diagram of solid solution of

P-173

234

BiFeO3-BaTiO3 system
Ryoji Kiyanagi, Tadashi Yamazaki, Yuma Sakamoto, Hiroyuki Kimura, Yukio Noda, Kenji Ohoyama

P-174

Development of laboratory SAXS spectrometer
Seok-Gn Ryu, Chang-Hee Lee, Myungkook Moon, Jongkyu Cheon, Hyun Hoon Song,Woon Bo Shim

- XIX -

235

AsCA’09

Content
Coordination Polymers of N-(7-hydroxy-4-methyl-8-coumarinyl)-amino acids:

P-175

236

Fabrication of Crystalline, Gel and Fiber Materials
Wei Lee Leong, Jagadese J. Vittal

P-176

RainbowMEM: A New Maximum Entropy Analysis Package

237

Hui LI, Jiaju LI, Xiaolong CHEN , Ze ZHANG

Crystallization Force: A Density Functional Theory Concept for Characterizing

P-177

239

Molecular Packing in Organic Crystals
Tonglei Li

Crystal structure of a lead(II) complex with furan-2- ylmethylene salicyloyl

P-178

240

hydrazine
Ying-Ying Zhang, Shi-Xiong Liu

P-179
P-180
P-181

Structures, Luminescence of Lanthanide-Organic Frameworks

241

Tian-Fu Liu, Rong Cao, Wen-Hua Sun

Cubic Lipid Phase & Bicelle Crystallization of Membrane Proteins242

Hartmut Luecke

New Inorganic Second-order NLO Materials Based on Lone Pair Cations

243

Jiang-Gao Mao, Ting Hu, Yong Zhou, Chuan-Fu Sun and Fang Kong

Crystal structure and phase transitions in C5H10NH2PbI3

P-182

Munehiko Nakatsuma, Miwako Takahashi, Kota Takano, Takuro Kawasaki, Kunimitsu Kataoka and244

Ken-ichi Ohshima

Crystallographic

P-183

3+

structure3+

Y(Ta,Nb)O4:Eu ,Tbandluminescence

properties

of

245

phosphors

Mihail Nazarov, Do Young Noh, Su Woong Lee

Structural Membrane Proteomics – X-ray Structure of Sulfide:Quinone

P-184

Oxidoreductase on The Hyperthermophilic Eubacteria Aquifex aeolicus
Guohong Peng, Marco Marcia, Ulrike Wedemeyer, Ye Gao, Tao Wang, Tanja Hedderich, Chuli

246

Zhang , Hartmut Michel

P-185
P-186
P-187
P-188

Kinetics of Crystalline-Non-Crystalline Phase Transition in Sucrose
Son Van Phung , Taro Fujita, Miwako Takahashi , Ken-ichi Ohshima

Metal Coordination Polymers containing tetrapyridyl based Ligands
Abdul Malik Puthan Peedikakkal, Jagadese J. Vittal

Structural basis for the mechanism of respiratory complex I
Leonid Sazanov, John Berrisford

Structural basis for translational inhibition by the tumour suppressor Pdcd4
Portia G Loh, Hsin-Sheng Yang, Haiwei Song

247
248
248
249

Exploring the Bond topological and Electrostatic properties of Benzimidazole

P-189

molecule via Experimental and Theoretical Charge Density Study

250

Arputharaj David Stephen, Reji Thomas, Vijayan Narayayanasamy, Poomani Kumaradhas

P-190

X-Ray Based Enzyme Design for Alkaloid Libraries
Joachim Stoeckigt

250

Crystal Structure of Porcine Reproductive and Respiratory Syndrome Virus

P-191(PRRSV) Leader Protease Nsp1α
Yuna Sun, Fei Xue, Yu Guo, Ming Ma, Ning Hao, Xuejun C. Zhang, Zhiyong Lou, Xuemei Li, Zihe
Rao

- XX -

252

AsCA’09

Content
Structure and guest release behavior comparison of inclusion crystals of

P-192

1,1,2,2- tetrakis (4- hydroxy phenyl) ethane and imidazole derivatives
Takenori Takeda, Akiko Sekine, Hidehiro Uekusa, Natsuki Amanokura, Masami Kaneko , Hiroshi

252

Suzuki

Calcium binds to LipL32, a lipoprotein from pathogenic leptospira, and

P-193

253

modulates fibronectin binding
Jung-Yu Tung, Shao-Wen Chou, Chien-Chih Lin, Yi-Ching Ko, Chih-Wei Yang, Yuh-Ju Sun

P-194

Purification, crystallization and preliminary data analysis of Proteorhodopsin
Ning Wang, Tingting Ran, Weiwu Wang

254

Structure, mechanistic action, and essential residues of laminaripentaose-

P-195

producing β-1,3-glucanase

255

Wen-Ching Wang, Hsin-Mao Wu, Sheng-Wen Liu, Ming-Tsung Hsu, Jong-Yih Lin, Yaw-Kuen Li

P-196

A novel (4,8)-connected 3D metal-organic framework based on in situ ligand
Peng Li, Jiaying Lou, Yaming zhou, Linhong Weng

255

Solvent-Dependent Assembly of Ni(II) Coordination Polmers: Structural

P-197

256

Variation from 1D to 2D
Jiaying Lou, Peng Li, Yaming zhou, Linhong Weng

Structural basis for the inhibition of human MTHFS by N10-substituted folate

P-198

analogues
Dong Wu, Yang Li, Gaojie Song, Chongyun Cheng, Rongguang Zhang, Andrzej Joachimiak, Neil

257

Shaw, Zhi-Jie Liu1

High-resolution crystal structure and functional analysis of a truncatedP-199

thylakoid lumen protein AtTLP18.3 reveal its novel phosphatase activity

258

Hsin-Yi Wu, Mao-Sen Liu, Tsan-Piao Lin, Yi-Sheng Cheng

Crystallization processes of inorganic functional materials: both experimental

P-200

259

and theoretical studies
Dongfeng Xue , Congting Sun

Chemical Bonding Characteristics and Structural Formability of Perovskite

P-201

260

Compounds
Na Li, Dongfeng Xue

Structural basis of nucleotide exchange and clients binding by a novel

P-202

260

hsp70-cochaperone bag2
Zhen Xu, Richard C Page, Saurav Misra

Structure of st0929, a putative glycosyl transferase from Sulfolobus tokodaii

P-203

Charles B.C. Cielo, Seiji Okazaki, Tatsuo Hikage, Atsuo Suzuki, Tsunehiro Mizushima, Ryoji Masui,

261

Seiki Kuramitsu, Takashi Yamane

Dimerization is important for the GTPase activity of chloroplast translocon

P-204

components atToc33 and psToc159
Yi-Hung Yeh, Muppuru M. Kesavulu, Hsou-min Li, Shu-Zon Wu, Yuh-Ju Sun, Emadeldin H.E

262

Konozy , Chwan-Deng Hsiao

Synthesis, Structure and Properties of Ba8Au5Ge40

P-205

Hui Zhang, Walter Schelle, Michael Baitinger, Mei-Bo Tang, Zhen-Yong Man, Hao-Hong Chen,
Xin-Xin Yang, Jing-Tai Zhao, Yuri Grin

- XXI -

262

AsCA’09

Content
Purification, crystallization and preliminary X-ray diffraction analysis of human

P-206

263

THRSP
Wenzheng Zhang,Wei Peng,Weihong Zhou, Mark Bartlam, Zonghao Zeng , Zihe Rao

Structure of main protease from a global infectious human coronavirus,

P-207

264

HCoV-HKU1
Qi Zhao, Shuang Li, Fei Xue, Yilong Zou, Cheng Chen, Mark Bartlam, Zihe Rao

Expression，Purification, Crystallization and Preliminary X-ray Analysis of

P-208

Cytochrome P450 153C1 from Novosphingobium aromaticivorans DSM12444

264

Weihong Zhou, Wen Yang, Stephen G. Bell, Mark Bartlam, Luet-Lok Wong and Zihe Rao

Author Index
266

Author Index- XXII -Abstracts

AsCA’09

Plenary and Keynote

Ted Baker CV and Abstract
Professor Ted Baker began his career in protein crystallography as a
Postdoctoral Fellow at Oxford University, working with Professor
Dorothy Hodgkin on the structure of insulin. He then led theestablishment of structural biology in New Zealand, and has madeinternational contributions in many areas, including protein structurerefinement, hydrogen bonding, and the function of metalloproteinsand bacterial toxins. In other international roles, he served as
President of the International Union of Crystallography (1996-1999),
and is a member of the Scientific Advisory Boards of several
international bodies, including the Worldwide Protein Data Bank. He
is currently Distinguished Professor of Structural Biology at the University of Auckland.
Professor Baker is a Fellow of the Royal Society of New Zealand, winner of the Rutherford
Medal (New Zealand’s foremost science honour) and the Hector Medal, and was an
International Research Scholar of the Howard Hughes Medical Institute. His current researchinterests focus on experimental protein structure analysis and its applications to functional
genomics, structure-based drug design, and the microbial pathogenesis.

-1-

AsCA’09

Plenary and Keynote

Celebrating Crystallography

PL-1

Edward N. Baker
Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences,
University of Auckland, Private Bag 92019, Auckland, New Zealand(ted.baker@auckland.ac.nz)

Crystallography provides a unique window on the natural world. Its ability to “see” theatomic and molecular structures of materials, whether from biology, chemistry or other areasof science, can give new insights into how things are and present wonderful opportunities forcreativity and applications. This lecture will trace the historical development ofcrystallography, celebrating its contributions to understanding the world around us.
Crystallography was initially the province of philosophers and mathematicians who marvelled
at the beauty and symmetries of crystals and speculated about what these might mean. The
idea gradually developed that external form must reflect internal structure, with Louis Pasteur
providing one of the first and most important demonstrations of this idea. The discovery of
X-ray diffraction in the early 1900s changed crystallography radically, with a series of great
pioneers such as William and Lawrence Bragg, Dorothy Hodgkin, J. D. Bernal, Linus Pauling,
Max Perutz, Francis Crick and others showing how crystallography could help reveal themysteries of chemistry and biology. Subsequent generations of crystallographers have also led
the way in showing how knowledge of atomic and molecular structures can be usefully
applied in areas such as the development of new therapeutics or novel materials. Finally it isalso apparent that the structures themselves carry connections between biology, chemistry
mathematics and even art and architecture.
These are all good reasons to celebrate the ways in which crystallography provides such a
stimulating and satisfying discipline.

-2-

AsCA’09

Plenary and Keynote

Hongkun Park CV and Abstract
Professor of Chemistry and of Physics, Harvard University
Contact:
12 Oxford Street, Cambridge, MA 02138
Tel: 617-496-0815
Fax: 617-384-7998
E-mail: hongkun_park@harvard.edu
WWW: www.people.fas.harvard.edu/~hpark/index.html

Curriculum Vitae
•
•
•
•
•
•
•

2004 – present: Full Professor Chemistry and of Physics, Harvard University
2003 – 2004: John L. Loeb, Associate Professor of the Natural Sciences, Harvard University
2003 – 2004: Associate Professor of Chemistry, Harvard University
1999 – 2003: Assistant Professor of Chemistry, Harvard University
1996 – 1999: Postdoctoral fellow, Lawrence Berkeley National Laboratory
1991 – 1996: Ph.D., Physical Chemistry, Stanford University
1986 – 1990: B.S., Chemistry, Seoul National University

Selected Awards and Honors
•
•
•
•
•
•
•
•
•
•
•
•

NIH Director’s Pioneer Award (2008)
Fellow, The World Technology Network (2004)
Ho-Am Prize for Science (2003)
Visiting Miller Research Professorship, University of California, Berkeley (2003)
Camille and Henry Dreyfus Teacher-Scholar Award (2003)
Alfred P. Sloan Foundation Research Fellowship (2002)
David and Lucile Packard Foundation Fellowship for Science and Engineering (2001)
National Science Foundation CAREER Award (2001)
Research Corporation Research Innovation Award (1999)
Camille and Henry Dreyfus New Faculty Award (1999)
Franklin Veatch Memorial Fellow, Stanford University (1993)
Presidential Prize and Valedictorian: Seoul National University (1990)

Research Interests
Nanometer-sized materials represent a natural size limit of the miniaturization trend of current
technology, and they exhibit physical and chemical properties significantly different from their bulk
counterparts. Hongkun Park is developing cutting-edge experimental methods to incorporate
individual molecules and nanostructures into electronic, optoelectronic, and plasmonic devices. Using
these methods, he is characterizing their behaviors in detail to gain insights about their behavior andexploring the potential of these devices for future technological applications.
He is also using his nanoscience expertise to develop new nano- and microelectronic tools that caninterface with live cells, cell networks, and living organisms. Specifically, he is investigating verticalnanowire arrays as a platform to perturb cellular functions in a massively parallel, arrayed fashion, andpatch-clamp and nanowire arrays for recording real-time dynamics of in vitro and in vivo neuronalensembles. These tools will impact a broad range of high-throughput discovery efforts in biology andhelp scientists to unravel the design principles of complex cellular networks.

-3-

AsCA’09

Plenary and Keynote

Vertical Nanowire Arrays: a Universal Platform forInterfacing with Living Cells

PL-2

Hongkun Park
Department of Chemistry and Chemical Biology and Department of Physics, Harvard
University, 12 Oxford Street, Cambridge, MA 02138(hongkun_park@harvard.edu)

At the heart of all investigations into cellular function lies the need to induce specific andcontrolled perturbations to cells. A variety of tools are now available to accomplish this in arational and directed fashion by delivering various biological effectors (small molecules,
DNAs, RNAs, peptides, and proteins). These options, however, are often limited to either
particular molecules or certain cell types due to the lack of a general strategy for transporting
polar or charged molecules across the plasma membrane. In this presentation, we show thatvertical silicon nanowires (NWs) can serve as a universal platform for delivering virtually any
type of molecule into a wide variety of cells in a format that is compatible with live-cell
imaging and microarray technology. The platform’s simplicity and generality stem from thedirect physical access to the cells’ interiors that NW penetration affords, thereby enabling
efficient introduction of numerous biological effectors without chemical modification or viral
packaging. Furthermore, this NW-based system is fully compatible with standard microarray
printing techniques, allowing large collections of biomolecules to be co-delivered into live
cells in a parallel and miniaturized fashion.

-4-

AsCA’09

Plenary and Keynote

Yoshinori Fujiyoshi CV and Abstract
Contact: Department of Biophysics, Graduate School of Science,
Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto,606-8502, Japan
Tel: +81-75-753-4215,
Fax; +81-75-753-4218
E-mail; yoshi@em.biophys.kyoto-u.ac.jp

Education:
1982
1976
1971

Kyoto University, Ph. D. (Chemistry)
Kyoto University, M. Sc. (Chemistry)
Nagoya University, B. Sc. (Chemistry)

Employment:
19961994-1996
1987-1994
1980-1987

Molecular Biophysics, Department of Biophysics,
Faculty of Science, Kyoto University, Professor
International Institute for Advanced Research,
Matsushita Electric Industrial Co., Ltd., Research Director
Protein Engineering Research Institute,
Senior research Scientist (1987-1988); Research Director (1988-1994)
Institute for Chemical research, Kyoto University,
Research Assistant (1980-1984); Instructor (1985-1987)

Other Activities and Awards:
2008
2007
2006
2005
2005
2005
2005
2000-2004
2003-2006
1999-2003
1988
1979-1980

Japan Academy Prize, The Japan Academy
Medal with Purple Ribbon, Government of JapanThe Shimadzu Prize, Shimadzu Science Foundation
The Keio Medical Science Prize, Keio University Medical Science FundThe Yamazaki-Teiichi Prize, Foundation for Promotion of Material Science andTechnology of Japan
DOCTOR HONORIS CAUSA of the “Iuliu Hatieganu” University of Medicine
and Pharmacy of Cluj-Napoca
Minister of Science and Technology Policy Award for the Industry-AcademiaGovernment Collaboration Contributor Awards
Japan Biological Information Research Centre, Structural Genomics team leader
RIKEN Harima Institute, MD group leader
RIKEN Harima Institute, MD group, Multisome team leader
Setoh Prize, the Japanese Society of Electron Microscopy
Kyoto University, Fellow of the Japan Society for the promotion of Science-5-AsCA’09

Plenary and Keynote

Structural physiology based on electron
crystallography

PL-3

Yoshinori Fujiyoshi
Department of Biophysics, Graduate School of Science, Kyoto University, Oiwake,
Kitashirakawa, Sakyo-ku, Kyoto 606-8502, JAPAN(yoshi@em.biophys.kyoto-u.ac.jp)

A biological cell, such as a nerve cell, regulates cell signaling mainly by ion channels. Water
permeation through biomembranes should therefore be strictly separated from the movementof ions. This means water channels must be highly specific and effective for water to prevent
any ions. One water channel can permeate 3 billion water molecules in a second without
proton permeation. When water molecules rapidly cross the membrane channel, they form acontinuous unbroken column and their hydrogen-bond chain conducts protons as domino
toppling with great efficiency. The pore has to prevent proton passage and the hydrogen-bondseparation is required while such requirement increases energy barrier reducing the water
permeation speed. For answering these questions, structure of aquaporin-1 was analyzed at aresolution of 3.8 Å by electron crystallography [1]. For accomplishing the effective water
channel functions, the structure showed peculiar structural determinants including an unusual
fold, for which we named aquaporin fold [1]. Based on the structure of aquaporin-1, we
proposed H-bond isolation mechanism by which we could explain a mechanism of high speed
water permeation without transfer of protons. However, the resolution was limited and we
could observe no water molecules in the structure analysis of aquaporin-1. By analyzing
structure of aquaporin-0 at a resolution of 1.9 Å, we could clearly observed water moleculesin the channel [2]. However, the structure was at closed state of the channel and only threewater molecules ware discriminated. By improving the resolution of fast water permeation
channel, aquaporin-4, whose structure was analyzed at 3.2 Å resolution [3] and showed 8
water molecules in the channel, we confirmed the H-bond isolation mechanism [4].
The aquaporin-4 molecule acquired two very important functions in cell biology, cell adhesiveand channel functions. We named this type channels as “Adhennel” family [3]. Gap Junction
channel is a typical Adhennel family protein and we analyzed structure of a mutant of Cx26
which was related with hearing loss. Based on the structure of the mutant Cx26 channel, we
proposed a plug gating model [5]. We also published a structure of wild type Cx26 at openstate analyzed by X-ray crystallography, and explained a gating mechanism by transjunctional
voltage [6]. Although the gating mechanisms of gap junction channels are complicated,
electron crystallography enables us to elucidate structural and functional relationship of suchmembrane proteins based on their structures in membrane.
By focusing on multifunctional channels like Adhennels, I would like to introduce recent
results in structural physiology based on electron crystallography of membrane proteins byutilizing our cryo-electron microscopes with helium cooled specimen stages [7].
References[1] K. Murata et al., Nature 407, 599-605 (2000)[2] T. Gonen et al., Nature 438, 633-638 (2005)[3] Y. Hiroaki et al. J. Mol. Biol. 355, 628-639 (2006)[4] K. Tani et al. J. Mol. Biol. 389, 694-706 (2009)[5] A. Oshima et al. PNAS 104, 10034-10039 (2007).
[6] S. Maeda et al., Nature 458, 597-602 (2009)[7] Fujiyoshi Y., Adv. Biophys. 35, 25-80 (1998)-6-

AsCA’09

Plenary and Keynote

Joel L. Sussman CV and Abstract
Prof. Joel L. Sussman is the Morton and Gladys Pickman Professor of
Structural Biology at the Weizmann Institute of Science, and the
Director of the Israel Structural Proteomics Center (ISPC,
http://www.weizmann.ac.il/ISPC) He is a member of the European Molecular
Biology Organization (EMBO) and a member of the Executive Board,
Int’l Structural Genomics Org (ISGO) and on the editorial board for thejournals: Proteins, PEDS & PLoS ONE. He is Chairman of the Israel
Council of Higher Education Bioinformatics Committee and the
Coordinator of the Forum for European Structural Proteomics. He isan Honorary Professor of the Chinese Academy of Sciences, received
the Bergmann Prize for Outstanding Research in Chemistry in Israel (1979), the U.S. Army
Science Conference Award for Outstanding Research (1991), the Elkeles Prize for
Outstanding Scientist in Medicine in Israel (2005), the Teva Founders Prize for Breakthroughs
in Molecular Medicine (2006) and. From 1994 -1999 he was the director of the BrookhavenProtein Data Bank (PDB). He obtained his B.A. at Cornell University in 1965, and his Ph.D.
in biophysics at MIT in 1972. His research group, at the Weizmann Institute, is studying the
3D structure/function of nervous system proteins, such as b-secretase, acetylcholinesterase,cholinesterase-like adhesion molecules (CLAMs), b-glucosidase (the enzyme that is defective
in Gaucher disease) and paraoxonase (a key enzyme that helps rid the arteries ofplaque-forming clumps of LDL (“bad” cholesterol) that can lead to arteriosclerosis). The goalof his research is to use the 3D structures of proteins that his group is determining as a basis
for new leads for treating neurological disorders, such as Alzheimer's Disease, autism, and indeveloping new therapies for Gaucher and arteriosclerosis. He is also studying intrinsicallyunfolded proteins as well as how proteins adapt to extreme environments, e.g. halotolerant
proteins. Most recently he and his colleagues have developed Proteopedia, the free,collaborative 3D encyclopedia of proteins & other molecules (http://www.proteopedia.org).

-7-

AsCA’09

Plenary and Keynote

Proteopedia - a Scientific ‘Wiki’ Bridging the Rift
Between 3D Structure and Function of
Biomacromolecules

KN-1

Joel L Sussman1,2, Eran Hodis3, Jaime Prilusky1,4, Israel Silman1,5, John Moult6 &Eric Martz7
1
The Israel Structural Proteomics Center, 2Departments of Structural Biology,
3
Computer Science & Applied Math, 4Biological Services Unit, 5Neurobiology,
Weizmann Institute of Science, Rehovot 76100 ISRAEL; 6CARB, Univ of MD
Biotechnology Institute, Rockville, MD 20850; 7Department of Microbiology, Univ of
MA, Amherst, MA 01003

Rather than relying just on printed text to provide the basis for the understanding of
biomacromolecular structures, acollaborative
websitecalledProteopedia is a new resource forlinking written information and 3D
structural information. Proteopedia(http://www.proteopedia.org)
displays protein structures and otherbiomacromolecules interactively, i.e.
can be rotated and zoomed (seefigure). These interactive images are
surrounded by text with hyperlinks
that change the appearance of the
3D structure to reflect the concept
explained in the text. This makes the complex structural information readily accessible andcomprehensible, even to non-structural biologists. Using Proteopedia, anyone can easily
create descriptions of biomacromolecules linked to their 3D structure, e.g.:β2-Adrenergic Receptor - http://www.proteopedia.org/wiki/index.php/Hoelzer_Sandbox
Proton Channels: http://proteopedia.org/wiki/index.php/Proton_Channels
HIV-1 protease: http:/proteopedia.org/wiki/index.php/HIV-1_protease
Lac repressor: http://proteopedia.org/wiki/index.php/Lac_repressor
AChE/Aricept complex in Chinese: http://www.proteopedia.org/wiki/index.php/1eve(Chinese)
Aside from content added by the more than 500 registered users of Proteopedia, pages oneach of the more than 60,000 entries in the PDB have been automatically created, and areprimed for expansion by users. Members of the scientific community are invited to request auser account to edit existing pages and to create new ones. For details, see: Hodis, Prilusky,
Martz, Silman, Moult & Sussman (2008) Genome Biol 9, R121.

-8-

AsCA’09

Plenary and Keynote

Matthew Rosseinsky CV and Abstract
Matthew Rosseinsky obtained a degree in Chemistry from the
University of Oxford and a D. Phil under the supervision of Professor
P. Day, FRS in 1990. He was a Postdoctoral Member of TechnicalStaff at A.T.&T. Bell Laboratories in Murray Hill, New Jersey where
his work with D.W. Murphy led to the discovery of superconductivity
in alkali metal fullerides. In 1992, he was appointed University
Lecturer at the Inorganic Chemistry Laboratory, University of Oxford,
where he remained until 1999 when he moved to the University ofLiverpool as Professor of Inorganic Chemistry. He was awarded theinaugural de Gennes Prize for Materials Chemistry by the RSC in 2009. He was elected a
Fellow of the Royal Society in 2008.
His work has spanned several fields, but is unified by the development of synthesis coupledwith detailed characterisation to control the functional behaviour of materials in a chemicallyunderstandable manner. He has demonstrated the new materials properties that arise from theconstruction of microporous materials from molecular components, focussing on differencesfrom the highly thermally stable aluminosilicate systems and emphasising flexibility of
response to guests and chiral sorption, most recently through the construction of open
frameworks from amino acid and peptide components. He has developed the metal fullerides
into the best model systems for correlated electron high temperature superconductivity. He
has worked extensively on transition metal oxide chemistry, developing hydride ion reduction
to access novel reduced materials with high ionic mobility and recently extending this work to
the identification of a new class of interstitial-based oxide ion conductor. To enable a more
direct relationship between the design of complex oxide structures and real synthetic
procedures, he has used layer-by-layer pulsed laser deposition to access metastable inorganic
solids as thin films by sequential assembly of unit cells of the structural components. His
work has been characterised by extensive collaboration with many academic and industrial
colleagues.

-9-AsCA’09

KN-2

Plenary and Keynote

Reactivity and flexibility in metal-organic
frameworks: amino-acid based and post-syntheticallyfunctionalised materials
M.J. Rosseinsky
Department of Chemistry, University of Liverpool

The precisely defined interior cavities of porous metal-organic frameworks with a high degreeof chemical diversity are attractive for selective sorption. We describe a family of amino-acidbased open frameworks (1) which display chirally selective sorption that is highly specific to
the functional group disposition within the sorbed molecules. The nature of the interaction
between the framework and sorbate is revealed by computational approaches used inprotein-ligand docking.
The cavities within metal-organic framework materials
are also attractive hosts for the observation of chemical
reactions with atomic-scale resolution by crystallography,
permitting the observation of co-operative involvement of
the surrounding solid in accommodating the changes at
the reacting centre (2). This motivates the development of
post-synthesis chemistry to introduce catalytically active
centres into metal-organic frameworks, which in turnopens up the possibility of reactive sites and reaction
chemistry that are inaccessible outside the metal-organic framework environment. (3)References[1] Vaidhyanathan, R., Bradshaw, D., Rebilly, J. N., Barrio, J. P., Gould, J. A., Berry, N. G., and Rosseinsky,
M. J., Angew. Chem. Int. Ed. Engl.. 45, 6495 (2006); Ingleson, M. J., Bacsa, J., and Rosseinsky, M. J.,
Chemical Communications (29), 3036 (2007); Barrio, J. P., Rebilly, J. N., Carter, B., Bradshaw, D.,
Bacsa, J., Ganin, A. Y., Park, H., Trewin, A., Vaidhyanathan, R., Cooper, A. I., Warren, J. E., andRosseinsky, M. J. Chemistry-a European Journal 14 (15), 4521 (2008); Rebilly, J. N., Gardner, P. W.,
Darling, G. R., Bacsa, J., and Rosseinsky, M. J., Inorganic Chemistry 47 (20), 9390 (2008). J.N.
Rebilly, J. Bacsa, M. J. Rosseinsky Chemistry – an Asian Journal 4, 892-903, (2009)[2] D. Bradshaw et al. Science 315, 977 - 980, 2007.
[3] Ingleson, M. J., Barrio, J. P., Bacsa, J., Dickinson, C., Park, H., and Rosseinsky, M. J., Chemical
Communications (11), 1287 (2008); Ingleson, M. J., Barrio, J. P., Guilbaud, J. B., Khimyak, Y. Z., andRosseinsky, M. J., Chemical Communications (23), 2680 (2008). M. J. Ingleson, J. Perez Barrio, J.
Bacsa, A. Steiner, G. R. Darling, J. T. A. Jones, Y. Z. Khimyak, and M. J. Rosseinsky Angew. Chemie.,Int. Ed., 48, 2012, (2009).

- 10 -

AsCA’09

Plenary and Keynote

David Owen CV and Abstract
Following a degree in biochemistry and a D.Phil with Professor Dame Lousie Johnson on the
structure and function of protein kinases, both at the University of Oxford, David Owen
moved to the MRC LMB in Cambridge in 1995. Here he carried out structure/function studies
on protein involved clathrin coated vesicle formation under the sponsorship of Dr PhilipEvans. In 2000 he was awarded a Wellcome Trust Senior Research Fellowship in Basic
Biomedical Science to start a small group in the Cambridge Institute for Medical Research in
Medical School at the University of Cambridge to carry on this work.

- 11 -

AsCA’09

KN-3

Plenary and Keynote

Cargo recognition during clathrin-coated vesicle
formationDavid Owen

Transmembrane proteins are moved between organelles in transport vesicles. Once cargo has
been sorted into a forming vesicle, the vesicle buds from the donor membrane and is thentransported to and fuses with its target membrane. Many steps in post-Golgi transport ismainly mediated by clathrin-coated vesicles (CCVs), whose coats are composed of an outerclathrin scaffold linked to the membrane by clathrin adaptors including AP complexes, GGAs,
epsins and ARH. Clathrin adaptors have folded domains that bind to membrane phospholipid
headgroups and in some cases simultaneously bind to transmembrane cargo thereby selecting
the cargo for incorporation into a CCV. The remainder of the proteins are extended, flexible
regions that connect contain multiple short motifs, which bind to clathrin and the appendagesof major clathrin adaptors, the APs and GGAs. Standard cargo possesses short, transplantable,
linear motifs such as YxxΦ, [DE]xxxLL and FxNPxY or are poly or multiply
monoubiquitinated so enabling the cargo to bind directly to the folded domains of clathrin
adaptors and so be recruited as cargo into forming CCVs. For clathrin mediated endocytosis
from the cell's limiting membrane, YxxΦ motifs are bound by the μ2 subunit of the AP2adaptor complex and [DE]xxxLL motifs by the σ2 subunit.
The SNAREs are type II integral membrane proteins, which are present on both transport
vesicles and target membranes. They form highly specific trans hetero tetrameric complexes
thus bringing the vesicle and its correct target into close apposition and so provide thespecificity and at least part of the mechanical driving force for the fusion of a transport vesicle
with its target. In addition to the SNARE helix that is common to all SNAREs and throughwhich SNARE complexes are formed, many SNAREs also small folded regulatory
N-terminal domains. We have very recently shown that there are highly specific,
fold-dependent, extensive surface patch mediated interactions between the N-terminal
domains of two SNAREs (vti1b and Vamp7) with two different CCV components (epsinRand Hrb respectively) by determining the structures of the complexes formed by the two
SNARE/adaptor pairs. In both cases disruption of the interactions by single point mutations
abolishes the interactions between the pairs of proteins in vitro and and alters the steady state
distribution of the SNAREs in vivo. These data, along with other published work, suggestthat non-motif mediated recognition of SNARE N-terminal folded domains by CCV
components is a general feature of the trafficking of individual SNAREs and SNARE
complexes.
Taken together, these two pieces of work suggest that there are at least two distinct cargorecognition systems that function in parallel without competing with each other during CCV
formation. This talk will present some of the molecular mechanisms behind these different
types of clathrin adaptor: CCV cargo interactions.

- 12 -

AsCA’09

Plenary and Keynote

Thomas Mak CV and Abstract
BSc (Hon. Chem & Phy) 1960, PhD (Chem) 1963,
The University of British Columbia
Wei Lun Research Professor and Professor Emeritus, The Chinese
University of Hong Kong
Member of Chinese Academy of Sciences
Ten Representative Publications[1]

X.-D. Chen, C.-Q. Wan, H. H.-Y. Sung, I. Williams and T.C.W. Mak*: Control of Channel Size for
Selective Guest Inclusion with Inlaid Anionic Building Blocks in a Porous Cationic Metal-organic
Host Framework. Chem. Eur. J. 15, 6518-6528 (2009).
[2] L. Zhao, C.-Q. Wan, J. Han, X.-D. Chen and T.C.W. Mak* . Ancillary Ligands and Spectator
Cations as Controlling Factors in the Construction of Coordination and Hydrogen-bonded Networks
Chem. Eur. J. 14, 10437-10444
with the tert-Bu−C≡C⊃Agn (n = 4, 5) Supramolecular Synthon.
(2008).
[3] J. Han, C.-W. Yau, C.-K. Lam and T.C.W. Mak*. Designed Supramolecular Assembly of AnionicHydrogen-bonded Rosette Layers. J. Am. Chem. Soc. 130, 10315-10326 (2008).
[4] S.-Q. Zang, L. Zhao and T.C.W. Mak*. Diverse Intermolecular Interactions in Metal-Organic
Frameworks Constructed with New Supramolecular Synthon Agn-L-Agn (n = 4 or 5) (H2L =2,2'-bis-prop-2-ynyloxy-biphenyl). Organometallics 27, 2396-2398 (2008).
[5] T.C.W. Mak,* X.-L. Zhao, Q.-M. Wang and G.-C. Guo. Synthesis and structural characterization ofsilver(I) double and multiple salts containing the acetylenediide dianion. Coord. Chem. Rev. 251,
2311-2333 (2007).
[6] L. Zhao, X.-L. Zhao and T.C.W. Mak. Assembly of Infinite Silver(I) Columns, Chains, and Bridged
Aggregates with Supramolecular Synthon Bearing Substituted Phenylethynides”. Chem. Eur. J. 13,
5927-5936 (2007).
[7] L. Zhao and T.C.W. Mak*: Assembly of Polymeric Silver(I) Complexes of Isomeric
Phenylenediethynides with the Supramolecular Synthons Agn⊂ C2—R—C2 ⊃Agn (R = p-, m-,
o-C6H4; n = 4, 5). J. Am. Chem. Soc. 127, 14966-14967 (2005).
[8] C.-K. Lam, F. Xue, J.-P. Zhang, X.-M. Chen and T.C.W. Mak*. Hydrogen-Bonded Anionic Rosette
Networks Assembled with Guanidinium and C3-Symmetric Oxoanion Building Blocks. J. Am. Chem.
Soc. 127, 11536-11537 (2005).
[9] L. Zhao and T.C.W. Mak*. Silver(I) Butadiynediide and Two Related Silver(I) Double Salts
Containing the C42- Dianion. J. Am. Chem. Soc. 126, 6852-6853 (2004).
[10] Q.-M. Wang and T.C.W. Mak*. Elliptic Column Consolidated by Acetylide Dianion, Cyanide andTrifluoroacetate in a Novel Quadruple Salt of Silver(I). J. Am. Chem. Soc. 123, 1501-1502 (2001).

Books
T.C.W. Mak and G.-D. Zhou, "Crystallography in Modern Chemistry: A Resource Book of Crystal
Structures", Wiley-Interscience, New York, 1992; Professional Paperback Edition, 1997.
W.-K. Li, G.-D. Zhou and T.C.W. Mak, "Advanced Structural Inorganic Chemistry", Oxford
University Press, Oxford, 2008.

- 13 -

AsCA’09

KN-4

Plenary and Keynote

Crystalline Silver(I) Complexes containing All-carbon
and Carbon-rich Anionic Ligands
Thomas C. W. Mak
Department of Chemistry and Center of Novel Functional Molecules,The Chinese
University of Hong Kong, Shatin, Hong Kong SAR,, China (tcwmak@cuhk..edu.hk)

In the context of supramolecular chemistry, the coordination concept as commonly applied tometal ions has been extended to polyatomic anionic species.[1] In the designed construction of
coordination networks, it is of interest to determine the highest ligation number (HLN) of
simple inorganic polyatomic anions, namely the largest number of coordination bonds that a
particular anion can form with neighboring metal centers in its complexes.[2]Over a decade ago, we embarked on a systematic study on the HLN of small inorganic anions
such as the pseudohalides CN−, SCN−, N3− and SeCN− using the silver(I) ion as an ideal probe.
Such a choice is favored by the tendency of Ag(I) to form multinuclear aggregates throughthe d10−d10 metallophilic interaction.[3] By dissolving each silver(I) pseudohalide in aconcentrated aqueous solution containing one or more water-soluble silver(I) salts, a series of
new double and triple silver(I) salts were obtained, and their crystal structures were
determined by single-crystal X-ray diffraction.
We subsequently investigated the all-carbon diatomic ligand ethynediide (also named
acetylenediide, C22−), an isoelectronic structural analog of CN−, N2 and NO+. In the resulting
double, triple and quadruple silver(I) salts, the dumbbell-like −C≡C− species was found to beinvariably encapsulated in a polyhedral silver(I) cage of 6-10 vertices, and each C-terminal
has significant σ, π, and mixed (σ, π) interactions with only four or five vertices. We then
expanded the scope to synthesize silver(I) complexes of 1,3-butadiyne-1,4-diide (−C≡C−C≡C−)
and related ethynide species R−C≡C− (R = alkyl, aryl), thereby establishing the identity andutility of the multi-nuclear metal-ligand supramolecular synthons Ag4⊂C≡C−C≡C⊃Ag4 andR−C≡C⊃Agn (n = 4,5) for the construction of multi-dimensional coordination networks.
Several factors of influence, including the choice of counter anions, the presence of ancillary
spectator molecules, and variation of aromatic ring substituents on the self-assembly ofsilver-ethynide supramolecular synthons in crystallization have been systematically explored.
Our work up to 2007 has been summarized in two reviews,[4] and some recent advances will
be presented here.
Acknowledgements: This work is supported by Hong Kong Research Grants Council GRF
CUHK 402405 and 402408.
References
1.
2.
3.
4.

(a) Supramolecular Chemistry of Anions, ed. Bianchi, A.; Bowman-James, K.; and Garcia-Espańa, E.
Wiley-VCH, New York, 1996. (b) Beer, P. D.; Smith, D. K.; Prog. Inorg. Chem. 1997, 46, 1−96.
Guo, G.-C.; Mak, T. C. W. Chem. Commun. 1999, 813−814.
Pyykkö, P. Chem. Rev. 1997, 97, 597−636.
(a) Mak, T. C. W.; Zhao, X.-L.; Wang, Q.-M.; Guo, G.-C. Coord. Chem. Rev. 2007, 251, 2311−2333.
(b) Mak, T. C. W.; Zhao, L. Chem. Asian J. 2007, 2, 456−467.

- 14 -

AsCA’09

Invited and Oral

Arms race between host and pathogen

MS1-1

Jijie ChaiNational Institute of Biological Sciences, Beijing 102206,China(chaijijie@nibs.ac.cn)

Molecular mimicry is a common strategy utilized by pathogens for manipulating host cellularsignaling to their own benefit. Here we first present an example where a large family bacterial
effector protein functions as GEFs mimics rather than GTPase mimics as previously proposed.
Our data define a novel mechanism underlying the selection of host substrates by bacterial
GEF mimics, which is consistent with pathogenic diversity observed in numerous bacterial
infectious agents. We then present evidence that host can also employ a mimicking strategy tocounter against the invading pathogens. Coupled with genetic and biochemical studies, thecrystal structure of a plant pathogen effector protein AvrPto in complex with its host Pto
kinase suggests that Pto may act as a ‘decoy’ by mimicking a kinase that is targeted bypathogens for their pathogenesis. Collectively, our results suggest that the interplay between
pathogen and host features a process of dynamic evolution.

Structural studies on the Glutathione Transferases
and their involvement in resistance to chemotherapy
treatment

MS1-2

Lorien J. Parker1,4, Paul J. Dyson2, Mario Lo Bello3 and Michael W. Parker4
1. RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho,Tsurumi-ku,
Yokohama City, 230-0045, Kanagawa, Japan (parker@ssbc.riken.jp)
2. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale deLausanne, 1015 Lausanne, Switzerland (paul.dyson@epfl.ch)
3. Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica
snc, Rome 00133 Italy (lobello@uniroma2.it)
4. St. Vincent’s Institute of Medical Research, 9 Princes St, Fitzroy, Melbourne, Victoria,
3065, Australia (mparker@svi.edu.au)

The clinical efficacy of anti-cancer drugs is often limited by the emergence of drug resistancein cancer cells. The Pi class GST enzyme, GSTP1-1, is believed to be an important factor inresistance and its overexpression has been reported in a number of different humanmalignancies. Changes in the levels of GSTs have repeatedly been correlated with resistanceto anti-cancer agents, presumably through accelerated detoxification of drugs by conjugation
with glutathione1. More recent evidence, described below, suggests GSTs also contribute toresistance through covalent or non-productive binding of some compounds, highlighting thepotential in targeting GSTs for inhibitor drug design.
To elucidate the mechanism behind drug deactivation by GSTs crystal structures of GSTP1-1
with numerous anti-cancer drugs were determined. Cisplatin, an extensively used anti-cancer
drug, was expected to bind in the active site where it was presumed to be deactivated by GSH
conjugation, thus explaining the resistance suffered by patients undergoing treatment with thiscompound. Surprisingly, the drug bound at dimer interface rather than the active site as
predicted. This is the first GSTP1-1 ligand identified to bind at the dimer interface, an
important discovery for drug design since, to date, all efforts targeting inhibition of GSTs
have focused on inhibiting the active site. The results from this structure indicate a necessary- 15 -

AsCA’09

Invited and Oral

shift towards targeting the dimer interface, in addition to the active site, when developing
potent and specific inhibitors for use as adjuvants in chemotherapy treatment.
The structure of the GST-ethacraplatin complex, (an inhibitor based on cisplatin designed byour collaborators) reveals the compound also binds at the dimer interface. In concordancewith these findings, collaborators in Switzerland designed a ruthenium-based drug to target
both sites simultaneously. This compound has been shown to successfully inhibit enzymatic
activity. The structure of the complex confirms the compound is able to bind at both sites ofthe enzyme2.
The structure of GSTP1-1 in complex with phenyl-arsine oxide, a membrane-permeable
phosphotyrosine phosphatase inhibitor, has been determined. Again the compound binds atthe dimer interface as well as at the active site. Furthermore, this structure reveals that each of
the molecules bound at the two separate sites also interact with each other. This structure
provides a scaffold for design of an inhibitor that binds simultaneously to both sites.
Taken together, these novel findings suggest that GSTP1-1 plays a role, other than classicaldetoxification, in contributing to the development of drug resistance. Surprisingly, themetal-based drugs bind at the dimer interface rather than the active site, thus revealing a newmechanism of resistance whereby the enzyme can sequester the drug from the cellular milieu.
Collectively, this information, in conjunction with findings from in-silico screening, have leadto crystallographic fragment based screening methods. Information gained from thesetechniques will be used for the design of optimal drug candidates by medicinal chemists in thenear future.

Figure depicting progress of GSTP1-1 drug targeting. Initial efforts targeted the active site. Results fromour work identified the dimer interface as important for metal-based inhibitors. Thus, current strategies
focus on targeting both sites. 1.Journal of Molecular Biology (2008) 380(1): 131-144. 2.Angewandt ChemieInternat. Ed (2009) 48: 3854-7

MS1-3Structural Study of PA subunit from an Avian
Influenza Virus RNA polymerase
Yingfang Liu1, Zihe Rao2
1.Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
2.IBP/Nankai University/Tsinghua University

Structural study of Influenza viral proteins especially its RNA polymerase proteins is criticalfor elucidation the underlying mechanisms of viral life cycle and for development ofanti-influenza virus drugs. The influenza RNA-dependent RNA polymerase (RdRp) complex,- 16 -

AsCA’09

Invited and Oralconsisting of PA, PB1 and PB2 subunits, plays crucial roles in viral RNA replication andtranscription. Recently, we have determined crystal structures of PA subunit from an avian
influenza A virus H5N1 by splitting it into two individual domains. Our results have not only
revealed some previously uncharacterized functional roles of PA, but also provided an ideal
target for novel anti-influenza therapy.

MS1-4

Ligand recognition by the TLR4-MD-2 complex
Jie-Oh Lee
Department of Chemistry, KAIST, Daejeon 305-701, Korea (jieoh.lee@kaist.ac.kr)

TLR4 and MD-2 form a heterodimer that recognizes LPS from Gram negative bacteria.
Eritoran is a candidate anti-sepsis drug that antagonizes LPS activity by binding to the
TLR4-MD2 complex. We determined the crystal structures of the TLR4-MD-2-Eritoran and
LPS complexes. TLR4 is an atypical member of the LRR family and is composed of
N-terminal, central and C-terminal domains. The sheet of the central domain shows
unusually small radii and large twist angles. MD-2 binds to the concave surface of the
N-terminal and central domains. Agonistic LPS induced the formation of an “m”-shaped
receptor multimer composed of two copies of the TLR4-MD-2-LPS complex arranged in asymmetrical fashion. LPS interacts with a large hydrophobic pocket in MD-2 and directly
bridges the two components of the multimer. Eritoran bind to the LPS pocket in MD-2 andblocks LPS binding and TLR4 heterodimerization. Five of the six lipid chains of LPS areburied deep inside the pocket and the remaining chain is exposed to the surface of MD-2,
forming a hydrophobic interaction with the conserved phenylalanines of TLR4. The F126
loop of MD-2 undergoes localized structural change and supports this core hydrophobic
interface by making hydrophilic interactions with TLR4. Comparison with the structures oftetraacylated antagonists, Eritoran and Lipid Iva, bound to MD-2 indicates that two other lipid
chains in LPS displace the phosphorylated glucosamine backbone towards the solvent area by~5 angstrom. This structural shift allows phosphate groups of LPS to contribute to receptor
multimerization by forming ionic interactions with a cluster of positively charged residues in
TLR4 and MD-2. The TLR4-MD-2-LPS structure illustrates the remarkable versatility of theligand recognition mechanisms employed by the TLR family, which is essential for defense
against diverse microbial infection.We propose that formation of the TLR dimer brings theintracellular TIR domains close to each other to promote dimerization and initiate signaling.

- 17 -

AsCA’09

Invited and Oral

Scaffold-Based Discovery of a Novel Selective
Inhibitor of Oncogenic B-Raf Kinase with Potent
Anti-Melanoma Activity

MS1-5

Kam Y.J. Zhang*, James Tsai, John T. Lee1, Weiru Wang, Jiazhong Zhang, Hanna
Cho, Shumeye Mamo, Ryan Bremer, Sam Gillette, Jun Kong1, Nikolas K. Haass1,
Katrin Sproesser1, Ling Li1, Keiran S.M. Smalley1, Daniel Fong, Yong-Liang Zhu,
Adhirai Marimuthu, Hoa Nguyen, Billy Lam, Jennifer Liu, Ivana Cheung, Julie
Rice, Yoshihisa Suzuki, Catherine Luu, Calvin Settachatgul, Rafe Shellooe, John
Cantwell, Sung-Hou Kim¶, Joseph Schlessinger$, Brian West, Ben Powell, Gaston
Habets, Chao Zhang, Prabha N. Ibrahim, Peter Hirth, Dean R. Artis, Meenhard
Herlyn1, Gideon Bollag
Plexxikon, Inc., 91 Bolivar Drive, Berkeley, CA 94710;*
Advanced Science Institute, RIKEN, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan(kamzhang@riken.jp).
1
Department of Molecular and Cellular Oncogenesis, The Wistar Institute, 3601 Spruce
Street, Philadelphia, PA 19104;¶
220 Calvin Laboratory, University of California, Berkeley, CA 94720;$
Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street,
New Haven, CT 06520

BRAFV600E is the most frequent oncogenic protein kinase mutation known. The BRAFV600E
gene is found in approximately 70% of malignant melanomas and a large number ofcolorectal and thyroid tumors. Furthermore, inhibitors targeting “active” protein kinases havedemonstrated significant utility in the therapeutic repertoire against cancer. Therefore, we
pursued the development of specific kinase inhibitors targeting B-Raf – and the V600E allele
in particular. Here, we present a novel scaffold targeting protein kinases, and we report theelaboration of this scaffold into a potent and selective inhibitor of “active” B-Raf. PLX4720,
a 7-azaindole derivative that inhibits B-RafV600E with an IC50 of 13 nM, defines a novel classof kinase inhibitor with marked selectivity in both biochemical and cellular assays.
PLX4720 preferentially inhibits the “active” B-RafV600E kinase compared to a broad spectrumof other kinases, and potent cytotoxic effects are also exclusive to cells bearing the V600E
allele. Consistent with the high-degree of selectivity, ERK phosphorylation is potently
inhibited by PLX4720 in B-RafV600E-bearing tumor cell lines but not in cells lacking
oncogenic B-Raf. In melanoma models, PLX4720 induces cell cycle arrest and apoptosis
exclusively in B-RafV600E-positive cells. In B-RafV600E-dependent tumor xenograft models,orally-dosed PLX4720 causes significant tumor growth delays – including tumor regressions– without evidence of toxicity. We describe here the entire discovery process, from initial
identification through structural and biological studies in animal models, to a promising
personalized therapeutic for testing in cancer patients bearing B-RafV600E-driven tumors.

- 18 -

AsCA’09

MS2-1

Invited and Oral

Metal Organic Frameworks for Proton Conduction
and CO2 Uptake
Jeff Hurd, Ramanathan Vaidhyanathan, Jared Taylor, Simon Iremonger, Karl
Dawson, George Shimizu
Department of Chemistry, University of Calgary, Calgary, Alberta, Canada(gshimizu@ucalgary.ca)

Two families of compounds will be presented in this talk, proton conducting MOFs and,MOFs with amine-lined pores for carbon dioxide sorption. MOFs are well studied for gas
sorption and the notion to include amine functionalities in pores has been pursued by several
groups. Recent results from our group concerning high heats of CO2 adsorption attained witha zinc aminotriazolate/oxalate system will be presented.1 On a separate theme, some recent
work on proton conducting MOFs prepared in our group will be shown.2 Beyond showingthat a crystalline MOF material can function to conduct protons in an anhydrous environment
at 150°C, the illustration will be made that the “PCMOFs” can function as gas separators.
References
1. R. Vaidhyanathan, S. S. Iremonger, K. W. Dawson, G. K. H. Shimizu, Chem. Commun., 2009, 5230 5232.
2. J. A. Hurd, R. Vaidhyanathan, V. Thangadurai, C. I. Ratcliffe, I. Moudrakovski, G. K. H. Shimizu,
Nature-Chem. accepted for publication.

MS2-2

Homoleptic Metal Organothiolate andOrganoacetylide Coordination Polymers: Structural
Determination using Powder X-ray Diffraction and
Their Materials Properties
Stephen Sin-Yin, CHUI1, Kam-Hung, LOW1, Roy V. A. L.2, Chi-Ming CHE1
1
Department of Chemistry, The University of Hong Kong, China(chuissy@hkucc.hku.hk)
2
Department of Physics and Materials Science, The City University of Hong Kong,
China.

In this presentation, several insoluble homoleptic metal organothiolate [M(S-aryl)n]∞ (M =Cu(I), Ni(II), Pd(II), Pt(II) and Ru(III) and Co(III)) and organoacetylide complexes [M(C≡C-R)]∞ (M = Cu, Ag, Au, R = aryl and n-alkyl) will be reported. All these complexes havebeen structurally determined and refined by powder X-ray diffraction data. They are found to
adopt either 1-D or 2-D coordination polymers with different topologies. For [Cu(SR)]∞, these1-D polymers grew along the long axes of the rod-like nano-crystals and their crystallite
morphology is significantly affected by the substituents of the thiolate ligands. Fabrication of
the respective bottom-contacted field-effect transistors using such nano-rod crystals, uses ofsingle-source precursor from [M(SR)n]∞ and magnetic properties of some [M(SR)3]∞ polymers
and photoluminescence of the [Cu(C≡C-R)]∞ will be discussed.
References- 19 -

AsCA’09

Invited and Oral

1. S. S. Y. Chui, M. F. Y. Ng, C. M. Che, Chem. Eur. J. 2005, 11, 1739–1749.
2. C. M. Che, C. H. Li, S. S. Y. Chui, K. H. Low, V. A. L. Roy, Chem. Eur. J. 2008, 14, 2965–2975.

Ionothermal Synthesis of Metal Organic Framework
Materials

MS2-3

Zhuojia Lin1, Linna Huang1, Ming-Liang Tong1 and Russell E. Morris2
1
MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry
and Chemical Engineering, Sun Yat-Sen University, Guangzhou 510275, China(linzhjia@mail.sysu.edu.cn)
2
EaStChem School of Chemistry, University of St. Andrews, St Andrews, Fife, Scotland,
UK KY16 9ST ( rem1@st-and.ac.uk)

Ionothermal synthesis, the use of an ionic liquid as solvent and structure directing agent in thesynthesis of crystalline materials, offers many advantages over traditional materials synthesis
methods. Here we report the use of ionothermal synthesis to prepare new metal organic
framework materials based on the copper, cobalt, nickel and manganese trimesate (TMA)
systems and discuss some interesting chemistry happened in ionic liquids.
A series of novel materials can be prepared simply by changing the metal used (Co/Ni) or theorganic cation of the ionic liquid, showing the template effect of ionic cations in theionothermal synthesis of metal organic frameworks. The anions in ionic liquids play asignificant role in solvent polarity and hydrophibicity, which in turn control the structures ofmaterials formed in the ionothermal synthesis. More surprisingly changing the anion frombromide to the enantiometically pure anion L-aspartate allows a chiral induction effect that
results in a chiral framework that does not occlude the L-aspartate anion and is composed ofonly non-chiral building blocks. This is, we believe, the first time such an effect has been seen
in materials synthesis. We also found that a highly porous copper-TMA metal organic
framework with an unusual chemical composition displaying copper-chloride bonds on theinternal surface of the pores is accessible using ionothermal approaches. Such a material is
impossible to prepare using hydrothermal approaches. Finally hydrogen bonding directing
effect in the ionothermal synthesis will be discussed. This work shows the great potential toadjust the structures and properties of metal organic framework materials via the control ofthe structures and composition of ionic liquids.

References
1. Z.-J. Lin, D. S. Wragg, P. Lightfoot and R. E. Morris* Dalton. Trans. 2009, 5287.
2. Z. Lin*, Y. Li, A. M. Z. Slawin and R. E. Morris Dalton. Trans. 2008, 3898.
- 20 -

AsCA’09

Invited and Oral

3. Z. Lin, A. M. Z. Slawin and R. E. Morris* J. Am. Chem. Soc. 2007, 129, 4880.
4. Z. Lin, D. S. Wragg, J. E. Warren and Russell E. Morris* J. Am. Chem. Soc. 2007, 129, 10334.
5. Z. Lin, D. S. Wragg and R. E. Morris* Chem. Commun., 2006, 2021.

MS2-4

To bridge or not to bridge – carbonyl ligand
configurations in some phosphine and arsine
substituted tricobalt carbon cluster systems
Jim Simpson , C. John McAdam, Brian H. Robinson, and Roderick G. Stanley.
Department of Chemistry, University of Otago, P.O. Box 56, Dunedin, 9054, NEWZEALAND. (jsimpson@alkali.otago.ac.nz)

In simple methinyltricobaltnonacarbonyl clusters, RCCo3(CO)9, six of the carbonyl ligands
occupy equatorial sites, close to the plane of the triangle of cobalt atoms with the the otherthree carbonyl groups approximately orthogonal to that plane in axial positions. Monodentate
or bidentate phosphine or phosphite ligands almost invariably substitute carbonyl groups fromequatorial sites [1,2]. Furthermore, the remaining equatorial carbonyl ligands generally adopt
terminal conformations. A search of the Cambridge Database [3] reveals that carbonyl
bridging of the Co—Co bonds is unusual and is generally found only in situations where theapical substituent R, or the substituting ligands, significantly increase the electron density on
the CCo3 cluster core.
Me

CO
OC
Co

Co

CO

Co
OC

CO

OC

P
Ph
H2C

P
Ph
Ph

Ph
Ph

H2C

P
Ph
CH2

CH3

We have prepared a number of derivatives of methinyltricobaltnonacarbonyl clusters with thepotentially tridentate 1,1,1-tris(diphenylphosphinomethyl)-ethane, CH3C(CH2PPh2)3, (triphos)
ligand. In all cases, the resulting compounds have bridging carbonyl ligands. This paper willreport the structure of these complexes and examine the factors that influence carbonyl
bridging
in
these
and
relatedclustersystems.
Crystalpackinginmethinyltricobaltnonacarbonyl clusters will also be discussed.
Acknowledgements: We thank the New Economy Research Fund; Grant No. UOO-X0808 forsupport of this work and the University of Otago for purchase of the diffractometer
References[1] Matheson, T.W., Robinson, B.H. & Tham, W.S. (1971) J Chem Soc A 1457-1464.
[2] Downard, A.J., Robinson, B.H. & Simpson, J. (1986) Organometallics 5, 1122—1131.
[3] Allen, F. H. (2002). Acta Cryst. B58, 380—388.

- 21 -

AsCA’09

MS2-5

Invited and Oral

Crystal Engineering of Chiral Metal Organic
Frameworks (MOFs) from Tartrates and N-Donor
Spacer Ligands
Pokka K-C. Pang, Herman H-Y. Sung, Ian D. Williams
Department of Chemistry, Hong Kong University of Science and Technology, Clear
Water Bay, Kowloon, Hong Kong, China (pokka@ust.hk)

Ten new crystalline phases have been structurally characterized with formulae related to[Cu(4,4’-bipy)(L-Tar)]. These fall into two isostructural series one is tetragonal with spacegroup P41212 and the other is triclinic, with space group P1 or P-1 depending on whether thetartrate is homo-chiral or not. The structures are open, 3D network polymers, which in thecase of L-tartrate or L-malate lead to chiral MOFs. The 1D channels in the triclinic family areslightly expanded and can contain water, acetic acid or 4,4-bipyridine. The copper II centers
are all square pyramidal with two trans N-donors and three O donors from the carboxylates.
Tartrates are all in μ3,κ3 bridging coordination mode, which form CuTar sheets with different
topological arrangements for the tetragonal and triclinic families. The channels can beenlarged by several angstrom by using more extended N-donor bridges than 4,4-bipy, and thechannel wall functional groups can be altered by varying tartrate stereochemistry from L-Tar
to DL-Tar and meso-Tar, as well as L-or DL-Malate analogues. This varies the extent andspatial location of hydroxyl functionalities pendant to the channel walls and which affect thechannel hydrophilicity. Several phases also show two different channel types with guest
molecule differentiation. Finally the structures are surprisingly robust to ca 150oC andsurvive loss of channel solvent. Selective and enantioselective sorption studies are now being
conducted on these promising MOF materials.

Acknowledgements: The Research Grant Council of Hong Kong is gratefully acknowledged
for financial support of this work (grant 603307)

MS3-1

Current status and future development of neutron
scattering at China Advance Research Reactor
Dongfeng Chen, Yuntao Liu, Hongli Wang, Kai Sun, Meimei Wu
China Institute of Atomic Energy, P. O .Box 275-80, Beijing, 102413, P. R. China(dongfeng@ciae.ac.cn)

Presently, both neutron and X-ray techniques are well developed internationally. For example,
America, Europe and Japan have both the world-class synchrotron sources, such as APS、
ESRF/ DIAMOND、SPRING8，and the world-class neutron sources, such as SNS/HFIR、- 22 -

AsCA’09

Invited and Oral

ILL/ISIS、J-PARC/JRR3. In China, although synchrotron facilities have been built andproperly developed in Beijing, Hefei and Shanghai, neutron scattering research is not welldeveloped due to lack of an advanced neutron source. However, the completion of the China
Advanced Research Reactor (CARR) will push the neutron scattering technique developing ina quick way.
The construction of the 60-MW China Advanced Research Reactor (CARR), a 7.7B¥RMB,
9-year project at the China Institute of Atomic Energy (CIAE), is scheduled to complete withthe reactor reaching criticality at the end of 2009. The Neutron Scattering Laboratory (NSL)of CARR is responsible for the development of a user facility which initially consists of atleast 7 beamlines and endstations. The power of CARR will be 60 MW and 8x1014n/(cm2.s)
unperturbed thermal neutron flux make it standing on an international advanced level.
A suite of instruments, including powder, single crystal, residual stress neutron
diffractometers and a neutron imaging facility will be opened for international and domestic
users from 2009. NSL will focus on following aspects: (A) the methodology study of neutron
scattering technique; (B) the neutron scattering study on the relation between the structuresand properties of novel function materials. (C) studies of the residual stress distribution inengineering components and the methodology of neutron imaging.
References
1. D.F. Chen et al., Physica B 385-386, 966(2006)
2. D.F.Chen et al., J Phys : Condens Matter. 10 , 255-260 (1998)
3. Z.H.Cheng et al., Physical Review B,57( 22) 14299-14309(1998)

MS3-2

Current Status of Shanghai Synchrotron Radiation
Facility
Jianhua He, Zhentang Zhao and Hongjie Xu
Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai, 201800,
China (hejh@sinap.ac.cn)

The Shanghai Synchrotron Radiation Facility (SSRF) is a third generation light source of
3.5GeV electron energy, aimed at producing very brilliant X-ray and soft X-ray beams tofacilitate the researches in life science, material science, earth and environmental sciences,and many other fields. The construction of SSRF started in December of 2004 and wascompleted by the end of April 2009. During the commissioning stage, the main parameters ofaccelerators and beamlines were measured with the conclusion that all the design
specifications of accelerators have been met and all the beamlines have reached therequirements for user operation. The user operation of SSRF started in May of 2009 and it
will provide more than 2000 hours beamtime to over 300 user groups this year.
At present, seven beamlines have been built on SSRF as the phase I beamlines:
1) Macromolecular Crystallography Beamline
2) X-ray Diffraction Beamline
3) X-ray Absorption Fine Structure Beamline
4) Hard X-ray Micro-focusing Beamline- 23 -

AsCA’09

Invited and Oral

5) X-ray Imaging and Biomedical Applications Beamline
6) Soft X-ray Spectromicroscopy Beamline
7) Small Angle X-ray Scattering Beamline
In this talk, an overview of SSRF construction and the commissioning of SSRF Phase I
beamlines will be introduced. Some preliminary experimental results obtained since the user
operation will be shown and the future beamline programs will be introduced as well.

MS3-3

Crystallography and Materials Science at the J-PARC
pulsed spallation neutron facility
Takashi Kamiyama
J-PARC Center / High Energy Accelerator Research Organization, KEK Tokai Campus,
2-4 Shirakata Shirane, Tokai, Naka, Ibaraki 319-1195, Japan(takashi.kamiyama@kek.jp)

The first spallation neutron beam was successfully delivered to 5 neutron instruments on May
30, 2008. At present (June, 2009), 12 instruments are carrying out neutron beam
experiments, among which 8 of them accepts general users. We have four polycrystalline
diffractometers: a super high resolution powder diffractometer (SuperHRPD), a
0.15 %-resolution powder diffractometer of Ibaraki prefecture (iMATERIA), an engineering
diffractometer (Takumi), and a high intensity S(Q) diffractometer (NOVA). In addition, thehigh-pressure community as well as the battery community are planning to constructdedicated polycrystalline diffractometers. A macromolecule single crystal diffractometer has
started commissioning from last year and accept the general user program. Another single
crystal diffractometer for solid-state sciences is proposed. A reflectometer with horizontal
sample geometry has been constructed and commissioning was started with the instrumentused at the KENS facility. We also have three chopper spectrometers with different S(Q,w)
range and resolution. The layout of the experimental hall is shown in Fig. 1(left).
SuperHRPD has recorded the world best resolution with ∆d/d = 0.035 %, which is compatible
with the best SR diffractometer. Figure 1 (right) shows the comparison of two Bragg peaks
measured by the SuperHRPD as well as the KENS Sirius diffractometer; FWHM is three time
improved in SuperHRPD and the tail of each Bragg peak observed in Sirius was not observedin SuperHRPD resulting in 10 times improvement in 1/10-width. This characteristics is rather
effective in both precise crystal structure analyses of complicated materials with large unit
cells as well as detection of tiny structural distortion.

Fig.1 (left) The layout of MLF experimental hall.

(right) The measured Bragg reflection at d = 1.36 Å.

- 24 -

AsCA’09

Invited and Oral

The Current Status of Taiwan Photon Source

MS3-4

Yu Wang2, Mau-Tsu Tang1, Gwo-Huei Luo1, Yaw-Wen Yang1 and Keng S. Liang1
1
National Synchrotron Radiation Research Center, 101 Hsin-Ann Road, Hsinchu
Science Park, Hsinchu 30076, Taiwan, (mautsu@nsrrc.org.tw)
2
Department of Chemistry National Taiwan University, No. 1, Sec. 4, Roosevelt Road,
Taipei, 10617 Taiwan (wangyu@ntu.edu.tw)

A new synchrotron project proposed by NSRRC several years ago, the Taiwan Photon Source,
has obtained government approval in June 2007 with a total budget of ~ US$215M for civil
and accelerator constructions. The project is aimed to build a low-emittance 3 GeV storage
ring for future X-ray research in nano and bio medical sciences. After extensive soil studies
and ground vibration survey, among other infrastructure considerations, the current site of
NSRRC, which houses the 1.5 GeV Taiwan Light Source, has been chosen for the new
synchrotron. The project has now reached some major millstones. The layout of the civil
construction is completed and detail architect design is in progress. The major machineparameters have been fixed: a circumference of 518.4 m with a concentric booster, 24 DBA
cells with six 12m straights and eighteen 7m straights, a lattice with an emittance of 1.6
nm-rad at high-dispersion and 4.9 nm-rad at zero-dispersion mode. The NSRRC is also
soliciting domestic and international scientific proposals for the first-phase beamlines to bebuilt at TPS. In our current schedule, the commissioning of TPS is aimed for late 2013.

Cold Neutron Research Facility at HANARO

MS3-5

Kye Hong LEE1, Young Ki KIM1
1
Korea Atomic Energy Research Institute, 1045 Daedeok-daero, Yuseong-gu, Daejejon
305-353, Korea (khlee@kaeri.re.kr)

The cold neutron research facility (CNRF) project is facing the last year of the project. The
cold source has been installed in the reactor core last June and the performance test of He
refrigerator has been completed. The process system for cold source has been installed and thefirst cold neutron beam will be produced this September. The neutron guide in the reactor hall
has been installed and aligned and the one in the guide hall is being manufactured andinstalled before this September so that the neutron instruments can start the performance tests.
8m SANS has been detached from the beam port in August last year so that the cold neutron
guide in-pile plug, the primary shutter, and the removable shielding have been installed inhigh radiation environment in October last year. REF-V will be disassembled at the end of
this year and be relocated to the guide hall. The procurement request of in-beam motor partand sample table for Bio-REF will be submitted in July this year. For 40 m SANS, thecollimator and vacuum chamber for detectors have been installed and aligned. The dance
floor for Cold-TAS is under construction in the guide hall. The chopper and detector tank for
DC-ToF is being manufactured. The guide bunker in the guide hall has been completed. Hr
SANS is being designed by KIST and will be completed by 2010.
Currently, 7 neutron beam instruments are operating. Thermal-TAS and Bio-diffractometerare being installed in the reactor hall. Hence, there will be 16 neutron beam instruments in2012 while DC-ToF has a budget problem to secure 352 PSD and detector circuits. Theinternational HANARO Symposium will be held in November 2010 to celebrate the- 25 -

AsCA’09

Invited and Oral

completion of CNRF project.

Fig. CNRF Project Group in the guide hall

MS3-6

New Facilities for Australian Research: The
Australian Synchrotron and the OPAL Research
ReactorRichard F. Garrett
ANSTO, Private Mail Bag 1, Menai, NSW, 2234, Australia

The last 2 years have seen unprecedented new opportunities for Australian science with the
opening of two world class major user facilities: the Australian Synchrotron and the OPAL
research reactor. Both facilities opened in 2007 have been quickly embraced by the Australianand international research communities with both having well over one thousand registeredusers.
The Australian Synchrotron is a 3 GeV third generation facility, located in Melbourne,
Victoria. Its initial suite of nine beamlines include dedicated Protein Crystallography, EXAFS,
powder diffraction, SAXS/WAXS, micro-beam Infra-red and soft X-ray spectroscopy
beamlines. A high energy beamline dedicated to imaging and medical therapy is underconstruction. The OPAL research reactor is a 20 MW swimming pool design reactor with avery compact core delivering high neutron flux. It is located at ANSTO in Sydney, New South
Wales, and is designed not only for neutron beam research, but also for radioisotope
production and irradiation services. It currently operates 7 instruments on thermal and cold
sources beams dedicated to powder diffraction, single crystal diffraction, residual stress andstrain, SANS, reflectivity and triple axis inelastic scattering, with two additional instruments
under construction.
The capabilities of these two new facilities and plans for future beamlines and instruments
will be presented. Some research highlights will also be shown.

- 26 -

AsCA’09

MS4-1

Invited and Oral

Structure of the bacterial flagellum and themechanism of its self-assembly
Katsumi Imada
Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita,
Osaka 565-0871, Japan (kimada@fbs.osaka-u.ac.jp)

Gram-negative bacteria, such as E. coli and Salmonella, swim by rotating a helicalfilamentous organelle called the flagellum. The flagellum rotates at a speed of 200 to 300 Hz
driven by a reversible rotary motor embedded in the cell membrane at the base of the filament.
The motor is powered by the electrochemical potential difference of proton across the cell
membrane. The torque is generated by rotor-stator interactions coupled with protontranslocation through the channel within the stator composed of MotA and MotB. About ten
stators are assembled around the rotor and anchored to the peptidoglycan (PG) layer, about
100 Å away from the hydrophobic surface of the cell membrane, by the
peptidoglycan-binding (PGB) domain of MotB. The stators dynamically assemble to anddisassemble from the functional motor, and proton translocation is activated only when thestator is installed.
The flagellum is a huge molecular assembly made of 20 to 30 thousands of subunits of about
30 different proteins. The rotational part of the flagellar structure can be divided into twoclasses, the basal body rings and the tubular axial structure. Since the axial structure extends
from the cytoplasmic membrane, its component proteins must be exported from the cytoplasm.
The protein subunits are synthesized in cytoplasm, are translocated into the central channel ofthe growing flagellum by the flagellar type III protein export apparatus, which is composed ofsix transmembrane proteins (FlhA, FlhB, FliO, FliP, FliQ, FliR) and three soluble components(FliH, FliI, FliJ), and then travel through the channel to the growing end for theirself-assembly.
Recent structural studies on the stator proteins have provided a possible molecularmechanisms of the motor activation coupled with the stator assembly. The structural studies
on the flagellar type III protein export apparatus have demonstrated a remarkable similarity
between the the flagllar export apparatus and F0F1-ATP synthase. I will show the recent
progress of the structural study of the bacterial flagellum and discuss the molecularmechanisms of flagellar self-assembly and the motor activation.

Understanding Cytokine Receptor SignallingMS4-2

Guido Hansen1, Tim R. Hercus2, Jack King-Scott1, Angel F. Lopez2, Michael W.
Parker2
1
St. Vincent’s Institute of Medical Research, 9 Princes Street, Fitzroy, Melbourne,
Victoria 3065, Australia (mparker@svi.edu.au)
2
Division of Human Immunology, Centre for Cancer Biology, Hanson Institute,
Adelaide, South Australia 5000, Australia

The GM-CSF, IL-3 and IL-5 family of cytokines regulates the survival, proliferation,differentiation and functional activation of hematopoietic cells. 1 These same cytokines havealso been implicated in multiple pathologies resulting from the excessive or aberrant- 27 -

AsCA’09

Invited and Oral

expression of the cytokine or their receptors, in conditions such as arthritis, asthma,autoimmunity and leukaemia. The receptors for these cytokines are expressed on the surfaceof hematopoietic cells and comprise a cytokine-specific alpha subunit and a beta subunit thatis common to all three receptors. The alpha subunit binds cytokine with low affinity forming acomplex that is able to recruit the beta subunit, converting the binding to a high affinity state.
This promotes dimerisation of both subunits which in turns leads to receptor activation
although the mechanisms of receptor activation are still quite poorly understood.
We have recently determined the structure of a GM-CSF:receptor ternary complex,
representing the first structure of an "activated" receptor of this family of cytokines.2
Inspection of the structure reveals exciting insights into the mechanism of receptor activationand provides a unifying molecular explanation for the diverse functional properties of related
cytokine:receptor systems.
References
1.
2.

Hercus, T.R., Thomas, D., Guthridge, M.A., Ekert, P.G., King-Scott, J., Parker, M.W. & Lopez, A.L.
(2009) The GM-CSF receptor: linking its structure to cell signaling and its role in disease. Blood, inpress.
Hansen, G., Hercus, T.R., McClure, B.J., Stomski, F.C., Dottore, M., Powell, J., Ramshaw, H.,
Woodcock, J.M., Xu, Y., Guthridge, M., McKinstry, W.J., Lopez, A.F. & Parker, M.W. (2008) The
structure of the GM-CSF receptor complex reveals a distinct mode of cytokine receptor activation.
Cell, 134, 496-507.

MS4-3

Effector recognition of Rab and Arf family small
GTPases in vesicle transport and membrane
remodeling
Soichi.Wakatsuki
Photon Factory, IMSS, KEK, Tsukuba, Japan (soichi.wakatsuki@kek.jp)

Vesicle transport is orchestrated by a network of dynamic protein-protein interactions which
present as challenging targets for structural biology. Rab and Arf family proteins are involvedin various stages of vesicle transport by interacting with effectors which are often multidomain proteins whose domains make specific but transient interactions. The small GTPases
are activated by guanine nucleotide exchange factors (GEF). Crystallographic studies oncomplexes between plant Rab5 GTPases (Ara6&7) and their GEF, Vps9a, in various stages of
GDP recognition and its release reveal the atomic details of the activation mechanism. In
particular, there is a pivoting motion of the plant Rab5 by about 20 degrees when thecomplexes are superimposed on Vps9a, which might account for the release of GDP by
Vps9a. By inspecting the binding mode of the nucleotide and the available space between thetwo proteins in the complex structures, a high throughput screening method has been
established. Some 14,000 compounds have been screened for activation or inhibition of the
GEF function, which yielded dozens of candidates and further investigation is underway.
Once activated, the GTP-bound Arf or Rab can interact with a number of effectors for specificfunctions such as cellular localization, control of vesicle budding or fusion, and membrane
remodeling. The effector/small GTPase specificities are achieved in most cases by the surface- 28 -

AsCA’09

Invited and Oralarea including Switches I/II and interswitch antiparallel beta sheet. This will be illustratedusing crystallographic examples: (1) Arf1 in complex with the N-terminal GAT domain of
GGA, (2) Rab11 in complex with the Rab11-binding domain (RBD) of FIP3/Arfophlin-1,
dual effector for Rab11 and Arf5/6, and (3) Rab27a with Exophilin4/Slp2-a, a Rab27 effector
responsible for melanosome and secretory granules. In these cases, the interswitch beta sheetalign parallel to the helices of the effectors, which will orient the effector helices
perpendicular to the membrane to reach other partner proteins in the cell. On the other hand,
there are cases where the interswitch beta sheet and effector helices lie orthogonal to eachother. One remarkable example is a complex between a GTPase and a BAR domain. The
complex structure shows a curved surface ideally shaped for bending the target membraneusing both the concave surface of the BAR domain as well as the small GTPase itself.

MS4-4

Structural Basis of Transcription: Backtracked RNAPolymerase II
Dong Wang, Roger D. Kornberg
Department of Structural Biology, Stanford University School of Medicine, FairchildBldg. D117, 299 Campus Dr. West, Stanford, CA 94305-5126 (dongwang@stanford.edu)

Transcription is the first step of gene expression. During transcription, RNA polymerases
oscillate between three stable states, two of which, pre- and post-translocated, werepreviously subjected to X-ray crystal structure determination. Here we report the crystal
structure of RNA polymerase II in the third state, the reverse translocated, or “backtracked”
state, which completes the picture of the transcribing enzyme [1].
Backtracking enhances the fidelity of transcription by enabling proofreading of the nascenttranscript. It is frequently caused by encountering a DNA lesion or incorporating amismatched nucleotide. The defining feature of the backtracked structure is a binding site forthe first backtracked nucleotide. This binding site is occupied in case of nucleotide
misincorporation in the RNA or damage to the DNA, and is termed the “P” site, because itsupports proofreading. Defined stable structure of RNA polymerase II backtracked by one
residue supports the idea that there is an equilibrium between forward and backward motion
during transcription. It also confirms that backtracking by one residue is favorable whereas
going back over several residues is not.. The work we present here provides a structural
framework for understanding the essential transcription proofreading process.
References[1] Wang, D., Bushnell, D. A., Westover, K. D., Huang, X. H., Levitt, M. & Kornberg, R. D. Structural
basis of transcription: Backtracked RNA polymerase II at 3.4 Å resolution. Science, 324, 1203-1206(2009)- 29 -

AsCA’09

Invited and Oral

Structure of RNA-guided RNA Modification Enzymes

MS4-5

Keqiong Ye, Ling Li, Jingqi Duan, Ru Jia, Jinzhong Lin, Minghua Ju, Jin Peng,
Anbi Xu, and Liman Zhang
National Institute of Biological Sciences, Beijing 102206, China(yekeqiong@nibs.ac.cn)

Over one hundred types of chemical modification are introduced at specific sites of cellular
RNAs after their transcription. These modifications, which greatly increase the chemical
diversity of RNA, are generally beneficial and sometimes even critical for the structure andfunction of host RNAs. RNA modifications are normally carried out by individual protein
enzymes. However, an exception is the large number of pseudouridine and 2'-O-methylated
nucleotides in rRNAs, snRNAs, and tRNAs that are synthesized by H/ACA and C/D
RNA-protein complexes (RNPs), respectively. In each such complex, a distinct guide RNA
belonging to the H/ACA or C/D RNA family determines the substrate specificity bybase-pairing with the substrate around the modification site. We are trying to understand themolecular mechanism by which guide RNAs direct RNA modification, with the main goal todetermine the crystal structure of H/ACA and C/D RNP and their complex with substrateRNA.
We previously solved the structure of an entire substrate-free H/ACA RNP from Pyrococcus
furiosus to 2.3 Å (1). The RNP complex comprises a 65-nucleotide H/ACA RNA,
pseudouridine synthase Cbf5 and accessory proteins L7Ae, Gar1 and Nop10. In the RNP
structure, the H/ACA RNA directly associates with Cbf5, Nop10 and L7Ae and places the
bipartite guide sequences, in a flexible conformation, near the active site. Gar1 does not bindRNA, yet sequesters a thump loop of Cbf5. To understand the enzyme in action, we also
recently determined the crystal structure of H/ACA RNP with a 14-nt substrate bound at theactive site cleft, revealing the mechanism of substrate recruitment (2). Substrate binding leads
to a reorganization of a preset pseudouridylation pocket and an adaptive movement of the
PUA domain and the lower stem of the H/ACA RNA. Moreover, the thumb loop flips fromthe Gar1-bound state in the substrate-free RNP structure to tightly associate with the substrate.
Mutagenesis and enzyme kinetics analysis suggest a critical role of Gar1 and the thumb in
substrate turnover, particularly in product release.
In archaea, a C/D RNA assembles with L7Ae, Nop5, and the methyltransferase fibrillarin intoa specific modification enzyme. We have determined the crystal structure of an archaeal C/D
RNP composed of all three core proteins and an engineered half guide RNA to 4 Å, as well as
two Nop5 protein substructures at higher resolution (3). The C/D RNP structure reveals that
the C-terminal domains of Nop5 in the dimeric complex provide symmetric anchoring sites
for two L7Ae-associated kink-turn motifs of the C/D RNA. A prominent protrusion in Nop5
appears to be important for guide RNA organization and function, and for discriminating thestructurally related U4 snRNA. Multiple conformations of the N-terminal domain of Nop5
and its associated fibrillarin in different structures indicate the inherent flexibility of thecatalytic module, suggesting that a swinging motion of the catalytic module is part of the
enzyme mechanism. Our results provide insight into the overall organization and mechanismof action of C/D RNA-guided RNA methyltransferases.
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Invited and Oral

References
1.
2.
3.

Li, L. and Ye, K. Crystal structure of an H/ACA box ribonucleoprotein particle. Nature 443, 302-307(2006).
Duan, J., Li, L., Lu, J., Wang, W. and Ye, K. Structural mechanism of substrate RNA recruitment in
H/ACA RNA-guided pseudouridine synthase. Mol Cell. 34:427-439 (2009)
Ye K., Jia R., Lin J., Ju M., Peng J., Xu A. and Zhang L. Structural organization of box C/D
RNA-guided RNA methyltransferase. PNAS (In press).

RNA-protein interactions in the core domain of
spliceosomal U4 snRNP

MS4-6

Adelaine K.W. Leung1, 2, Jade Li1, Kiyoshi Nagai1
1Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge,
CB2 0QH, U.K. (jl@mrc-lmb.cam.ac.uk)
2
Department of Neurobiology, Harvard Medical School, 220 Longwood Avenue, Boston,MA, 02115, USA (Adelaine_Leung@hms.harvard.edu)

The spliceosome responsible for processing pre-mRNA to mRNA is assembled from U1, U2,
and U4/U6-U5 snRNPs (small nuclear ribonucleoprotein particles). The core domain of the
U1, U2, U4 and U5 snRNPs is formed when seven Sm proteins (B/B’, D1, D2, D3, E, F andG) are assembled into a ring around the Sm site sequence within the particular snRNA.
Particle-specific proteins are added to this core to produce mature snRNPs.
The Sm proteins share a conserved sequence motif in two segments, called Sm1 and Sm2,
joined by a linker of variable length. We have reconstituted and crystallised the human U4
snRNP core domain comprising the U4 snRNA Sm site with flanking helices and the seven
Sm proteins. Crystals belong to space group P31 with 12 copies of the core domain per
asymmetric unit, related by approximate 222 rotational ncs and 3-fold translational ncs in thea,b-plane. Using MAD with SeMet labelling of the EFG proteins, the structure was solved
initially in P6122 in a reduced unit cell containing one copy per asymmetry unit, byapproximating the non-crystallographic symmetries as crystallographic. A partial model
was built and used for molecular replacement into the true cell.
The structure at 3.6Å resolution shows the seven Sm proteins forming a closed ring throughH-bonding across the Sm1, Sm2 motifs all the way round, and the snRNA threaded throughthe central pore. In the central pore the seven bases of the U4 Sm site (AUUUUUG) aresplayed out, each base bound in a unique pocket formed primarily by one protein. RNA
helices flanking the Sm site are located on opposite faces of the ring; the 5’ RNA is on theface with the N-terminal protein helices, while the 3’ RNA after passing through the ringmakes sequence-non-specific interactions with the Sm1-Sm2 linker loops. Compared with theU1 snRNP structure at 5.5Å resolution [1], peripheral regions of the Sm proteins show
RNA-dependent conformational differences. These differences, in addition to the snRNAsequence, may provide selectivity for the addition of particle-specific proteins.
References[1] D A Pomeranz Krummel, C Oubridge, A K W Leung, J Li & K Nagai (2009) Nature 458: 475-480.
Crystal structure of human spliceosomal U1 snRNP at 5.5 Å resolution.
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MS5-1

Invited and Oral

Recent Progress in X-ray Charge Density Studies ofAdvanced Materials
Bo Brummerstedt Iversen
Centre for Materials Crystallography, Centre for Energy Materials and iNANO,
Department of Chemistry, University of Aarhus, DK-8000 Århus C, Denmark(bo@chem.au.dk)

During the last decade the X-ray charge density method has been revitalized due to majoradvances in the experimental methods with the availability of area detectors, intense shortwavelength synchrotron radiation and stable helium cooling devices. The use of area detectors
has greatly increased the data collection speed, and this has made the technique a generally
applicable analytical tool. Furthermore, comparative ED studies between related materials are
now possible, which may provide insights that cannot be obtained in single system studies.
While area detectors primarily produce speed, the latter two developments, synchrotrons andhelium cooling devices, produce significant improvements in data accuracy. However, theintense short wavelength synchrotron radiation also has made it possible to tackle
experimental charge density studies on complex molecular systems containing heavy atoms
and on weakly diffracting microcrystals. The talk will illustrate the application of charge
density methods in studies of magnetic coordination polymers [1], polynuclear transition
metal systems [2] and photomagnetic systems [3].
References:[1] (a) Clausen, H. F.; Overgaard, J.; Chen, Y. S.; Iversen, B. B., J. Am. Chem. Soc. 2008, 64, 7988-7996.
(b) Poulsen, R. D.; Jørgensen, M. R. V.; Overgaard, J.; Larsen, F. K.; Morgenroth, W.; Graber, T.; Chen,Y.; Iversen, B. B. Chem. Eur. J. 2007, 13, 9775 – 9790. (c) Poulsen, R. D.; Bentien, A.; Chevalier, M.;
Iversen, B.B., J. Am. Chem. Soc. 2005, 127, 9156-9166[2] (a) Overgaard, J.; Schulman C. J.; Stasch. A.; Iversen, B. B. J. Am. Chem. Soc. 2009, 131, 4208–4209.
(b) Poulsen, R. D; Overgaard, J.; Schulman, A.; Østergaard, C. D.; Murillo, C. A.; Spackman, M. A.;
Iversen, B. B. J. Am. Chem. Soc. 2009, 131, 7580–7591. (c) Overgaard, J.; Clausen, H. F.; Platts, J. A.;
Iversen, B. B. J., J. Am. Chem. Soc. 2008, 130, 3834-3843. (d) Overgaard, J.; Larsen, F. K.; Schiøtt, B.;
Iversen, B. B. J. Am. Chem Soc. 2003, 125, 11088-11099[3] Svendsen, H.; Overgaard, J.; Chevallier, M.; Collet, E.; Iversen, B. B. Angew. Chem. Intl. Ed. 2009, 48,
2780-2783

Non-linear Optical Properties and Spin Densities from
X-ray Charge Density Measurements

MS5-2

Dylan Jayatilaka1, P. Munshi2, M.J. Turner1, J.A.K. Howard3, M.A. Spackman1
1
University of Western Australia, Perth, Western Australia(dylan.jayatilaka@uwa.edu.au)
2
Universite Henri-Poincare, Nancy, France
3
Durham University, Durham, United Kingdom

According to the Hohenberg-Kohn theorem, the electron density determines the electronicenergy and hence all electronic properties of a system. But, in practice, how do we use theelectron density to get these properties?
In the X-ray constrained wavefunction approach, a model wavefunction is constrained to- 32 -

AsCA’09

Invited and Oralreproduce the X-ray structure factors from a charge density measurement. Electronic
properties can then be calculated from this “fitted” wavefunction. The constrained
wavefunction approach combines ab initio quantum chemistry and X-ray diffraction
techniques.
In this talk I will describe the results for obtaining refractive indices, non-linear opticalproperties [1], and even spin densities from the X-ray constrained wavefunctions [2] applied
to molecular crystals. The properties will be compared to measurements from independent
electro-optical and polarised neutron diffraction experiments.
References
1.
2.

D. Jayatilaka, P. Munshi, M.J. Turner, J.A.K. Howard, M.A. Spackman, Phys. Chem. Chem. Phys. 11,
7209-7218 (2009)
D. Jayatilaka, Phys. Rev. Lett. 80, 798-801 (1998); D.J. Grimwood and D. Jayatilaka, Acta. Cryst A 57,
76-86 (2001); D. Jayatilaka and D.J. Grimwood, ibid, 87-100 (2001)

MS5-3

Exploring Halogen -Halogen Interactions via Charge
Density Analysis
T. N. Guru Row
Solid State and Structural Chemistry Unit, Indian Institute of Science, Bangalore
560012,India (ssctng@sscu.iisc.ernet.in)

The presence of halogen…halogen intermolecular interactions and their capability ingenerating supramolecular assemblies has been studied extensively in recent years. Theinteractions are represented as C-X1···X2-C moieties (where X1 and X2 are halogens and thegeometry is defined as type I, type II and type III based on the values of the angles θ1=CX1···X2 and θ2=X1···X2-C; distance Rij=X1···X2)1. These contacts are classified as either
attractive or repulsive based on the geometry. However interactions involving organic fluorine
have remained controversial issue. Experimental2 and theoretical3 charge density analysis will
provide the necessary inputs to the understanding of the nature of such halogen…halogen
contacts. Several recent examples of charge density analysis on some molecular crystals
which display all three types of Halogen –Halogen interactions, in particular C-Cl…Cl -Cand
C-F…F-C will be presented in this talk bringing out the evaluation of the nature of suchinteractions in terms of electron density related properties like net charges, dipole moments
and other one electron properties.
References
1. (a) K. Gnanaguru, N. Ramasubbu, K. Venkatesan, and V. Ramamurthy, J. Org.Chem., 1985, 50, 2337.
(b) G. R. Desiraju and R. Parthasarathy, J. Am. Chem.Soc. 1989, 111, 8725.
(c) N. Ramasubbu, R. Parthasarathy, and P. Murray-Rust, J. Am. Chem. Soc., 1986, 108, 4308.
2. A. Volkov, P. Macchi, L. J. Farrugia, C. Gatti, P. Mallision, T. Richter and T. Koritsanszky, XD2006,
2006.
3. R. Dovesi, V. R. Saunders, C. Roetti, R. Orlando, C. M. Zicovich-Wilson, F. Pascale, B. Civalleri,
K. Doll, N. M. Harrison, I. J. Bush, Ph D’Arco and M. Linuell, CRYSTAL06, University of Torino, 2006.

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MS5-4

Invited and Oral

Challenge to Atomic Orbital Visualization by 0.2A
Resolution Synchrotron Radiation Single Crystal
Experiment
Hiroshi Sawa, Eiji Nishibori, Shinobu Aoyagi
Department of Applied Physics, Nagoya University, Nagoya, 464-8603, Japan(z47827a@cc.nagoya-u.ac.jp)

An ultimate goal of the structure analysis is determination of the charge density distribution in
the unit cell of crystal. There are various types of accurate structural analysis method, themulti-pole refinement, anharmonic thermal factor refinement, Bader topological analysis, andmaximum entropy method. If you use these analyses, common attention to experimental
conditions of X-ray diffraction is necessary. Those conditions are high statistical accuracies
and high Q resolution in diffraction data.
The high stability of X-ray is obtained by the Top-up driving mode in SPring-8. Almost
constant ring current produces extremely steady X-ray to the diffraction experimental systembecause the thermal loading of an optical component may become constant. A new large
cylindrical camera was set up as an X-ray diffractometer for a single crystal at the beamline,
BL02B1/SPring-8. In conceptual design, the image plate (IP) was selected as the detector,
because IP detector not only takes care until high 2θ angle for one shot but also statisticallyobserve the reliable data.
The functional transition metal complexes are currently attractive in the investigation ofdegree of freedom of d-orbital and charge. The statistically reliable and high resolution data isdemanded to lead the exact orbital resolution of d-electron configuration. The resolution of
0.2A is necessary to determine the d-orbital that differs from p-orbital and occupies a narrow
range of the space. These conditions are achieved by the high stability and parallel of asynchrotron radiation X-ray.
Recently, we have carried out various types of accurate structural studies. The main targetedmaterials are strong correlated transition metal oxides, organic conductors, endohedral
fullerenes, and so on. The single crystal data of multiferroic transition metal oxide has been
observed using high energy X-ray enough for order resolution of d-electron configuration.
The method of orbital resolution was developed by the combination of maximum entropy
method and multi-pole analysis.

MEM Electrostatic Potential Imaging

MS5-5

Hiroshi Tanaka
Dept. of Materials Science, Shimane University 1060, Nishi-kawatsu-cho, Matsue,
Shimane, 690-8504, Japan(h.tanaka@riko.shimane-u.ac.jp)

Recently, we developed a new method evaluating the electrostatic potential from x-ray
diffraction data by using the MEM (Maximum Entropy Method) [1]. In this method,electrostatic potential is divided into the contribution from nuclear charge and that fromelectron charge. The former is estimated by ordinary Ewald's method, while the later is- 34 -

AsCA’09

Invited and Oralevaluated by the MEM charge density in the reciprocal lattice (structure factor). It is a key
point that we can soundly extrapolate the structure factor by MEM up to the reciprocal lattice
points needed for the convergence of the calculation.
The electrostatic potential is sensitive to the number of valence electrons and/or electron
polarization at atomic level. Then, our method is useful for the analysis of ionic crystals suchas ferroelectric [1], charge transfer[2], and charge ordering materials [3].
For example, Fig. 1 shows the isosurface of charge density for Nd0.5Sr0.5MnO3 colored by the
amplitude of electrostatic potential in gray scale. It is known that this material shows chargeorder transition at 150K. After the transition, the Mn ions are separated into the Mn3+ ions andthe Mn4+ ions. It is clearly shown in the figure that the electrostatic potential is higher aroundthe Mn4+ ions than around Mn3+ ions corresponding to the difference in the valence between
the two ions.

Fig.1 Isosurface of charge density for Nd0.5Sr0.5MnO3 colored by the amplitude of electrostatic potential
in gray scale from 0.5 e/Å (black) to 4.0 e/Å (white).

Acknowledgements:This work was financially supported by the X-ray Free Electron Laser
Utilization Research Project and by a Grant-in-Aid for Scientific Research from the Ministryof Education, Culture, Sports, Science and Technology, Japan.
References[1] H. Tanaka, Y. Kuroiwa, and M. Takata, Phys. Rev. B74, 172105 (2006).
[2] K. Katoh, et al., J. Phys. Soc. Jpn. 76, 123602 (2007).
[3] K. Katoh, et al., Phys. Rev. B77, 081101 (2008).

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AsCA’09

Invited and Oral

Photo-induced structure determination and electron
density study by MEM of Spin Crossover complex[Fe(abpt)2(NCS)2]

MS5-6

Che Hsiu Shih1,2, Chou Fu Sheu3, Kunihisa Sugimoto2,4, Jungeun Kim2,4, Kenichi
Kato2,4, Yu Wang3, Masaki Takata1,2,4
1. University of Tokyo, 7-3-1 Hongo Bunkyo-kyu, Tokyo, Japan. 113-8654.
2. RIKEN, Harima, Japan.
3. National Taiwan University, Taipei Taiwan.
4. Japan Synchrotron Radiation Research Institute (JASRI)/SPring-8.
(karu@spring8.or.jp)

Molecular multi-stability has attracted an increasing interest in the context of functional
materials. To study the relationship between crystal structure and functions allows gaining
new insights into novel material design. Spin Crossover (SCO) materials are one of lightswitchable molecular system. We have investigated the photo-induced (PI) switching process
in SCO complex Fe(abpt)2(NCS)2 (abpt = 4-amino-3,5 bi(pyridine) 1,2,4-triazole) through the
crystal structure determination and its charge density study by Maximum Entropy Method(MEM). For the precise structure analysis of photo-induced phase transition, we collected thehigh resolution data at BL02B1/SPring-8. The PI spin transition of Fe(abpt)2(NCS)2 was takenplace under 532nm green light laser irradiation from low spin (LS) to high spin (HS) at
cryogenic temperature. We could hold sufficiently stable HS state by PI at 35 K using heliumgas flower cooling device during data collection. The single crystal data was collected on the
maximum resolution of 0.6 Å (Rint=3.49%) using high brilliant and stable synchrotron
radiation X-ray source and large cylindrical Image Plate camera, and the data was refined to
R1=3.35% , GOF =1.054 for 13094 unique observed reflections. The Light Induced Excited
Spin State Trapping (LIESST) effect gives the extension of the Fe-N bond length by ~0.2 Å
based on electronic configuration transition eg0 t2g 6(LS) → eg2 t2g 4 (HS). The results of
SQUID and infrared spectroscopy are reasonable with precise structure analysis. The
difference of electron density distribution between ground state and PI meta-stable state could
be directly visualized by MEM. In our presentation, we will show the direct observation ofelectron density distribution by MEM and discuss about the electron configuration between
GS and PI meta-stable states.
Keywords: LIESST, photo-induced single-crystal-single-crystal-transformation. MEM charge
density

MS6-1

Recent Developments in Coherent Diffractive Imaging
Instrumentation and Applications
Andrew G. Peele1,2
1
Department of Physics, La Trobe University, 3086, Australia (a.peele@latrobe.edu.au)2Australian Research Council, Centre of Excellence for Coherent X-ray Science

Coherent diffractive imaging (CDI) has the potential to become an important high resolution
microscopy technique. Potential applications include projection and 3D imaging of biologicaland advanced materials samples. While much of the impetus for the development of CDI has
come from the promise of high brightness from a new generation of x-ray source – the x-ray- 36 -

AsCA’09

Invited and Oral

free electron laser – there are many applications possible at 3rd generation synchrotron
sources.

Keyhole FCDI image of a fusebay region in an integrated circuit with resolution at 20 nm. Image from B.
Abbey et al “Quantitative Coherent Diffractive Imaging of an Integrated Circuit at a Spatial Resolution of
20 nm” Appl. Phys. Lett. 93, 214101, (2008)

CDI relies on the detection of photons scattered to relatively high angles (at least in a small
angle scattering sense). At a 3rd generation source, where long exposures are required tocollect sufficient high angle photons, it is important to develop very efficient data collection
and analysis methods. In terms of analysis methods relevant problems include overcoming
stagnation issues in the iterative solution methods used to phase the measured diffraction
patterns and overcoming the requirement for the sample to be small and isolated.
Introducing phase curvature into the illumination alters the nature of the diffraction pattern by
removing the translational invariance seen in the far field diffraction pattern for plane wave
illumination. In this “Fresnel” CDI method we have been able to show that stagnation isgreatly ameliorated. In addition, the known illumination function can be used to define anisolated region within a larger sample – allowing “Keyhole Fresnel CDI” to be used to mosaic
an image of extended objects. A further advantage includes the ability to compete against thedegrading effects of poor spatial coherence by using appropriately chosen illuminating
curvature. We also describe our results dealing with the case of illumination that is not simply
monochromatic, as can be seen in a single XFEL pulse.
The application of these methods requires the development of a new class of instrument withextremely strict tolerances on the relative stability between the optics producing the phasecurvature in the illumination and the sample. We describe the dedicated endstation at
beamline 2-ID-B at the Advanced Photon Source that has been developed to meet these needs.
We demonstrate our successful application of our instrumentation and methods to the imagingof biological and materials samples and discuss the implications of our results for imaging
protein structures.

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Invited and Oral

Visualization of Bio-Structures Using Coherent X-Ray
Diffraction

MS6-2

Yoshinori Nishino1, Kazuhiro Maeshima2, Naoko Imamoto3, Ryuta Hirohata4,
Eiichiro Matsubara4, Yukio Takahashi5, Tetsuya Ishikawa1
1
RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan(nishino@spring8.or.jp, ishikawa@spring8.or.jp)
2
Structural Biology Center, National Institute of Genetics, Shizuoka 411-8540, Japan(kmaeshim@lab.nig.ac.jp)
3
Cellular Dynamics Laboratory, RIKEN, Saitama 351-0198, Japan(nimamoto@riken.jp)
4
Department of Materials Science and Engineering, Kyoto University, Kyoto 606 8501,
Japan (e.matsubara@materials.mbox.media.kyoto-u.ac.jp)
5
Graduate School of Engineering, Osaka University, Osaka 565-0871, Japan(takahashi@prec.eng.osaka-u.ac.jp)

We report our studies on X-ray diffraction microscopy (XDM) for biological samples. XDM
requires no lenses, and a sample image is directly reconstructed from the coherent diffraction
data. It is ideal X-ray phase-contrast imaging with no contrast degradation due to lenses.
XDM is especially useful for observing internal structures of thick objects, such as cells orcell organelles, thanks to high penetrating power of X-rays.
The first biological application of XDM was for Escherichia coli bacteria cells [1]. Theinternal distribution of the proteins stained with manganese oxide was two-dimensionallyimaged. In the image reconstruction, the Fourier transform of a lower-resolution sample
image observed under a full-field soft X-ray transmission microscope was used to make up
for missing coherent X-ray diffraction data near-forward direction. The missing data problem
was later solved by improvements of microscope instruments to reduce parasitic scattering
noise [2,3] and also by improvements of the phase retrieval algorithm, e.g. the iterative
normalization algorithm [4]. These improvements have made it possible to reconstruct asample image only from the coherent diffraction data.
Recently, we succeeded in observing an unstained human chromosome in three dimensions[5]. This is the first three-dimensional electron density mapping of a cell organelle by using
hard X-rays. It is important because XDM is directly connected with X-ray crystallography,
which is currently the most powerful method of the atomic structure analysis for proteins. The
observed images reveal an axial structure with high electron-density in the chromosome,which other microscopic methods have been unable to visualize under unstained condition.
Such mesoscopic-scale structures as cell organelle have been difficult to be observed,
although molecular structures of their components like DNA and histone proteins could bestudied by X-ray crystallography or electron microscopy. Our result experimentallydemonstrates the high imaging ability of coherent X-ray diffraction for unstained biological
specimens, which are almost transparent to X-rays, opening a novel and strong means of
exploring cellular structures.
References[1] Miao J., Hodgson K.O., Ishikawa T., Larabell C.A., LeGros M.A., Nishino, Y., Proc. Natl. Acad. Sci.
USA 100, 110 (2003).
[2] Nishino Y. et al., IPAP Conference Series, Proceeding of 8th International Conference on X-Ray
Microscopy 7, 386 (2006).
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[3] Nishino Y. et al., IPAP Conference Series, Proceeding of 9th International Conference on X-Ray
Microscopy, to be appeared.
[4] Nishino Y., Miao J., Ishikawa T., Phys. Rev. B 68, 220101 (2003).
[5] Nishino Y., Takahashi Y., Imamoto N., Ishikawa T., Maeshima K., Phys. Rev. Lett. 102, 018101 (2009).

MS6-3

Phase imaging using a liquid cell in a transmission
x-ray microscope
Gung-Chian Yin

MS6-4

Improved Accuracy Laue Neutron Diffraction
Ross Piltz, Alison Edwards
Bragg Institute, ANSTO, PMB 1, Menai NSW 2234, Australia (rop@ansto.gov.au)

Koala is a neutron Laue diffractometer designed for rapid data collection from single crystals
with primitive cell lengths up to 30Å. The high speed is achieved using a cylindricalimage-plate detector with 3-π coverage and a white beam via super-mirror guides from athermal moderator. While the use of image-plates and a white beam ensures rapid datacollection, it also creates several problems in obtaining accurate intensities for structurerefinement. Structure refinements using this technique commonly have wR2 about 15% due tosystematic errors via inadequately corrected intensity data.
An improved set of intensity corrections has been devised based on the wavelength, spatial,
and time dependent behavior of neutron-sensitive image-plates. The intensity correction also
includes wavelength dependent absorption and extinction effects. The result is a 50%
reduction in wR2 for model systems, greater accuracy for atomic parameters, and greater
ability to distinguish between competing structural models.
A comparison of structural refinements will be presented for well characterized samples aswell as a selection of user program samples. The latter provide a snap shot of current Koala
experiments: resolving oxidation states potentially misassigned due to the presence of hydride;hydrogen position and motion for supramolecular framework compounds; superlattice
structure of BiRe2O6; comparison of the Ba(Re,Y,Tb)Co4Ox family of materials.

Development and Application of Neutron 2D-Counterfor Crystal and Magnetic Structure Analysis

MS6-5

Y. Noda1, C-H. Lee2, M-K. Moon2, S-A. Kim2, Y. Ishikawa1, H. Kimura1 and R.
Kiyanagi1
1
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University,
2-1-1 Katahira, Aobaku, Sendai 980-8577, Japan (ynoda@tagen.tohoku.ac.jp)
2
HANARO, Korea Atomic Energy Research Institute, 150 Deokjin-dong, Yuseong-gu,
Daejeon 305-353, Korea (leech@kaeri.re.kr)

Neutron single crystal structure analysis is very powerful tool to investigate accurate positionof light atoms such like Oxygen and Hydrogen. Neutron is also very sensitive for magnetic- 39 -

AsCA’09

Invited and Oralstructure. Thus, neutron single crystal experiment is indispensable for crystal and magnetic
structure analysis for complicated magnetic system in multiferroics. The only difficulty is thelack of efficiency of the measuring time. Usually it requires long beam time, and sometimes,
it is impossible to carryout.
In order to overcome such low efficiency on single crystal neutron experiments, we havedeveloped a large two dimensional position sensitive neutron counter (2D-PSD), and applied
to structure analysis. We have started from the small size of a flat 2D-PSD for evaluation
study, and extended the size until 1m x 0.5m of the active area. Fig.1 shows the 2D-PSD
installed at KAERI-HANARO. As the test experiment, standard samples NaCl and Tb3Fe5O12(TbIG) are used. In Fig.2, the result of the structure analysis for TbIG is shown, as thecomparison of |Fcal|2 vs |Fobs|2. The rotation speed of the crystal is 0.4 degree/min, and 120
degree is covered. Exposure time is 5 hours. TbIG is a body centered cubic lattice with thelattice constant 12.44A. Within this short time measurement, 962 Bragg points are covered
including 181 absent Bragg reflections by symmetry.
This work has been supported by a Grant-In-Aid for Scientific Research (A) No. 21244051,
from the Ministry of Education, Culture, Sports, Science and Technology, and also by
National Research Foundation and Ministry of Education, Science & Technology, Korean
government through its National Nuclear Technology R&D Program.
1000

unclear peakno peakwell defined peakdamaged data

TbIG: Tb 3 Fe 5 O 12
R(F)=8.3%
R(F2)=10.5%
800

a=12.44A
Z=16|Fobs |

2

2x2x4mm3

scaleF= 0.3023
Ext= 0.0265

400

Lattice points:962
well defined peak: 411(unclear peak:160)(no peak: 172)
(Extinction Bragg(a-,d-glide): 181)
(partial:38)

200

Tb : (1/8,0,1/4) B=0.441
Fe1: (3/8,0,1/4) B=0.558
Fe2: (0, 0, 0) B=0.853
O: (-0.03042, 0.05485, 0.1494) B=1.108

0
0

200

400

|F cal |Fig.1 Neutron 2D-PSD

MS6-6(088):x=312,y-243

scan speed=0.4degree/min
120degree: 5hours

600

2

600

800

1000

Fig.2 Result for TbIG

State-of-the-art Multilayer Optics for Modern X-ray
Analytics
J. Wiesmann, T. Samtleben, C. Michaelsen, B. Hasse, J. Graf, F. Hertlein
Incoatec GmbH, Max-Planck-Straße 2, D-21502 Geesthacht, Germany(administration@incoatec.de)In this contribution, we give an overview on current developments of multilayer optics for
diffractometry in the lab as well as for synchrotron applications. We explain the
manufacturing process of the optics, summarize the different types of optics and give someexamples of typical applications which benefit from the new possibilities, especially in
combination with modern microfocus X-ray sources for diffractometry.
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The optics consist of bent substrates with shape tolerances below 100 nm, upon which
multilayers are deposited with single layer thicknesses in the nanometer range and up to
several hundreds of layer pairs. The multilayers were designed with lateral thickness gradients
within ± 1% deviation of the ideal shape. We use sputtering technology for deposition, opticalprofilometry in order to characterize the shape and X-ray reflectometry in order tocharacterize the multilayer thickness distribution both laterally and as in-depth. The
microstructure is investigated by transmission electron microscopy. The beam parameters likemonochromaticity, flux, brilliance and divergence demonstrate the quality of the multilayer
optics used for different applications in the home-lab as well as at synchrotrons.
We will present actual results of a combination of our new microfocus source IµS with a new
type of 2-dimensional beam shaping multilayer optics. These so called Quasar Optics are now
developed for different wavelengths like Cu, Mo, Ag and Cr. They shape a focused or acollimated beam with a very high flux density as well as an adequate divergence directly at
the sample position. Optics are also available, which focuses in one dimension and collimatesin the other. This delivers a line-shaped beam profile. Some applications realized with an IµS
are (GI)SAXS, texture, stress analysis, µ-diffraction or single crystal diffractometry to namebut a few.

MS7-1

Structure and Mechanism of An Amino Acid
Antiporter
Xiang Gao, Feiran Lu, Lijun Zhou, Jiawei Wang, and Yigong Shi
Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing
100084, China

Virulent enteric pathogens such as Escherichia coli strain O157:H7 rely on acid resistance(AR) systems to survive acidic environment in the stomach. A major component of AR is anarginine-dependent arginine:agmatine antiporter that expels intracellular protons. Here we
report the crystal structure of AdiC, the arginine:agmatine antiporter from E. coli O157:H7
and a member of the amino acid/polyamine/organocation (APC) superfamily of transporters a.
The overall fold is similar to that of several Na+-coupled symporters. AdiC contains 12transmembrane segments, forms a homodimer, and exists in an outward-facing, open
conformation in the crystals. A conserved, acidic pocket opens to the periplasm. Structuraland biochemical analysis reveals the essential ligand-binding residues, defines the transportroute, and suggests a conserved mechanism for the antiporter activity.

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The structure of human connexin 26 gap junction
channelMS7-2

Shoji Maeda1, So Nakagawa1, Michihiro Suga1, Eiki Yamashita1, Atsunori Oshima2,
Yoshinori Fujiyoshi2, Tomitake Tsukihara1,3
1
Institure for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka-fu,
Japan (maesyou@protein.osaka-u.ac.jp)
2
Dept. of Biophysics, Graduate School of Science, Kyoto University, Oiwake,
Kitashirakawa, Sakyo-ku, Kyoto, 606-8502, Japan3
Picobiology Institute, Graduate School of Life Science, University of Hyogo,
Kamigohri, Akoh, Hyogo 678-1297, JapanGap junctions consist of arrays of intercellular channels between adjacent cells that permit theexchange of ions and small molecules. Here, we report the crystal structure of the gap
junction channel formed by human connexin-26 (Cx26) at 3.5 Å resolution and discuss
structural determinants of solute transport through the channel (Figures). The density map
revealed the two membrane-spanning hemichannels and the arrangement of the fourtransmembrane helices of the six protomers forming each hemichannel. The hemichannels
feature a positively charged cytoplasmic entrance, a funnel, a negatively charged
transmembrane pathway, and an extracellular cavity. The pore is narrowed at the funnel,
which is formed by the six N-terminal helices lining the wall of the channel, which thus
determining the molecular size restriction at the entrance of the channel. The structure of the
Cx26 gap junction channel also has implications for the gating of the channel by thetransjunctional voltage.

Figure. Structure of the Cx26 gap junction channel. The corresponding protomers in the two hemichannels
are shown in the same color. (left) Side view of the Cx26 gap junction channel. (right) Top view of the
Cx26 gap junction channel showing the arrangement of the transmembrane helices.

MS7-3

The role of AmtB-GlnK complex in nitrogen
regulation
Xiaodan Li*1, Fritz Winkler1, Mike Merrick2
1
Paul Scherrer Institute, 5232 Villigen, Switzerland (xiao.li@psi.ch)2
Department of Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, United
Kingdom.

Ammonia is an important nitrogen source for bacteria, fungi and plant, therefore its regulationin the cell is essential and important. Ammonia exists in two forms at physiological condition,- 42 -

AsCA’09

Invited and Oral

namely as ammonia gas (NH3) and ammonium ion (NH4+). Under nitrogen deficiency
condition, the gene encodes the ammonia channel protein (AmtB) from E. coli and is strictly
subjected to nitrogen control. AmtB is expressed and inserted into membrane in order to makesure that the bacteria get enough nitrogen for their growth. Once the bacteria have enoughnitrogen, the expression of AmtB protein will stop and also the existing AmtB will be blocked
by the de-uridylylated regulation protein GlnZ. We have solved the structure of AmtB as wellas AmtB-GlnZ complex structures at atomic resolution and have studied the function of
AmtB protein and relevant mutants.
From our structural and functional studies, weconclude that AmtB protein works as an ammonia channel with an ammonium binding siteand both conserved histidines are essential for optimum substrate conductance. The
de-uridylylated GlnZ interacts with AmtB via a long surface loop containing Y51 (T-loop),
the tip of the T-loop inserts deeply into the cytoplasmic pore exit of AmtB, blocking ammonia
conduction. GlnK interacts with AmtB almost exclusively via a long surface loop containing
Y51 (T-loop), the tip of which inserts deeply into the cytoplasmic pore exit, blocking
ammonia conduction. Y51 of GlnK is also buried in the pore exit, explaining why
uridylylation of this residue prevents complex formation.

Structure and function of A-ATPase: combining
electron microscopy and X-ray crystallography to
study a transmembrane rotary motor complex

MS7-4

Lawrence K. Lee1, Alastair G. Stewart1, Mhairi Donohoe1, Olga Esteban2, Ricardo
A. Bernal3 & Daniela Stock1
1
Victor Chang Cardiac Research Institute, 405 Liverpool St, Darlinghurst NSW 2010,
AUSTRALIA (d.stock@victorchang.edu.au)2
MRC Laboratory of Molecular Biology, Hills Rd, Cambridge CB2 2QH, UK
3
Department of Chemistry, The University of Texas at El Paso, 500 West University, El
Paso, Texas 79968, U.S.A.

Proton translocating ATPases are central to biological energy conversion. While eukaryotes
contain specialised F-ATP synthases for ATP synthesis and V-ATPases for proton pumping,eubacteria and archaea typically contain only one enzyme for both tasks. Although many
eubacteria contain H+-ATPases of the F-type, some eubacteria and all known archaea contain
ATPases of the A-type. A-ATPases are closely related to eukaryotic V-ATPases, but simpler indesign and thus more amenable for structural studies. We are using a low-resolution 3D
reconstruction from electron micrographs as an envelope to build a composite model of theintact A-ATPase from high-resolution X-ray structures of individual subunits. We have now
fitted eight of the nine different subunits, which has given us ample insights into the functionof this intricate molecular machine.
References
1.
2.

Ricardo A. Bernal & Daniela Stock (2004) “Three Dimensional Structure of the Intact Thermus
thermophilus H+-ATPase/Synthase by Electron Microscopy” Structure 12, 1789-1798.
Hisayoshi Makyio, Ryota Iino, Chiyo Ikeda, Hiromi Imamura, Masatada Tamakoshi, Momi Iwata,
Daniela Stock, Ricardo A. Bernal, Elisabeth P. Carpenter, Masasuke Yoshida, Ken Yokoyama & So
Iwata (2005) “Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from
Thermus thermophilus” EMBO J. 24, 3974-3983.
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3.

4.

Invited and Oral

Ingmar Schäfer, Susanne M. Bailer, Monika G. Düser, Michael Börsch, Ricardo A. Bernal, Daniela
Stock & Gerhard Grüber (2006) “Crystal Structure of the Archaeal A1AO ATP Synthase Subunit B
from Methanosarcina mazei Gö1: Implications of Nucleotide-binding Differences In the Major
A1AO Subunits A and B” J. Mol. Biol. 358, 725-740.
Olga Esteban, Ricardo A. Bernal, Mhairi Donohoe, Hortense Videler, Michal Sharon, Carol V.
Robinson & Daniela Stock (2008) “Stoichiometry and localisation of the stator subunits E and G in T.
thermophilus H+-ATPase/synthase.” J. Biol. Chem. 283, 2595-2603.

MS7-5

Crystal Structure of Bacterial Nitric-oxide Reductase,a Key Enzyme in the Respiratory Evolution
Yushi Matsumoto1,2, Shingo Nagano1, Yoshitsugu Shiro1
1
Division of Protein Chemistry, Post-genome Science Center Medical Institute of
Bioregulationm Kyushu University, Japan, (ymatsumoto@bioreg.kyushu-u.ac.jp)
2
RIKEN SPring-8 Cente, Japan

Nitrous oxide (N2O), a major non-carbon dioxide greenhouse gases, is mainly produced insoils through microbial processes. Nitric oxide reductases (NORs) produce N2O from nitricoxide (NO) and are involved in nitrate respiration and denitrification where stepwise
reduction of nitrate (NO3-) to molecular nitrogen is coupled to energy production1.
Cytochrome oxidase and NOR belong to the same superfamily of heme-copper oxidases andNOR is generally considered to be the evolutionary progenitor to cytochrome oxidases. To
date, several crystal structures of cytochrome oxidase have been solved, but there is no known
crystal structure of NOR thereby limiting our understanding of nitrate respiration,
denitrification, and molecular evolution of respiratory enzymes. Here we report the first
crystal structure of Bacillus stearothermophilus NOR and its complex with an electron donor
analogue 2-heptyl hydroxyquinoline N-oxide (HQNO) at 2.5- and 2.7-Å resolution,
respectively. The overall structure of the transmembrane region and the position of the metal
centers are similar to those of cytochrome oxidase clearly indicating an evolutionary
relationship. However, a His-Tyr covalent linkage in the binuclear center found incytochrome oxidases is not found in NOR. In addition, two highly conserved Glu residues notpresent in cytochrome oxidase may provide protons required for NO reduction. These
differences create a relatively larger substrate binding pocket capable of binding two NO
molecules. In contrast to previous predictions1, there is no obvious proton transfer pathway
from the extracellular side to the active site. These and other structural similarities anddifferences provide new insight into NO reduction and suggest how this enzyme evolved forO2 reduction, which was essential step in the evolution of respiration.

MS8-1

Engineering Organic Crystals Using ArenePerfluoroarene Interactions
Todd B. Marder
Department of Chemistry, Durham University, South Road, Durham, DH1 3LE, UK(todd.marder@durham.ac.uk)

Arene-arene interactions play a critical role in a number of important areas of chemistry,
biology and materials science including, for example, influencing protein structures, charge- 44 -

AsCA’09

Invited and Oraltransport in organic field effect transistors (OFETs), light emission from aromatic
luminophores, etc. The main motifs arise from face-to-face or edge-to-face interactions, withedge-to-edge interactions often being neglected. Interestingly, whilst benzene andhexafluorobenzene (HFB) exhibit similar crystal structures dominated by alternatingedge-to-face stacking, and both compounds have melting points of ca. 5°C, in 1960, Patrick
and Prosser showed1 that a 1:1 mixture of the two compounds melts at ca. 24 °C. It was
subsequently shown that a 1:1 co-crystal is formed comprising alternating face-to-face stacksof the C6H6 and C6F6 molecules, although there is a lateral slippage of the rings. Thus, thering centroids are not directly ‘on top’ of one another, i.e., the vector connecting the ring
centroids is not normal to the ring planes. Whilst subsequent studies focused predominantly
on co-crystals of HFB with other 6-membered arenes, we have concentrated our efforts on thefollowing areas: (1) controlling the solid-state organization of mono-disperse
phenylene-ethynylene oligomers; (2) examining the influence of arene-perfluoroarene
interactions on liquid crystal phase behaviour; and (3) exploring the limits of the use of suchinteractions as synthons with respect to the sizes and shapes of the two components in binary
co-crystals, and the incorporation of substituents with various steric and electronic properties.
The latter issues are important for potential applications involving ‘molecular recognition’effects in which the fluoroarene might be required to be tethered to another group. The talkwill address these issues with examples2-9 drawn from our work on conjugated rigid-rods,
disk-like polycyclic aromatics and heterocycles, and will discuss potential applications as wellas current thinking on the nature of the interaction.
References
1. C. R. Patrick and G. S. Prosser, Nature, 187, 1021, 1960.
2. C. Dai, P. Nguyen, T. B. Marder, A. J. Scott, W. Clegg, and C. Viney, Chem. Commun., 2493, 1999.
3. J. C. Collings, K. P. Roscoe, R. Ll. Thomas, A. S. Batsanov, L. M. Stimson, J. A. K. Howard, and T.
B. Marder, New J. Chem., 25, 1410, 2001.
4. J. C. Collings, K. P. Roscoe, E. G. Robins, A. S. Batsanov, L. M. Stimson, J. A. K. Howard, S. J.
Clark, and T. B. Marder, New J. Chem., 26, 1740, 2002.
5. C. E. Smith, P. S. Smith, R. Ll. Thomas, E. G. Robins, J. C. Collings, C. Dai, A. J. Scott, S. Borwick,
A. S. Batsanov, S. W. Watt, C. Viney, J. A. K. Howard, W. Clegg, S. J. Clark, and T. B. Marder, J.
Mater. Chem., 14, 413, 2004.
6. S. W. Watt, C. Dai, A. J. Scott, J. M. Burke, R. Ll. Thomas, J. C. Collings, C. Viney, W. Clegg, and T.
B. Marder, Angew. Chem. Int. Ed., 43, 3061, 2004.
7. J. C. Collings, A. S. Batsanov, J. A. K. Howard, D. A. Dickie, J. A. C. Clyburne, H. A. Jenkins and T.
B. Marder, J. Flourine Chem., 126, 515, 2005.
8. I. A. I. Mkhalid, D. N. Coventry, D. Albesa-Jové, A. S. Batsanov, J. A. K. Howard, R. N. Perutz, andT. B. Marder, Angew. Chem. Int. Ed. Engl., 45, 489, 2006.
9. A. S. Batsanov, I. A. I. Mkhalid, and T. B. Marder, Acta Crystallogr., E63, o1196, 2007.

MS8-2

Proton Dynamics in Hydrogen-bonded Organic
Solids from Protonic Dielectrics to Proton-motor
Tadashi Sugawara1, Kentaro Suzuki1
Dept. of Basic Science, Graduate School of Arts and Science, University of Tokyo, Japan(suga@pentacle.c.u-tokyo.ac.jp)

The tautomerization of 3-hydroxyenones in the solid state is generally frozen at lower
temperatures due to the anti-parallel ordering of dipolar moments of individual tautomers.
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However we found that such tautomerization of 5-bromo-9-hydorxyphenalenone in the crystal
was not suppressed even at 4 K due to the quantum proton-tunneling in the symmetrical
double well of the proton potential on the basis of the symmetrical crystal environment [1, 2].
These findings prompted us to measure the temperature and frequency dependence of the ac
dielectric permittivity of single crystals of bisquaric acid (H2BSQ). This hydrogen-bonded
crystal exhibited dielectric response (ε' = 180 at 800 Hz at 290 K) due to the movement ofprotonic solitons along the intermolecular hydrogen bond [3].
More distinct dielectric property was observed in a hydrated crystal of bis(squaryl)biphenyl(BSQB·4H2O). The squaryl group and four water molecules form a hybrid 1D-hydrogenbonded chain. The dielectric permittivity showed a distinct frequency dependence (ε' = 4.7 ×
104 at 340 K and 1 kHz), suggesting that the proton-rely transmitted along the infinitehydrogen-bonded chain in crystal [4]. Proton transfer along this artificial system provides
important insight into the mechanism of the active proton transport that membrane proteins
exhibit.
Recently we found that oleic acid formed multilamella tubular vesicle of a helical structure ina buffered water solution at pH = 8.0. Surprisingly this helix spontaneously rewound in water,
associating with the movement of the kink that is a movable boundary between helicaldomains [5]. If the mode of undulation of the membrane due to the local stress, which is
caused by the difference in the effective volumes of oleic acid and oleate, is transmitted inphase, macroscopic dynamics, such as winding and unwinding a helix, will emerge. The
dynamics could be regarded as a molecular motor in a sense that the local undulation isconverted to the rational motion promoted by the concerted exchange of protons and counter
anions (Na+) between facing oleic acid and oleate across a thin water layer between bilayer
membranes.
References
1) T. Mochida, A. Izuoka, T. Sugawara, et al., J. Chem. Phys., 101, 7971-7974 (1994)
2) R. Kiyanagi, A. Kojima, H. Kimura, Y. Noda, et al. J. Phys. Soc. Jpn., 74, 613-620 (2005)
3) I. Takasu, T. Sugawara, T. Mochida, J. Phys. Chem. B, 108 (48), 18495-18499 (2004)
4) H. Terao, T. Sugawara, Y. Kita, N. Sato, et al., J. Am. Chem. Soc., 123, 10468-10474 (2001)5) M. Ishimaru, T. Toyota, K. Takakura, T. Sugawara, Y. Sugawara, Chem. Lett., 34(1), 46-47 (2005)

Structure–Property Correlations: Mechanical
Properties of Molecular Crystals

MS8-3

C. Malla Reddy,1, 2 Michael T. Kirchner,2 K. Anantha Padmanabhan,3 Gautam R.
Desiraju2
1
Indian Institute of Science Education and Research, Kolkata, Nadia, West Bengal; 741
252 (cmreddy@iiserkol.ac.in)2
School of Chemistry, University of Hyderabad, Hyderabad 500046
3
Department of Mechanical Engineering, Anna University, Chennai 600025

The typical organic crystal is generally known to be brittle and is susceptible to deformationor breakage on application of a mechanical stress. In our study, it was found that some of theorganic crystals may be sheared through crystal layers like pack of cards, and some other bent
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plastically.1-2 A survey of over 60 molecular crystals helped us to establish a causative
correlation between the mechanical properties and crystal packing.3 Based on the observed
mechanical properties and the crystal structures, the crystals divided into three categories; (1)shearing, (2) bending and (3) brittle. Crystals with parallel layered (4 or 8 Å) structure having
strong intralayer and weak interlayer interactions could be sheared on application of amechanical stress. Bending occurs when the strength of intermolecular interactions inorthogonal directions is significantly different. Isotropic crystals with comparable
intermolecular interactions in the three orthogonal directions are “cross-linked” and do not
bend; they are hard and brittle.

References
1.
2.
3.

C.M. Reddy, S. Basavoju, and G.R. Desiraju, Chem. Commun., (2005) 2439.
C.M. Reddy, R.C. Gundakaram, S. Basavoju, M.T. Kirchner, K.A. Padmanabhan and G.R. Desiraju,
Chem. Commun., (2005) 3945.
C.M. Reddy, K.A. Padmanabhan, and G.R. Desiraju, Cryst. Growth Des., 6 (2006) 2720.

MS8-4

Polymorph and Pseudopolymorph of Co-crystal:
Controlling Formation and Structural Transformation
Miao Du,* Xiu-Juan Jiang, Min Tang
College of Chemistry and Life Science, Tianjin Key Laboratory of Structure andPerformance for Functional Molecule, Tianjin Normal University, Tianjin 300387, P. R.
China (dumiao@public.tpt.tj.cn)

Both co-crystal and polymorphism are attractive topics in crystal engineering of organic
supramolecular solids. In the past years, ee have made a systematic investigation on theco-crystal system of different carboxylic acids and bent dipyridyl tectons with an oxadiazole
spacer.1 In this course, hydrothermal technique that is widely used in synthesizing inorganicand inorganic-organic hybrid crystalline materials, has been demonstrated to be a suitableapproach in preparation of such co-crystals. On the other hand, further studies indicate thatpolymorph of co-crystal may be readily obtained under different synthetic conditions whenrelated dipyridyl building blocks with multiple H-bonding sites are applied.2 In our recent
continuous effort, controlling formation of several polymorph and pseudopolymorph of aco-crystal system as well as the salt-co-crystal continuum has been well realized byadjustment of the crystallizing temperature. In addition, possible structural transformation
between these multi-component complexes will also be presented.
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References(a) M. Du, Z.-H. Zhang, X.-J. Zhao, Cryst. Growth Des. 2005, 5, 1199–1208. (b) M. Du, Z.-H. Zhang,
X.-J. Zhao, Cryst. Growth Des. 2005, 5, 1247–1254. (c) M. Du, Z.-H. Zhang, X.-J. Zhao, H. Cai, Cryst.
Growth Des. 2006, 6, 114–121. (d) M. Du, Z.-H. Zhang, X.-J. Zhao, Cryst. Growth Des. 2006, 6,
390–396.
2. (a) M. Du, Z.-H. Zhang, X.-G. Wang, H.-F. Wu, Q. Wang, Cryst. Growth Des. 2006, 6, 1867–1875. (b)M. Du, X.-J. Jiang, X. Tan, Z.-H. Zhang, H. Cai, CrystEngComm 2009, 11, 454–462.
1.

Acknowledgements: This work was supported by the National Natural Science Foundation ofChina, Program for New Century Excellent Talents in University and Tianjin Normal
University.

MS8-5

Towards knowledge-based design & control ofpharmaceutical crystal forms
Colin R. Groom, Peter T. A. Galek, Peter A. Wood
Cambridge Crystallographic Data Centre, Cambridge, UK (groom@ccdc.cam.ac.uk)

The pharmaceutical industry is becoming increasingly concerned with better control of thesolid form of drugs due to the financial risks represented by possible polymorphism and thepotential improvements in physicochemical properties that could be afforded by utilisingco-crystallisation. The Cambridge Structural Database (CSD, [1]) now contains half a million
crystal structures and the wealth of information this provides is highly relevant to all aspectsof Crystal Engineering and the understanding of intermolecular interactions at a fundamental
level. The accessibility and application of relevant data is of prime importance wheninvestigating issues like polymorphism and co-crystal design.
Recent software advances [2] have broadened the opportunities for using the CSD in thedesign and control of crystal forms. Analysis of a large family of pharmaceutical co-crystals
containing a consistent API component [3] utilising this software has provided a great deal of
insight into intermolecular interactions in general as well as co-crystal design in particular.
Further specific work exploring the propensity for hydrogen-bond formation [4] hashighlighted the importance of the CSD in estimating the relative stabilities of pharmaceuticalpolymorphs.
References
1.
2.
3.
4.

Allen, F. H. A; Acta Cryst. B, 2002, 58, 380-388.
Macrae, C. F.; Bruno, I. J.; Chisholm, J. A.; Edgington, P. R.; McCabe, P.; Pidcock, E.;
Rodriguez-Monge, L.; Taylor, R.; van de Streek, J.; Wood, P. A.; J. Appl. Cryst., 2008, 41, 466-470.
Childs, S. L.; Wood, P. A.; Rodriguez-Hornedo, N.; Reddy, L. S.; Hardcastle, K. I.; Cryst. GrowthDes., 2009, 9, 1869-1888.
Galek, P. T. A.; Fábián, L; Motherwell, W. D. S.; Allen, F. H. A; Feeder, N; Acta Cryst. B, 2007, 63,
768-782.

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A small/wide-angle X-ray scattering instrument forstructural characterizations with soft matter,nanomaterials, and air-liquid interfaces

MS9-1

U-Ser Jeng,1 Chiu Hun Su,1 Chun-Jen Su,1 Kuei-Fen Liao,1 Wei-Tsung Chuang,1
Ying-Huang Lai,2 Je-Wei Chang,2 Yi-Jiun Chen,2 Yu-Shan Huang,1 Ming-Tao Lee,1
Kuan-Li Yu,1 Din-Goa Liu,1 Zia-Fung Chang,1 Chin-Yen Liu,1 Chien-Hung Chang,1Keng S. Liang1
1
National Synchrotron Radiation Research Center, 101 Hsin-Ann Road, Hsinchu
Science Park, Hsinchu 300,Taiwan, (usjeng@nsrrc.org.tw)
2
Department of Chemistry, Tunghai University, Taichung, 407, Taiwan

At the National Synchrotron Radiation Research Center (NSRRC) a small/wide-angle X-ray
scattering (SAXS/WAXS) instrument has been installed to the BL23A beamline with asuperconducting wiggler insertion device. With the two monochromators incorporated into
one rotating cradle for fast exchange, the X-ray beam can be monochromatized either by the
double Si(111) crystal monochromator (DCM) for high energy resolution (ΔE/E ≈2×10-4) inthe energy range of 5-23 keV, or by the double Mo/B4C multilayer monochromator (DMM)
for 10-30 times higher photon flux of ~2×1011 photons/s in the 6-15 keV range. A plane Si
mirror is especially installed to selectively deflect the beam downwards with an appropriate
incident angle for grazing-incidence SAXS (GISAXS) with air-liquid/liquid-liquid interfaces.
Synchronized SAXS and WAXS measurements are achieved via a data acquisition protocolthat can integrate two linear gas detectors for WAXS and an area detector (gas type orMAR165 CCD) for SAXS; the protocol also incorporates sample change and temperature
control for programmable data collection. The post-sample section is comprised of thevacuum bellow system, beamstop system, and detector systems, all situated on a motorized
optical bench for motion in 6 degrees of freedom. In particular, the 4-m vacuum bellow
system of 260 mm inner diameter provides convenient and continuous changes of thesample-to-detector distance under vacuum. The performance of the instrument is illustrated
via the measurements of several on-going projects of different classes, including (1)simultaneous SAXS/WAXS and differential scanning calorimetry for polymer crystallization,(2) structural evolution with a large ordering spacing of ~200 nm in a supramolecularcomplex, (3) SAXS for polymer blends under in situ drawing, (4) SAXS and anomalous
SAXS for unilamellar lipid vesicles and metalloprotein solutions, (5) anomalous grazing
incidence SAXS (GISAXS) for oriented membranes of Br-labeled lipids embedded withpeptides, and (6) GISAXS for silicate films in situ formed at the air-water interface.

Surface and flow induced ordering of complex fluids

MS9-2

W.A. Hamilton1, L. Porcar2, P.D. Butler3 and G.G. Warr4
1
Bragg Institute, Australian Nuclear Science and Technology Organisation, Lucas
Heights, NSW 2234, Australia (wha@ansto.gov.au)
2
Large Scale Structures Group, Institut Laue-Langevin, Grenoble, France
3
National Institute of Standards and Technology, Center for Neutron Research,
Gaithersburg, MD 20899, USA
4
School of Chemistry, University of Sydney, Sydney, NSW 2006, Australia

Over the last few decades an ever increasing number of soft matter systems have been shown(or engineered) to exhibit a degree of ordering and symmetry traditionally associated with- 49 -

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Invited and Oral

inorganic crystals – most obviously in the self-assembly of controlled polymer systems.
Another area in which more order exists than might have been expected is in colloid systems.
The name itself means gluelike (from the Greek “κόλλα”) and was given to the class by thefather of colloid science, English physicist Thomas Graham, to distinguish the inchoate
characteristics of its members from those of the more obviously ordered “crystalloids”.
Over the last ten years or so using both small angle neutron scattering and reflectometry ourgroup has probed the response of complex fluid colloidal structures to anisotropic ordering
conditions – either under flow or constrained by a proximate surface - or in Poiseuille flow a
combination of both. In a number of cases we have found that the increased order imposed
under such conditions does result in a more regular arrangement of some rather flexible andextended self-assembled structures than is observed under static conditions, and that the
responses of these systems to these conditions can reveal some of the finer details of theirdynamics.

MS9-3

Intimate Relationship between Micro-phase
Separation and Crystalline Phase Transitions in
Polyethylene- Poly(ethylene Oxide) Diblock
Copolymer as Viewed by Synchrotron SAXS/WAXD
and IR/Raman Measurements
Kohji Tashiro1, Weiyu Cao1, Makoto Hanesaka1, Hiroyasu Masunaga2, Sono Sasaki2
and Masaki Takata2
1
Department of Future Industry-oriented Basic Science and Materials, Toyota
technological Institute, Tempaku, Nagoya 468-8511, Japan (ktashiro@toyota-ti.ac.jp)
2Japan Synchrotron Radiation Institute (SPring-8)

Among the various kinds of diblock copolymers, the crystalline-crystalline diblock
copolymers should show complicated behaviors since there occur two types of structuralchanges: (i) the structural changes in the crystalline lattices of each polymer domains and (ii)the morphological changes in higher-order structure of these domains (micro-phaseseparation). In the present paper we describe the details of these structural changes (i) and (ii)forpolyethylene-poly(ethyleneoxide)(PE-b-PEO)
diblock
copolymer[H(CH2CH2)m(OCH2CH2)nOH, EmEOn], one of the most typical crystalline diblock
copolymers. There have been reported quite limited papers so far, in which only theorder-disorder change of lamellar structure was described (L.Sun et al. Polymer 2004, 45,8181; R. V. Castillo et al., Macromolecules 2008, 41, 879). We have found out thecomplicated morphological changes between lamella-(perforated lamella)-gyroidcylinder-sphere phases in the heating and cooling processes on the basis ofsimultaneously-measured synchrotron SAXS/WAXD data. At the same time the infrared andRaman spectral data revealed the phase transition of PE phase between
orthorhombic-hexagonal-melt phases (W-Y Cao et al., J. Phys. Chem. B, 113, 2338, 8495
(2009)). For example, Figure 1 shows the intimate relationship between the structural changes(i) and (ii) clarified for E39EO86 sample. One of the most noticeable points is that thelamella-to-gyroid transition occurs even when the PE parts are still in the orthorhombic
crystal phase (PEO parts are already melted). It is difficult in general to imagine such a- 50 -

AsCA’09

Invited and Oralremarkable morphological change as long as the crystalline component remains in the sample.
The temperature dependent Raman spectral measurement clarified that the PE chains
experience thermally-activated motion even in the orthorhombic phase. In this way thethermal motion of chain segments is found to be one important factor for the mesoscopic
phase transition phenomenon. In the case of E131EO171 sample with longer chain segments,
the morphological transition did not occur at all and only the order-disorder transition wasobserved in the lamellar phase. The quantitative analysis of SAXS data revealed that the PE
chain segments are once folded on the lamellar surface. The Raman measurement told us thatthe thermal motion was not active even at high temperature. Therefore, it may be reasonably
said that the existence of folded chain structure depresses the thermal motion of PE chains,prohibiting the morphological changes from the lamellar structure. In this way the
micro-phase transition phenomena of PE-b-PEO diblock copolymers are governed by suchimportant factors as thermal mobility and folded structure of PE chain segments in addition to
the conventionally-discussed volume ratio between PE and PEO segmental parts. This new
idea of “folded chain structure” as one important factor helps us to understand the reason why
the general crystalline diblock copolymer with relatively long chain segments does not show
any complicated transitions from lamella to gyroid and cylinder phases.
PE

Orthorhombic Phase
Regular trans-zigzag

PEO

Monoclinic Phase-10 oC

MS9-4

Melt
Coil

Melt

(7/2) Helical
LamellaRotator Phase
Thermally-activated/Condis

Coil
Gyroid
50 oC

60 oC

Cylinder70 oC

Sphere90 oC

100 oCThe Quokka Small Angle Neutron Scattering
Instrument at OPAL
Richard F. Garrett, Elliot P. Gilbert, William A. Hamilton and Kathleen Wood
ANSTO, Private Mail Bag 1, Menai, NSW, 2234, Australia

Quokka is a 40m small angle neutron scattering instrument installed on the cold source of the
OPAL research reactor operated by ANSTO. The source – sample distance is selectablefrom 1 – 20 metres via a series of neutron super-mirror guides, and the sample to detector
distance is continuously variable over the same range. Coupled with a standard operating
neutron wavelength of 5Å, this produces a q range of .0008 to 0.8 Å-1. The heart of the
instrument is a 1m2 2-D wire detector with 5mm pixels. In addition to the standard
20-position automatic sample changer, a wide range of sample environment equipment isavailable including variable temperature cryostats and furnaces, cryo-magnets capable offields up to 11T, a rapid heat/quench cell, and standard shear and stirring cells.
Quokka is one of the flagship instruments at OPAL and is attracting users from a wide rangeof research disciplines, from polymers/soft matter to complex fluids and condensed matterphysics. In the Australian context it is a key instrument for a number of food science- 51 -

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projects investigating proteins, polymers and emulsions. Construction and commissioningof Quokka was completed in the first half of 2009, and the instrument was made available togeneral users for the first time in the May 2009 proposal round. It attracted intense interest
from the Australian and international research community with instrument time requests far
exceeding the available time.
The capabilities and performance of Quokka will be presented, along with highlights from thefirst experiments.

MS9-5

The effect of interface on the crystallization behavior
of Poly(3-hydroxybutyrate) ultra-thin film revealed bygrazing incident X-ray dffraction
Xiaoli Sun,1, 2 Harumi, Sato,1 Yukihiro Ozaki, 1Shouke Yan, 2*Isao Takahashi1*
1 Faculty of Science and Technology, Kwansei-Gakuin University, Sanda, Hyogo
6691337, Japan (suikyo@kwansei.ac.jp)
2 State Key Laboratory of Chemical Resource Engineering, Beijing University ofChemical Technology, Beijing 100029, China. (skyan@mail.buct.edu.cn)

Poly(3-Hydroxybutyrate) (PHB) is one of the most intensively studied crystalline
biodegradable polymers. In the present study, crystallization behavior of PHB ultra-thin filmwith different interface was investigated by the out-of-plane grazing incident X-ray diffraction(GIXD). On the substrate of Si(100) wafer capped by natural oxide, only (020) Braggreflection is observed at 2θ = 13.56°. The orientation of b-axis in the thin PHB film is leadedby the mobile surface layer in the polymer-air interface. However, on the surface of hydroxyl
Si, another Bragg reflection around 23.05° appears in the GIXD profile. This may be inducedby the hydroxyl group which has an interaction with the C = O group in the PHB helicalchains. When polystyrene (PS) is covered on the surface of PHB (i.e. sandwiched structure of
Si-oxide/PHB/PS), crystallization of PHB was not significantly affected. However, thesandwiched structure of hydroxyl-Si/PHB/PS, (020) Bragg reflection disappears and only thereflection around 23.05° is observed.
References
1.
2.
3.

Mori,K.; Mukoyama, S.; Zhang, Y.; Sato, H.; Ozaki, Y.; Terauchi, H.; Noda, I.; Takahashi, I.
Macromolecules 2008, 41, 1713
Capitan, M. J.; Rueda, D. R.; Ezquerra, T. A. Macromolecules 2004, 37, 5653
Toney, M. F.; Russell, T. P.; Logan, J. A.; kikuchi, H.; Sands, J. M.; Kumar, S. K. Nature, 374,
709

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MS10-1

Invited and Oral

Tracking ligand migration pathways incarbonmonoxy myoglobin at cryogenic temperatures
Shin-ichi Adachi
Photon Factory, KEK, 1-1 Oho Tsukuba, Ibaraki, 305-0802, Japan(shinichi.adachi@kek.jp)

In general, protein crystallography reveals static structures of proteins. However, in order toexplore the mechanism of protein function, it is also crucial to unveil their dynamic structures.
For example, myoglobin (Mb) is a small oxygen storage protein in muscle, which reversibly
binds gas ligands (O2, CO, NO etc.) at the heme iron site deeply inside the protein matrix.
Ligand dissociation can be easily triggered by photo-irradiation [1], and the ligand binding
reaction in Mb has been studied by using various techniques. In particular, the photolysis ofcarbonmonoxy myoglobin (MbCO) in crystal has been extensively studied by X-ray
diffraction experiments (e.g. Laue diffraction at room temperature and monochromatic X-ray
diffraction at cryogenic temperatures [2, 3]). Although many details are known regarding gas
ligand molecules trapped in internal hydrophobic cavities in Mb, there exists no direct
evidence to show the dynamic properties of migration pathways connecting these cavities. In
order to explore these pathways in Mb, we have carried out cryogenic X-ray crystallographic
investigations of native sperm whale MbCO under photo-irradiation. Our method ofcontinuous illumination of MbCO crystals with pulsed laser light at cryogenic temperatures
has allowed the production of a movie of ligand migration in Mb on the time scale of several
hours [4]. The whole data collection was done at beamline NW14A at the PF-AR, KEK [5].
The experimental details and the dynamic nature of the ligand migration pathways will be
discussed.
References[1] Q. H. Gibson, J. Physiol., 134(1956)112.
[2] F. Schotte et al., Science, 300 (2003) 1944.
[3] T. Y. Teng et al., Nature Struct. Biol., 1 (1994) 701.
[4] A. Tomita et al., Proc. Nat. Acad. Sci. USA, 106 (2009) 2612.
[5] S. Nozawa et al., J. Synchrotron Rad., 14 (2007) 313.

Exploring the conformational energy landscape ofacetylcholinesterase by kinetic crystallography

MS10-2

Jacques-Philippe Colletier, Benoît Sanson, Didier Fournier, Joel L. Sussman, Israel
Silman, Dominique Bourgeois and Martin Weik.
1
Institut de Biologie Structurale, CEA/CNRS/UJF 41 rue Jules Horowitz, 398027
Grenoble, France (colletier@ibs.fr; benoit.sanson@ibs.fr; dominique.bourgeois@ibs.fr;
weik@ibs.fr)
2
Institut de Pharmacologie et de Biologie Structurale, CNRS, 218 Route de Narbonne,
31400 Toulouse, France (didier.fournier@ipbs.fr)
3,4Departments of Structural Biology and Neurobiology, Weizmann Institute of Science,
76100 Rehovot, Israel (joel.sussman@weizmann.ac.il; israel.silman@weizmann.ac.il).

Acetylcholinesterase (AChE) is a very rapid enzyme, essential in the process of nerve impulse
transmission at cholinergic synapses [1]. It is the target of most currently approved
anti-Alzheimer drugs [1] and further progress in the modulation of its activity requires- 53 -

AsCA’09

Invited and Oralstructural as well as dynamical information. The set of conformations accessible to AChE forthe formation of complexes [2] indeed pre-exists in the conformational energy landscape ofthe native enzyme [3], a point of particular interest in the quest for “tailor-made”, more
efficient drugs [4].
Three experimental approaches will be outlined, which have allowed gaining structural
insights into the dynamics of this captivating enzyme. We will first describe a steady-state
approach for determining atomic-resolution structures of enzyme/substrate complexes, which
has allowed to structurally follow the traffic of substrates within the active site of AChE [5,6].
Shall then be described a new kinetic-crystallography strategy in which a photolabile
precursor of the enzymatic product is cleaved in-crystallo by means of UV-laser irradiation,and the molecular motions necessary for the expulsion of photolysis-products to occur
triggered and quenched by temperature-controlled X-ray crystallography [7]. Last, we will
present a novel yet extremely simple approach for following in “real-time” the traffic of
enzymatic products in crystalline enzymes, and discuss the results obtained on AChE [8].
The relevance of these results as to permit a detailed description of the traffic of substrates
and products within acetylcholinesterase will be discussed, as well as the provided insights
into its conformational energy landscape[9].
References
1.
2.
3.
4.
5.
6.
7.
8.
9.

Silman I and Sussman JL. (2005) Curr Opin Pharmacol, 5, 293-302.
Colletier J.P., Sanson B., Nachon F., Gabellieri E., Fattorusso C., Campiani G. and Weik M. (2006)
J Am Chem Soc, 128, 4526-4527.
Xu Y., Colletier J.P., Weik M., Jiang H., Moult J., Silman I. and Sussman J.L. (2008) Biophys J,
95, 2500-2511.
Xu Y., Colletier J.P., Jiang H., Silman I., Sussman J.L. and Weik M. (2008) Protein Science, 17,601-605.
Stojan J., Brochier L., Alies C., Colletier J.P. and Fournier D. (2004) Eur J Biochem, 271,
1364-1371.
Colletier J.P., Fournier D., Greenblat H.M., Sussman J.L., Zaccai G., Silman I. and Weik M.
(2006) EMBO J, 25, 2746-2756.
Colletier J.P., Royant A., Sanson B., Specht A., Nachon F., Masson P., Zaccai G., Sussman J.L.,
Goeldner M., Silman I., Bourgeois D. and Weik M. (2007) Acta Crystallogr D, 63, 1115-1128.
Colletier J.P., Bourgeois D., Fournier D., Silman I., Sussman J.L. and Weik M. (2008) Proc Natl
Acad Sci USA, 105, 11742-11747.
Colletier J.P and Weik M. (2007) Ann Pharm Fr, 65, 108-118

MS10-3Structure of HIV-1 protease in complex with inhibitor
KNI-272 determined by neutron crystallography
Motoyasu Adachi1, Ryota Kuroki1
1
Japan Atomic Energy Agency, Tokai, Ibaraki, 319-1195, Japan(adachi.motoyasu@jaea.go.jp)

Neutron crystallography will provide us important structural information to elucidate catalytic
mechanism of enzymes through observation of hydrogen atoms in catalytic residues. We
have recently determined a crystal structure of HIV-1 protease by neutron crystallography.
HIV-1 protease is a dimeric aspartic protease that cleaves the nascent polyproteins of HIV-1
and plays an essential role in viral replication. Althogh the development of HIV-1 protease- 54 -

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inhibitors is regarded as a major success of structure-based drug design and contributes toestablish highly active anti-retroviral therapy for AIDS, the catalytic mechanism of HIV-1
protease has still been a matter of some devate. To further understand the catalytic
mechanism of HIV-1 protease, we have determined the crystal structure of HIV-1 protease incomplex with a transition state mimetic tripeptide inhibitor, KNI-272 to 1.9 Å resolution by
neutron crystallography in combination with 1.4 Å resolution X-ray diffraction data (Figure 1)[1]. Our results indicates that the carbonyl group of allophenylnorstatine (Apns) in KNI-272
forms a significant hydrogen bond with protonated Asp 25, and the hydrogen atom from thehydroxyl group of Apns forms a remarkable hydrogen bond with the deprotonated Asp125(Figure 2). These results show direct evidence that Asp25 provides a proton to carbonylgroup of substrate and Asp125 contributes to activate the attacking water molecule as anucleophile.

Figure 1. Tertiary structure of HIV-1 protease
determined by neutron diffraction

Figure 2. Nuclear Density of the hydrogenatoms seen in the catalytic site of HIV-1

Reference
M. Adachi et al. Proc. Natl. Acad. Sci. USA, 106, 4641-4646 (2009).

MS10-4

Taking the edge off: The softer side of in-house SAD
phasing
Joseph D. Ferrara, James W. Pflugrath, Cheng Yang
Rigaku Americas Corporation, The Woodlands, Texas, USA(joseph.ferrara@rigaku.com)

The phase problem in macromolecular crystallography has been mitigated dramatically inrecent years by advances in methodology and instrumentation. SAD phasing has now become
the primary de novo phasing method. A search of the PDB of structures released in 2007
reveals the number of structures solved by SAD phasing exceeds those solved by MAD forthe first time. A number of these examples of successful S-SAD and Se-SAD phasing used
Cr radiation (λ = 2.29 Å), which can double the anomalous signal of sulphur and selenium
compared to Cu radiation.
This report reviews recent results from phasing with the enhanced anomalous signal provided
by Cr radiation to demonstrate this longer wavelength can be used to solve de novo structures.
Selenium, as the heavy atom, with Cr radiation can provide sufficient anomalous scattering
for routine phasing. Cr radiation opens a new path to extracting the weak anomalous signal
from sulphur to phase native protein data. With the addition of Cr radiation to the
crystallographer’s toolkit, in-house X-ray sources can routinely provide at least two- 55 -

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Invited and Oral

wavelength options. The combination of diffraction data collected using both Cu (λ = 1.54 Å)
and Cr radiation can improve the electron density tremendously. Anomalous scattering fromsulphur can also assist in molecular replacement solutions. Finally, the data collected with Cr
radiation can be used to refine a structure. Ultimately, this makes it possible to solve a protein
structure with a single data set.
This in-house phasing approach we describe has been given the label “know before you go”
by John Rose and B.C. Wang at the University of Georgia.
This method improves theefficiency of the solution of macromolecular crystal structures and usage of the synchrotron
beam time.

MS10-5

Reductive methylation of surface lysines assists
crystallization of proteins
Neil Shaw, Chongyun Cheng, Zhi-Jie Liu
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of
Sciences, Beijing 100101, China

A pure, homogenous protein sample may not guarantee a 3D structure. Often the side chainsof surface residues like lysines and glutamic acids are dis-ordered and hinder the formation ofa crystal or interfere in the packing of the molecules in the lattice. Chemical modification of aprotein using a reductive methylation protocol1, 2, results in the addition of 2 methyl groups tothe side chain amine nitrogen of lysine residues. The methyl groups have been observed tophysically bridge the distance between the amine nitrogen and carboxyl group of glutamic
acids, resulting in the formation of cohesive (NZ)CH…O contacts3. (NZ)CH…O contacts
help localize the side chains and make the protein compact. Analytical ultracentrifugation
analysis and thermal denaturation studies reveal a more compact protein structure with better
solvent exclusion of buried tryptophan residues in the folded state of the methylated protein,assisting crystallization3.
Examples of proteins that have been successfully crystallized in our laboratory by methylating
the side chain amine nitrogen of lysine residues will be discussed.
References
1.
2.
3.

Neil Shaw, Chongyun Cheng, and Zhi-Jie Liu. Procedure for reductive methylation of protein to
improve crystallizability. Nature Protocols DOI: 10.1038/nprot.2007.287 (2007).
Rayment, I. Reductive alkylation of lysine residues to alter crystallization properties of proteins.
Methods in Enzymology 276, 171-179 (1997).
Neil Shaw, Chongyun Cheng, Wolfram Tempel, Jessie Chang, Joseph Ng, Xin-Yu Wang, Sarah Perrett,John Rose, Zihe Rao, Bi-Cheng Wang, Zhi-Jie Liu. (NZ)CH...O Contacts assist crystallization of a
ParB-like nuclease. BMC Struc. Biol. 7, 46-58 (2007).

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MS10-6

Invited and Oral

Improvement of a new rotation function for molecularreplacement by designing new scoring functions
such as relative entropy and dynamic correlation
coefficient
Fan Jiang, Wei Ding
Institute of Physics, Chinese Academy of Sciences, 8 South St. No.3, Zhong Guan Cun,
Haidian District, Beijing, 100190, China (fjiang@aphy.iphy.ac.cn)

As structural genomics progresses, automatic structure determination using molecularreplacement method has becoming increasingly important. This has spurred moredevelopment of both the search engine and the automatic intelligent pipeline for molecularreplacement, such as AMORE, MOLREP, PHASER, Mr.Bump and so on.
Previously we have introduced a new rotation function for the rotation search of the molecularreplacement method [1]. In this new method, the atomic coordinates of the search model isdirectly matched with the Patterson map of the target crystal. The goodness of matching ismeasured by several scoring functions such as product of atomic and map weights, correlation
coefficient of atomic and map weights, relative R-factor of atomic and map weights, and soon. The signal-to-noise ratio of the matching is enhanced by first averaging the peaks of all
possible matches and then optimizing a set of weights by linear regression method to obtain a
combined score of all the individual matching functions. We have found that the set ofweights optimized from local search around the correct solution can be generalized to global
search with reasonably good results. This set of weights should at least applicable for a given
model and a target crystal with known space group and cell parameters. We also found the setof weights optimized depends on the crystal form. This will greatly limit the applicability of
our new rotation function when applying to an unknown target crystal form.
In this work, we propose a new method of calculating the correlation coefficient for eachrotation angle sampled in the rotation function search, and this “dynamic” correlation
coefficient is used as the value of our new rotation function. So the set of weights are
optimized dynamically and locally instead of globally for a given target crystal, this will
reduce the dependence of the weights on the crystal form. In addition, we add two newmatching scoring functions: the relative entropy between the model weights and the Patterson
map weights, and the mean-square residue between the model weights and the map weights.
The relative scales between the model and map weights are such to minimize their differencesin distribution. We found that our new rotation function was applicable to a number of crystal
structures extracted PDB with experimental diffraction data.
References
1.

Fan Jiang (2008) A new rotation function for molecular replacement by using both the self and crossPatterson vectors. Acta Cryst. D64, 561-566.

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MS10-7

Invited and Oral

New and Underused Methods for X-ray
Crystallography at Low Resolution
Yong Xiong
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven,
CT 06511, USA

The challenge for X-ray crystallography at low resolution. While crystals of many important
macromolecules/complexes are often obtained, they frequently only diffract to low
resolutions, leading to a large amount of available data unused. For example, structural
genomic centers produced 11547 unique crystals in the past four years; however, only 3417
have resulted in structures, all at a resolution higher than 3.5 Å [1]. Similarly, only the mostexperienced structural biology labs will use only low-resolution data to pursue structure
determination. Of the greater than 13,000 unique crystal structures deposited in the PDB todate, only about 150 structures have been determined at a resolution lower than 3.5 Å, fewer
than 10 of which are lower than 4 Å.
Theoretically, detailed amino acid side chain information exists even in the range of 3.5-5 Å
resolutions. We have demonstrated in practice that the theoretical limit is achievable withadequate treatment of the computation factors affecting the resolution [2]. These general but
underused techniques can have an immediate impact on structural analysis of macromolecularcomplexes.
Sharpening, is an effective method to correct the electron density blurring caused by motion
or displacement of molecules in the crystal, with atypical symptom of high B-factors. Despite its provensuccess, it is practiced only by a small number of
research groups. Our survey of the PDB depositions
shows that the vast majority of crystal structures
Fig. 1 Resolution-enhancing by sharpening.
determined at a resolution lower than 3 Å could havebeen sharpened to produce an electron density map with enhanced details, which is crucial for
atomic model building by reducing the uncertainty of main chain connectivity and side chain
assignment. However, even in 2009, few published structures have used the sharpening
technique. We have implemented a correlation-based method to standardize the procedure anddetermine the optimal sharpening factor. In addition, we are extending capability of thetechnique to perform domain-wise sharpening. The optimized sharpening method will
significantly increase the likelihood and accelerate the pace for structure determination ofmacromolecular complexes at low resolution.
A general use of multi-crystal averaging, perhaps the most powerful phase improvement
technique. To date, use of this technique has been limited to when more than two crystal formsof the same molecule are available. We have demonstrated the use of this method between
crystals that contain many common components, such as crystals of a molecular complex at
different functional stages, crystals of a complex and its individual components, or crystals ofdifferent complexes that have any common protein/nucleic acid component. Significantly, we
have successfully extended its use to crystals of homologous, but not identical molecules [5].
These much more general applications of this powerful technique means that the large amount- 58 -

AsCA’09

Invited and Oralof structural information in PDB can be harvested through multi-crystal averaging to aid thedetermination of new structures.

Fig. 2 a) and b) Two functional structures ofresolvase [3]. c) Effect of multi-crystal averaging.
The improvement is an unbiased overall phase
improvement as the helix is not included in the
averaging.

Fig. 3 Structures of a) CCA-adding enzyme and b)
its ternary complex with RNA and ATP [4]. c) Effectof multi-crystal averaging. ATP is not included inaveraging.not included in the averaging.

References
1.
2.
3.
4.
5.

http://olenka.med.virginia.edu/mcsg/phtml/progress_viewer.phtml.
Lomakin, I.B., Y. Xiong & T.A. Steitz (2007). Cell 129, 319-32.
Li, W., et al. (2005). Science 309, 1210-5.
Xiong, Y. & T.A. Steitz (2004). Nature 430, 640-5.
Fang, Y., et al. (2009). Nature (Advance online publication).

Thermoelectric Zintl Compounds in R-T-Sb (R = Ca,
Sr, Ba, Eu, Yb; T = Zn, Cd) Systems

MS11-1

X.J. Wanga, H. Zhanga, M.B. Tanga, X.X. Yanga, H.H. Chena, Z.Y. Mana, U.
Burkhardtb, Y.Grin*b, J.T. Zhao*aa
Key Laboratory of Transparent and Opto-Functional Inorganic Materials of Chinese
Academy of Sciences, Shanghai Institute of Ceramics, Shanghai 200050, P.R. China;b

Max-Planck Institute for Chemical Physics of Solids, Dresden, Germany(jtzhao@mail.sic.ac.cn)

Recently many new promising thermoelectric (TE) materials have been found in a special
category of intermetallic compounds, i.e. Zintl phases. The classical Zintl phases are
semiconductors with narrow band gap and many have complex crystal structures containing“rattle” heavy atoms to produce low lattice thermal conductivities. In our systematicinvestigations of potential TE materials in intermetallic compounds with polar character,ternary Zintl phases RxTySz(R=Ca, Sr, Ba, Yb and Eu; T=Transition elements; S= Semi-metalelements) showed to be promising. Based on first principle calculations on electronic
structures and crystal structure analyses, the pnictide candidates such as BaZn2Sb2, YbCd2Sb2
and EuCd2Sb2 were synthesized and their thermal and electrical transport properties werecharacterized. These compounds show promising TE properties with considerably high figureof merit (e.g. ZT~1at 700K for YbCd2Sb2). The solid solution system YbCdxZn2-xSb2 (x = 0,0.4, 0.8, 1, 1.2, 1.6 and 2) were synthesized and their TE properties were also characterized.
The results revealed that Zn substitution of Cd in YbCd2Sb2 can easily tune carrier
concentration and decrease thermal conductivity, which resulted in improvement of ZT value(e.g. ZT ~1.2 at 700K for x = 0.4).
References
1.

X.J. Wang, M.B. Tang, H.H. Chen, X.X. Yang, J.T. Zhao, U. Burkhart, Yu. Grin, Appl. Phys. Lett. 94(2009) 092106- 59 -

AsCA’09
2.
3.

Invited and Oral

H. Zhang, J.T. Zhao, Yu. Grin, X.J. Wang, M.B. Tang, Z.Y. Man, H.H. Chen, X.X. Yang, J. Chem.
Phys. 129 (2008), 164713.
H. Zhang, L. Fang, M.B. Tang, H.H. Chen, X.X. Yang, X.X. Guo, J.T. Zhao, Yu. Grin,
Intermetallics-D-08-00373R1 (2009).

MS11-2

Solid-state photochemical reactivity of coordination
polymers and metal complexes containing
trans-1,2-bis(4-pyridyl)ethylene
Jagadese J. Vittal, Mangayarkarasi Nagarathinam, Abdul Malik Puthan Peedikakkal
Department of Chemsitry, National University of Singapore, 3 Science Drive 3,
Singapore 117543 (chmjjv@nus.edu.sg)

The criteria for solid-state photochemical [2+2] cycloaddition reactions have been wellestablished, however, it is still a challenge to stack a pair of C=C bonds in the crystal latticeby design. A number of weak interactions have been serendipitously discovered to align the
double bonds in the crystal lattice congenial for the photochemical dimerization reactions.
The strength and directionality of the hydrogen bonds have been elegantly exploited to alignthe double bonds in 4,4’-bipyridylethylene (bpe) with considerable success. Such
photochemical reactions have also been carried out in the inorganic compounds containing
ligands with C=C bonds in their backbones. For example, coordination polymers withladder-like structures provided an interesting possibility to align the photoreactive double
bonds in the solid-state. In another example, a 1D coordination polymer was found toreorganize to form ladder structure on desolvation which undergoes [2+2] cycloaddition under
UV irradiation quantitatively. However, hydrogen bonded metal complexes have not beenused to align the C=C bonds for photochemical cycloaddition reactions. Different strategies
used to align the C=C bonds in the author’s laboratory will be discussed and the challenges
for the coordination chemist in utilizing this rational approach to orient the coordination
polymers will be highlighted with reference to trans-1,2-bis(4-pyridyl)ethylene (bpe).

Anatomy of a Void in an Aluminium-Copper-Tin Alloy

MS11-3Laure Bourgeois1,2, Matthew Weyland1, Philip N.H. Nakashima2, Barry C. Muddle2
1
Monash Centre for Electron Microscopy and Department of Materials Engineering,
Monash University, Victoria 3800, Australia
2Australian Research Council Centre of Excellence for Design in Light Metals andDepartment of Materials Engineering, Monash University, Victoria 3800, Australia

Under certain conditions voids are able to nucleate and grow in association with precipitatephases in an aluminium-copper-tin alloy. This alloy, of composition Al-1.7at.%Cu-0.01at.%Sn,constitutes a model system for the study of the mechanisms by which some trace alloying
additions like Sn are able to efficiently promote the nucleation of strengthening phases, in thiscase the phase θ’ of composition Al2Cu [1]. Since vacancies are a key element in nucleationand growth mechanisms of precipitates, the presence of voids, or giant vacancy clusters,
associated with Sn and θ’ nano-particles, is of great interest.
The present work is a detailed structural study of large voids (∼50 nm in diameter) in a
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Al-1.7at.%Cu-0.01at.%Sn alloy, using several transmission electron microscopy (TEM)
techniques: high-resolution scanning (S)TEM and phase-contrast TEM imaging,energy-dispersive X-ray (EDX) mapping, electron tomography, and convergent beam electron
diffraction (CBED).
Fig. 1 shows a typical example of a void associated with a precipitate each of θ’ and tin; thelatter was found to be the β-Sn phase. Viewed along the [100] direction of the α-Al matrix
phase, the void-matrix interface displays clear facetting parallel to the {200}α planes, together
with 2 Å steps corresponding to the {200}α interplanar distance. A three-dimensional electron
tomographic reconstruction of another such void-tin-θ’ group confirmed the distinct facettingof the void surface (Fig. 2). In combination with high resolution TEM, the crystallographic
characteristics of the β-Sn- and θ’-void interfaces could be determined; the latter isparticularly useful information given that the θ’ phase is always found embedded in α-Al.
CBED revealed the total absence of strain in the void-matrix region, suggesting that the void
acts as strain relief for the β-Sn and θ’ precipitates in contact with it. Although EDX failed todetect any content in the void, one cannot discount the presence of trace impurities such as
oxygen at the void surface, which might reduce its surface energy.

Fig. 1: TEM image along [100]α of avoid-tin-θ’ group. There is distinct{200}α facetting and 2 Å steps at thevoid-matrix interface.

Fig. 2: Electron tomographic reconstruction ofanother void-tin-θ’ group, revealing the 3-D void
morphology, including the clear facetting exhibitedby the β-Sn and θ’ precipitates-void interfaces.

Reference
L. Bourgeois, J.F. Nie, B.C. Muddle, 2005, Phil. Mag. 85, 3487.

SMART X2S - Chemical Structures at the Touch of a
ButtonMS11-4Eric Hovestreydt1, Michael Ruf2, Holger Ott1
1
Bruker AXS GmbH, Oestliche Rheinbrueckenstrasse 49, D 76181 Karlsruhe, Germany(info@bruker-axs.de)2
Bruker AXS Inc., E. Cheryl Parkway 5, MADISON, WI 53711-5373, United States ofAmerica (info@bruker-axs.com)

Modern research moves at breakneck speed. The newly introduced SMART X2S produces
3-D structures at the touch of a button in your own laboratory! The compact and economical
SMART X2S has a couple of unique features, such as fully automated operation from sample
loading and alignment through data collection and structure solution which will be addressed- 61 -

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Invited and Oralin detail.
Its compact air-cooled benchtop design that requires only standard single-phase AC power,
allowing the instrument to be easily placed anywhere. Cost of ownership will be compared tostandard instruments. The SMART X2S is an expert system that allows chemists to do routine
publication quality crystal structures in a few hours. The
SMART X2S automatically loads and aligns your sample,
acquires a complete crystallographic dataset, and thensolves and refines the 3-D structure, completely without
user intervention! The user-friendly software, operated
from a touch-screen, combines an expert knowledge ofstructural chemistry with the power of industry-standard
SHELXTL data processing engines for structure solution and refinement. A number ofexamples will be shown during the talk. Additional applications of the SMART X2S, e.g. as a
crystallographic teaching tool, will be presented.

Rational Design, Synthesis and Properties of Layered
Compounds LnOZnSb (Ln=La, Ce, Pr, Nd)

MS11-5Kai Guo1, 2, Hao-Hong Chen1, Zhen-Yong Man1, Mei-Bo Tang1, Xin-Xin Yang1,
Xiang-Xin Guo1, Jing-Tai Zhao1
1
Key Laboratory of Transparent Opto-functional Inorganic Materials of Chinese
Academy of Sciences, Shanghai Institute of Ceramics, Shanghai 200050, PR China（jtzhao@mail.sic.ac.cn）
2Graduate School of Chinese Academy of Sciences, Beijing 100039, PR China

The rational design of new inorganic compounds perplexes solid-state chemists while
serendipity still plays important role to explore new material. However, controlling the
microcosmic structures of compounds is prerequisite for mastering the physical properties insolids. For this reason, extensive efforts are devoted to reach the breakthroughs in the field. In
this paper, a stacked method with 2D building blocks combined with theoretical computation
is proposed to design the ZrSiCuAs type layered compounds: LnOZnSb (Ln=La, Ce, Pr, Nd).
Then, the design was confirmed by their syntheses and structure characterizations.
The tetragonal ZrSiCuAs type structure is relatively simple with ZrSi and CuAs layers
stacked along c-axis with space group P4/nmm (as shown in Fig.1). A new set of“compounds” are constructed by replacing ZrSi and CuAs layers with LnO and ZnSb layers,respectively. The structures of LnOZnSb are subsequently optimized by means of quantum
calculation methods and the electronic structure investigated using Castep code to understandtheir stability. Furthermore, LnOZnSb (Ln=La, Ce, Pr, Nd) are synthesized via three-stepsolid reaction and the optimized structures were confirmed by XRD (Fig.2). The results ofsimulation and experiment show that LnOZnSb (Ln=La, Ce, Pr, Nd) are narrow band-gap
semiconductors.

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Fig.1 Crystal structure of ZrSiCuAs

Fig.2 XRD pattern of NdOZnSb (the red line represents the simulation result)

References
1.
2.

Laurent Cario, Houria Kabbour, Alain Meerschaut, Chem. Mater. 17 (2005) 234.
R.Pöttgen and D.Johrendt, Z. Naturforsch. 63 (2008) 1135.

MS11-6

Cation⋅⋅⋅Cation Supramolecular Interactions inZinc–Imidazole–Oxovanadate Compounds
Samroeng Krachodnok1, Kenneth J. Haller1, Ian D. Williams2
1
Institute of Science, 111 University Avenue, Muang, Nakhon Ratchasima, 30000,
Thailand (ken.haller@gmail.com, dsk4610137@live.com)
2
Hong Kong, University of Science and Technology, , Hong Kong, (chwill@ust.hk)

Noncovalent interactions involving aromatic sections of molecules are ubiquitous, andparticularly when acting in concert, rival the robustness of hydrogen bonds. Herein, we report
the ability of an imidazole and its derivatives capable of both hydrogen bonding and aromaticinteractions in three zinc–imidazole–oxovanadate compounds, namely [Zn(Im)4]2[V4O12] (1),[ImH]2[{Zn(Im)3}2V10O28]·2H2O (2), and [2-MeImH]2[Zn(2-MeIm)4]2[V10O28] (3), to form
extended concerted aryl interaction motifs. Cationic [Zn(Im)4 ]42 + dimers in 1 bind in two
concerted (EF)2 embrace motifs and further bind to neighboring zinc complexes to form 2D
supramolecular layers perpendicular to the c axis. Adjacent layers are held together by two FF
π···π interactions to form a 3D supramolecular network. The tetrahedral zinc complexes in 2
form two EF C–H···π hydrogen bond interactions in 1D herringbone fashion to generate 2D
nets and further interact with pillared imidazolium dimers to construct a 3D supramolecular
framework. Two different EF C–H···π hydrogen bond interactions in 3 link cationic4+[Zn(Im) 4 ]2 dimers with imidazolium dimers to form 1D –Zn–Zn–ImH–ImH– chains.

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Synthesis and X-ray Structures of Diorganotin
Complexes with Tris{(hydroxymethyl)aminomethane
Schiff baseSee Mun Lee, Hapipah Mohd Ali and Kong Mun Lo
Chemistry Department, University of Malaya, 50603 Kuala Lumpur, Malaysia(smlee@um.edu.my)Tris(hydroxymethyl)aminomethane (THAM) and its derivatives are known to display avariety of biological activities such as antibiotic, anticancer, antihistamine, antifungal,
anti-inflammatory and many others. In this study, two THAM Schiff bases, namely
tris{(hydroxymethyl)-[5-bromosalicylideneiminate]}andtris{(hydroxymethyl)aminomethane [5-chlorosalicylideneiminate]} were prepared. The Schiff bases were reactedwith diorganotin starting materials to form the diorganotin complexes,
bis[1-hydroxy-2-hydroxymethyl-2-(5-bromo-2-oxidobenzylideneamino)-3-oxidomethylpropane]dimethyltin(IV),C1,[1-hydroxy-2-hydroxymethyl-2-(5-chloro-2-oxido-benzylideneamino)-3oxido-methylpropane]dimethyltin(IV),C2,[1-hydroxy-2-hydroxymethyl-2-(5-bromo-2-oxidobenzylideneamino)-3-oxidomethylpropane]diphenyltin(IV), C3 and [1-hydroxy-2-hydroxymethyl2-(5-chloro-2-oxido-benzylideneamino)-3-oxidomethylpropane]-diphenyltin(IV), C4. The complexes
were characterized by using various spectroscopic methods and their X-ray structures were
determined.

The compound C1 crystallises in the monoclinic, P21/n space group. Its molecular structure
shows that the ligand, tris{(hydroxymethyl)aminomethane[5-bromosalicylideneaminate]} istridentate in which the one hydroxymethyl oxygen, one phenoxy oxygen and an imino
nitrogen atoms are involved in coordination with the tin atom. The same hydroxylmethyl
oxygen is also involved in the coordination with the adjacent molecule to form a dimer with acentral Sn2O2 stannoxane ring. Whereas, the X-ray structure of C2 which contains achloro-substituted Schiff base is monomeric. Compounds C3 and C4 are also monomeric,probably due to the steric effect as a result of the presence of bulky phenyl organic groups.

MS12-1

Precise Structure Analysis of Ceramic Materials up to1830 K
Masatomo Yashima
Department of Materials Science and Engineering, Interdisciplinary Graduate School of
Science and Engineering,, Tokyo Institute of Technology, Nagatsuta-cho 4259-J2-61,
Midori, Yokohama, 226-8502, Japan (yashima@materia.titech.ac.jp)

We review our recent works on the visualization of diffusional pathway of mobile ions andchemical bonding in ceramic materials through synchrotron and neutron powder diffraction
experiments, which would be useful for the design of ceramic materials. Crystal structure andelectron-density distribution of α-silicon nitride (α-Si3N4, space group: P31c) have been
investigated by a combined technique of Rietveld method, maximum-entropy method (MEM)
and MEM-based pattern fitting (MPF) of high-resolution synchrotron powder diffraction data.
In combination with density functional theory (DFT) calculations, the present experimental
electron-density distribution of the α-Si3N4 indicates covalent bonds between Si and N atoms- 64 -

AsCA’09

Invited and Oraland the charge transfer from the Si to N atom. The present work suggests that the high bulk
modulus of the α-Si3N4 is attributable to the high minimum electron density of the Si-N bond.
Tantalum oxynitride (TaON) is investigated by neutron and synchrotron diffraction analysis toclarify the structural and electronic features responsible for the visible-light activity of thismaterial. In combination with DFT calculations, the present measurements confirm the TaON
photocatalyst to be monoclinic with space group P21/c. Bond valence sums for the oxygenand nitrogen atomic sites are calculated to be 2.1 and 3.2, respectively. Electron density
analyses based on synchrotron data in combination with DFT calculations reveal covalentbonds between Ta and O atoms and between Ta and N atoms. The hybridization of anion 2p
and Ta 5d orbitals attributed to the covalent bonds between Ta and O or N atoms results inincreased dispersion of the valence band, raising the top of the valence band and leading to avisible-light response. Our group has developed new high-temperature neutron andhigh-resolution synchrotron diffraction techniques to study the precise crystal structures,
nuclear and electron density in inorganic materials up to 1900 K. These techniques enabled
precise structural analysis leading to diffusion path and structural disorder in ionic conductors.
Here we review our recent works on the positional disorder and diffusion path of oxide ions in
Bi2O3,(La0.8Sr0.2)(Ga0.8Mg0.15Co0.05)O2.8,

CeO2,

Bi1.4Yb0.6O3,

Ce0.93Y0.07O1.96,

andLa0.64(Ti0.92Nb0.08)O3 at high temperatures. We also describe the diffusion path of Li cations in
Li-doped lanthanum titanate perovskite La0.62Li0.16TiO3 at room temperature and of Cu
cations in copper iodide CuI at 760 K. These were studied through the nuclear/electron
density distribution obtained by a combined technique including a Rietveld refinement and amaximum-entropy method (MEM)-based pattern fitting of the neutron-powder-diffraction
data. We found that the mobile ions in fluorite-type ionic conductors have a complicateddisorder spreading over a wide area and shift to the <111> directions from the ideal fluorite
site at high temperatures. The fast oxide-ion conductors Bi1.4Yb0.6O3 and Ce0.93Y0.07O1.96
exhibited a curved diffusion pathway along the <100> direction. The Cu cation conductor has
also a fluorite-type structure and curved diffusion pathway along the <100> direction. The
curve feature would be common for various ionic conductors. We have demonstrated that the
diffusion path of mobile oxide ions in the lanthanum gallate-based compound was not along
the straight line between the ideal positions, but exhibited an arc shape away from the B-site
cation (Ga0.8Mg0.15Co0.05). The diffusion pathway forms a three-dimensional network. The
double perovskite-type La0.64(Ti0.92Nb0.08)O3 exhibits a curved diffusion pathway at hightemperatures. The diffusion pathway in the La0.64(Ti0.92Nb0.08)O3 forms a two-dimensional
network. We also report for the first time the diffusional path of oxide ions in a K2NiF4-type
mixed conductor (Pr0.9La0.1)2(Ni0.74Cu0.21Ga0.05)O4+δ, through a high-temperature neutron
powder diffraction study.

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Zeolite Structure Analysis by Powder X-ray Data

MS12-2

Yingxia Wang1, Jie Su1, Jianhua Lin1, Hermann Gies2
1
State Key Laboratory of Rare Earth Materials Chemistry and Application, College ofChemistry and Molecular Engineering, Peking University, Beijing, 100871, China(wangyx@pku.edu.cn)
2Inst. Geologie, Mineralogie und Geophysik, Ruhr-Universität Bochum, 44780 Bochum,
Germany

Zeolites have attracted considerable attention due to their use in industrial applications as
catalysis, ion exchange, adsorption, and separation. As metastable phases with microporous
framework structures, zeolites are often obtained as polycrystalline products fromhydrothermal reaction systems. Then powder X-ray diffraction is a powerful technique for the
structure determination or the framework confirmation. Zeolite frameworks are built on thebasis of vertex sharing tetrahedra. Conventionally zeolites are silicates/aluminosilicates. The
combination modes of SiO4 groups as well as the corresponding structural parameters, such as
Si-O bond length (~1.61 Å), Si-O-Si angle (~145°) and Si…Si distance (~3.0 Å) are helpful
in the analysis of new structures. On the basis of structural principle, we can apply every kindof methods by the aid of suitable programs to puzzle out the structures.
1.

Ab intio structure determination

1) Model building: It is a straight way to have the structure visible, which involves thereasonable use of the known structure building units. RUB-41, the condensation product of alayered hydroxyl silicate RUB-39, is a microporous silica. After indexing the powder X-ray
profile, the lattice constants are obtained1. By searching the database of zeolite structures, wefound the resemblance of RUB-41 with HEU framework 2, 3. Accordingly the same layer isbuilt, but linked in a different way from that of HEU to meet the demand of the lattice
constant along b direction. Five unique Si positions are read out directly from the model andO atoms are obtained by tetrahedral geometric relations. The structure is finally refined by
Rietveld method. As the precursor of RUB-41, the layer in the structure of RUB-39 is similar
to that of RUB-41, then a rigid body is defined, one additional O atom is revealed using
TOPAS by simulated annealing method. The SDA molecules are located during the structurerefinement process.
2) Solving the structure from powder X-ray data: RUB-43 is a microporous germinate. It
crystallizes in a c-centered monoclinic lattice with unit cell parameters of a=13.9340(4)Å,b=33.016(1)Å, c=11.6808(3)Å and β=127.5210(12°) and space group C2/m. Five germanium
atom-positions were revealed by EXPO using direct method4. The missing germanium atoms
were located by Fourier techniques. The positions of O, N and C atoms were found in thecourse of the Rietveld refinement using TOPAS5.
2.

Confirmation of the known framework topology by structure refinement

We shall discuss two examples. PKU-11 is a silicate synthesized by a simple quarternaryammonium SDA. A comparison with the Atlas indicates that the XRD profile is similar to thatof framework STF. A set of electron diffraction patterns related to one grain in different
tilting angles were taken. The indexing result of ED patterns reveals a triclinic lattice with theconstants of a=11.56 Å, b=11.30Å, c=7.30 Å, α=94.7o, β=97.7o, and γ =103.9 o, which areconsistent with the framework parameters of STF. The Rietveld refinement of the calcined- 66 -

AsCA’09

Invited and Oralproduct was performed by TOPAS, using the structure data from SSZ-35 as initial setting.
The other example is a silicogermanate (PKU-12) with CLO- framework type. CLOframework contains 20-rings，which is the largest pore size among all known zeolite
frameworks. It was firstly obtained as a gallium phosphate, named as Cloverite. Much work
has been done on the synthesis of new materials with this topology; however, the reported
compounds were all phosphates. As a silicogermante, the framework structure of PKU-12 hasbeen confirmed to be isostructural to CLO- by Rietveld analysis.
References (selected)[1] C. Dong, J Apply Crystallogr., 32(1999) 838.
[2] M. M. J. Treacy, J. B. Higgins, Collection of Simulated XRD Powder Patterns for Zeolites, 5th,2007[3] Ch. Baerlocher, L. B. McCusker, D. H. Olson, Atlas of Zeolite Framework Types, 6th, 2007
[4] A. Altomare, M.C. Burla, G. Cascarano, C. Giacovazzo, A.Guagliardi, A.G.G. Moliterni, G. Polidori, J.
Appl. Crystallogr. 28(1995) 842.
[5] TOPAS V3: General profile and structure analysis software for powder diffraction data, Bruker AXS,
Karlsruhe (Germany)

Spinner-Scan Method for Evaluation of Particle
Statistics in Powder Diffractometry

MS12-3

Takashi Ida1, Taishi Goto1, Hisashi Hibino2
1
Omohi college, Graduate School of Engineering, Nagoya Institute of Technology,
Gokiso, Showa-ku, Nagoya, 466-8555, Japan (ida.takashi@nitech.ac.jp)
2
Ceramics Research Laboratory, Nagoya Institute of Technology, Asahigaoka, Tajimi,
Gifu, 507-0071, Japan)

The uncertainty in measured diffraction intensities caused by particle statistics, which
originates from the limited number of crystallites satisfying the diffraction condition, has been
evaluated by a step-scan measurement about the rotation angle of a specimen spinner attached
to a laboratory powder X-ray diffractometer.
Particle statistics for a standard Si powder (NIST SRM640c) and three size fractions(nominally 3-7, 8-12 and 18-22 μm in Stokes diameter) of quartz powder separated by asedimentation method have been analysed by scanning electron microscopy (SEM) and thespinner-scan method using a powder X-ray diffractometer (Rigaku RAD-2C). The effective
particle sizes of Si and three fractions of quartz powder have been estimated at 5.6, 7.1, 12, 25
μm by analyzing the SEM images.
The observed spinner-scan intensity profile of the Si 111 reflection is shown in Fig. 1.
Periodic drift in the observed intensity profile is modeled by Fourier expansion up to thesecond order. The residual statistical variance, after subtraction of the periodic drift andvariance caused by counting statistics, has been assigned to the variance caused by particle
statistics. It has been found that the effective numbers of diffracting crystallites evaluatedfor different reflections well correspond with the multiplicities of reflection, which confirmsthat particle statistics has certainly been evaluated by this method. Crude values of theeffective diameter D’eff estimated for each reflection by applying the theoretical formula ofAlexander et al. (1948) are shown in Fig. 2. A calibration curve has been derived assuming
the effective diameter of 5.6 μm determined by the SEM image analysis and slight- 67 -

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Invited and Oralmodification of the formula.

Fig. 1 Spinner-scan profile of Si 111 reflection. The
upper panel shows raw intensity (grey line) andassumed drift profiles (black line). The lower panel
shows the residuals (grey line) and counting errors(broken lines).

Fig. 2 Effective diameter D’eff of Si powder
calculated with assumed instrumental parameters(circles) and the calibration curve (broken line).

The spinner-scan X-ray diffraction intensity data of quartz powder samples were similarlycollected. The effective diameters of three fractions of quartz powder have been estimated at
6.5(2), 11.7(2) and 22.8(2) μm, by analyzing the spinner-scan profiles applying the above
calibration curve. The results show that the statistical variance assigned to particle statistics
can be quantitatively evaluated by this method, and estimation of crystallite size over a rangeof several μm, which is practically impossible to be evaluated by conventional methods basedon line-broadening analysis, has been achieved at considerable accuracy.

Structural and magnetic properties of doped widebandgap semiconductors

MS12-4Gang Wang1, Bo Song1,2, Hui Li1, Liangbao Jiang1, Xiaolong Chen1, Wenjun
Wang1, Wanyan Wang1
1
Beijing National Laboratory for Condensed Matter Physics, Institute of Physics,
Chinese Academy of Sciences, P.O. Box 603, Beijing, 100190, China(gangwang@aphy.iphy.ac.cn)
2
Academy of Fundamental and Interdisciplinary Sciences, Harbin Institute ofTechnology, Harbin, 150080, China

Diluted magnetic semiconductors (DMSs) represent the most promising candidates for
spintronics simultaneously manipulating charge and spin of electrons.[1] Theoretical work has
predicated that III-V and II-VI DMSs possess Curie temperatures (TCs) exceeding room
temperature,[2] which is crucial for the proposed spintronic applications. Many experiments
based on thin films have been carried out to verify such hypotheses.[3-5] However, muchdebate existing over second phase segregation and intrinsic defects in these films originatingfrom the non-equilibrium epitaxial growth process make argument for the origin of hightemperature ferromagnetism in the materials.
Here we report on the structural and magnetic properties of doped wide bandgap
semiconductors AlN, SiC synthesized by solid state reaction and physical vapor transporttechniques. Especially, in order to exclude the effect of magnetic second phase, nonmagnetic
element Al is adopted to make the compounds magnetic besides transition metals Ni, Mn, and- 68 -

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Invited and Oralso on. Ferromagnetism with TCs above 300 K is observed in the homogenous polycrystals,
whiskers and single crystals confirmed by structural analyses. Obviously, current models,such as superexchange, carrier-mediated exchange and magnetic polarons, seem notapplicable for the formation of the ferromagnetic order in these high resistive samples. The
origin of the magnetic interactions responsible for TCs higher than room temperature bydoping less than 1 at.% needs to be further explored. Our work demonstrates the potential forthe spin moments controlling by doping in wide bandgap semiconductors and for thedevelopment of wide bandgap semiconductor based spintrosic devices.
References[1] H. Ohno, Sicence 1998, 281, 951.
[2] T. Dietl, H. Ohno, F. Matsukura, J. Cibert, D. Ferrand, Science 2000, 287, 1019.
[3] M. L. Reed, N. A. El-Masry, H. H. Stadelmaier, M. K. Ritums, M. J. Reed, C. A. Parker, J. C. Reberts,
S. M. Bedair, Appl. Phys. Lett. 2001, 79, 3473.
[4] M. E. Overberg, C. R. Abernathy, S. J. Pearton, N. A. Theodoropoulou, K. T. McCarthy, A. F. Hebard,
Appl. Phys. Lett. 2001, 79, 1312.
[5] M. C. Park, K. S. Huh, J. M. Myoung, J. M. Lee, J. Y. Chang, K. I. Lee, S. H. Han, W. Y. Lee, Solid
State Commun. 2002, 124, 11.

Vanadium substituted potassium tungsten bronzes –its synthesis and characterization

MS12-5A. M. Abdullah1, A. Hussain2
1
Bangladesh Council of Scientific and Industrial Research (BCSIR) Laboratories,
Chittagong – 4220, Bangladesh, (abdullah059@yahoo.com)
2
Department of Chemistry, University of Dhaka, Dhaka – 1000, Bangladesh,(altaf@univdhaka.edu)

Polycrystalline samples with nominal compositions KxVyW1-yO3 (x = 0.3, y ≤ 0.3 and x = 0.5,
y ≤ 0.3) were synthesized by conventional solid state method at 800°C using appropriate
amount of WO3, WO2, V2O5, and K2WO4. The samples were characterized with XRD,
SEM/EDX and optical spectroscopy. Analysis of X-ray powder patterns reveal that single
phase of vanadium substituted potassium hexagonal tungsten bronzes (K-HTB) could be
prepared for nominal composition x = 0.30 , y ≤ 0.15. For further increase in nominal
vanadium content (y), an additional phase appears as a second phase. Structure refinement ofpure K-HTB samples using Rietveld fitting procedures reveal a decrease in a and an increasein c lattice parameters with increasing nominal V content. The elemental compositions of thepure samples were determined by SEM/EDX analysis and show an increase in V content withincreasing y. The samples with nominal composition K0.5VyW1-yO3 show pure tetragonaltungsten bronze (TTB) type structure up to y = 0.05. Investigations of the optical reflectivity
and the infrared absorption spectra of powder K0.3VyW1-yO3 (HTB) samples indicate adecreasing polaron concentration with increasing V content.

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MS12-6

Invited and Oral

Charge Density study from high-resolution powder
diffraction data
Eiji Nishibori1, Shinobu Aoyagi1, Hiroshi Sawa1
Department of Applied Physics, Nagoya University, Nagoya, 464-8603, Japan(o47271a@cc.nagoya-u.ac.jp)

The electron density distribution in materials determines their properties and functions. The
structure factors from x-ray diffraction give information of total electron density distribution
including both the core and the valence electrons. Required accuracy of structure factors for
accurate charge density study is much higher than that of normal crystallographic structural
study in atomic level, where main concern is atomic arrangement.
The accuracy of powder diffraction data has been considered to be much poorer than that of
the single crystal diffraction method due to the following reasons. Firstly, the measured
integrated Bragg intensities are relatively weak. Secondly, it is difficult to obtain theindividual integrated Bragg intensities due to peak overlaps and some other relatively minor
reasons. Therefore, it has been considered that the powder diffraction data is not appropriate
for accurate charge density studies.
Recent progress of synchrotron powder x-ray diffraction technique including the third
generation synchrotron x-ray source such as SPring-8, detector, measurement system andanalytical method provides us a possibility to obtain accurate structure factors for charge
density studies. We have recently developed the both experimental and analytical techniques
based on multi-powder diffraction data1) for an improvement of the accuracy of the data. The
method have been successfully applied charge density studies of silicon, diamond, andCoSb32) by Maximum Entropy Method (MEM). The MEM provides total charge density ofmaterial from experiment. For an observation of valence electrons from experiment,
additional analytical techniques are required.
Recently, we have carried out various types of accurate structural studies, the multi-polerefinement, anharmonic thermal factor refinement, and Bader topological analysis, of several
kinds of inorganic materials from multi-powder diffraction data. Furthermore, we havedeveloped a new method for the determination of the experimental valence charge density by
a combination of the MEM and the multi-pole refinement. The experimental valence charge
densities of some inorganic materials from high resolution (d>0.2Å) multi-powder data will
be presented.
References
1.
2.

Nishibori E., Sunaoshi E., Yoshida A., Aoyagi S., Kato K., Takata M., Sakata M., Acta
Crystallographica, A63 (2007) 43-52
Ohno, A,, Sasaki, S, Nishibori,E., Aoyagi, S., Sakata,M., Iversen, B. B. Physical Review B76.
(2007) 064119.

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AsCA’09

Invited and OralInterplay between the crystalline and magnetic
structures in lightly Cr-doped
Bi0.37Ca0.63Mn0.96Cr0.04O2.9

MS12-7

Wen-Hsien Li1,.Chun-Chuen Yang1, Chun-Ming Wu1, Jirong Sun2, Jeffrey W. Lynn3
1
Center for Neutron Beam Applications and Department of Physics, National Central
University, Jhongli, 32001 Taiwan (whli@phy.ncu.edu.tw)
2State Key Laboratory for magnetism, Institute of Physics and Center for Condensed
Matter Physics, Chinese Academy of Science, Beijing, 10008 China.
(jrsun@g203.iphy.ac.cn)
3
NIST Center for Neutron Research, National Institute of Standards and Technology,
Gaithersburg, MD 20899, USA (Jefrey.Lynn@nist.gov)

The strong interplay between the crystalline structure, electrical transport and spin magnetism
has generated a large variety of interesting properties in hole-doped perovskite manganeseoxides (Ln1-xAx)(Mn1-yBy)O3, where Ln is a lanthanide ion, A is an alkaline-earth metal and B
is a transition metal. It is known that the physical properties of this class of materials are
sensitive to A-site as well as B-site doping. Generally speaking, A-site doping creates a
Mn3+/Mn4+ mixed-valence state that not only affects the carrier density but also significantly
influences the colossal magnetoresistance exhibited by this class of material. B-site doping, on
the other hand, disrupts the electrically and magnetically active Mn-O-Mn network,
weakening the double exchange (DE) interaction, and is believed to be detrimental to the
conduction mechanism. Here, we report on the results of studies made on the interplay
between the crystalline and magnetic structures of a 4% Cr-doped Bi0.37Ca0.63Mn0.96Cr0.04O2.99
by ac magnetic susceptibility, electrical resistivity, and neutron diffraction measurements. The
compound crystallizes into a monoclinic P21/m symmetry, where Mn-trimers are formed
along the [101] and [101] crystallographic directions. A Jahn-Teller distortion occurs at 280
K. The thermal behavior of charge transport may be described by a three-dimensional variable
range hopping conduction. Strong interplay between the localized magnetic electrons and theitinerant electrons are clearly revealed as the localization length increases by 20% when the
Mn spins become ordered. The Mn spins order at 85 K, but short range magnetic correlations
persist up to 160 K. Exchange integrals favor a magnetic structure with the moments pointing
in the [101] direction, which agrees well with the magnetic structure proposed based on theneutron magnetic diffraction patterns. Both the Jahn-Teller transition and the magnetic
ordering temperature are substantially reduced with Cr doping compared to the undoped
system.

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AsCA’09

Invited and Oral

The structure of rat liver vault

MS13-1

Hideaki Tanaka,1Koji Kato,1 Eiki Yamashita,1 Tomoyuki Sumizawa,2 Yong Zhou,3
Min Yao,3 Kenji Iwasaki,1 Masato Yoshimura,4 and Tomitake Tsukihara1,5
1
Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita, Osaka
565-0871, Japan,
2
University of Occupational and Environmental Health, 1-1 Iseigaoka, Yahatanishi,
Kitakyushu, Fukuoka 807-8555,
3
Faculty of Advanced Life Sciences, Graduate School of Life Sciences, Hokkaido
University, Sapporo, Hokkaido 060-0810, Japan,
4
National Synchrotron Radiation Research Center, 101 Hsin-Ann Road, Hsinchu Science
Park, Hsinchu 30076, Taiwan,
5
Department of Life Science, University of Hyogo, 3-2-1 Koto, Kamighori, Akoh, Hyogo
678-1297, Japan. (e-mail: tsuki@protein.osaka-u.ac.jp)

Vaults are large barrel-shaped ribonucleoprotein particles that are highly conserved in a wide
variety of eukaryotes. Though several functions have been
proposed for vaults since their first discovery in 1986, includingroles in multidrug resistance, cell signaling and innate immunity,
their cellular function remains unclear. Most vault particles arepresent in the cytoplasm, but a few of them localize to the
nucleus. Rat liver vault comprises a small untranslated RNA
consisting of 141 bases (vRNA) and three proteins. The
sequences of these proteins are known for the human vault. The
99-kDa major vault protein (MVP) is the major structural protein
and can self-assemble to form vault-like particles, the 193-kDa
vault poly(ADP-ribose)polymerase presumably ribosylates
substrates, and the 290-kDa telomerase-associated protein 1 isimportant for stabilization of vRNA.
On the basis of the X-ray structure, which was of an empty vault built from a cysteine-tagged
construct of MVP (termed cpMVP vaults), cpMVP vault was proposed to comprise 96 MVP
molecules each folding into 14 domains. 48 MVP molecules were proposed to extend between
the middle and each tip of the vault, so that the cpMVP vault exhibited 48-fold dihedral
symmetry(1). However, our crystallographic analysis of rat liver vault, at 10 Å resolution,
demonstrated that the particle exhibits 39-fold dihedral symmetry instead of 48-fold dihedral
symmetry (2).We have determined the X-ray structure of rat liver vault at 3.5 Å resolution (3)and show that the cage structure consists of a dimer of half vaults, with each half vault
comprising 39 identical major vault protein (MVP) chains (Figure). Each MVP monomer
folds into 12 domains; nine structural repeat domains, a shoulder domain, a cap-helix domain
and a cap-ring domain. Interactions between the 42-turn long cap-helix domains are key tostabilizing the particle. The shoulder domain is structurally similar to a core domain of
stomatin, a lipid-raft component in erythrocytes and epithelial cells.
References
1.
2.
3.

D. H. Anderson, V. A. Kickhoefer, S. A. Sievers, L. H. Rome, D. Eisenberg, PLoS Biol. 5, e318(2007).
Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, Masato Yoshimura, Eiki Yamashita, Kenji Iwasaki
and Tomitake Tsukihara, Acta Crystallogr. D 64, 525-531 (2008).
H. Tanaka, K. Kato, E. Yamashita, T. Sumizawa, Y. Zhou, M. Yao, K. Iwasaki, M. Yoshimura and- 72 -

AsCA’09

Invited and Oral

T. Tsukihara, Science, 323, 384-388 (2009).

Recognition of Nuclear Export Signal by CRM1

MS13-2

Xiuhua Dong, Anindita Biswas, Katherine Suel, Laurie Jackson, Hongmei Gu, Rita
Martinez, Yuh Min Chook
Dept. of Pharmacology, UT Southwestern, 6001 Forest Park, Dallas, TX 75390-9041,
USA (yuhmin.chook@utsouthwestern.edu)

CRM1 (also known as XPO1 and exportin 1) mediates nuclear export of hundreds of proteinsthrough the recognition of the leucine-rich nuclear export signal (LR-NES). Here we present
the 2.9 Å structure of CRM1 bound to snurportin 1 (SNUPN). Snurportin 1 binds CRM1 in a
bipartite manner by means of an amino-terminal LR-NES and its nucleotide-binding domain.
The LR-NES is a combined a-helical-extended structure that occupies a hydrophobic groove
between two CRM1 outer helices. The LR-NES interface explains the consensus hydrophobic
pattern, preference for intervening electronegative residues and inhibition by leptomycin B.
The second nuclear export signal epitope is a basic surface on the snurportin 1
nucleotide-binding domain, which binds an acidic patch on CRM1 adjacent to the LR-NES
site. Multipartite recognition of individually weak nuclear export signal epitopes may becommon to CRM1 substrates, enhancing CRM1 binding beyond the generally low affinity
LR-NES. Similar energetic construction is also used in multipartite nuclear localization
signals to provide broad substrate specificity and rapid evolution in nuclear transport.

NEMO regulates NF-κB activation by specificrecognition of linear
ubiquitin chains

MS13-3

Simin Rahighi1,2 , Fumiyo Ikeda3,, Masato Kawasaki1,2, Masato Akutsu1,2,4,
Nobuhiro Suzuki1, Ryuichi Kato1,2, Tobias Kensche3, Tamami Uejima1, Stuart
Bloor4, David Komander4, Felix Randow4, Ivan Dikic3 and Soichi Wakatsuki1,2
1
SBRC, PF, IMSS, High Energy Accelerator Research Organization (KEK), Tsukuba,
Ibaraki 305-0801, Japan (simin@post.kek.jp), (soichi.wakatsuki@kek.jp)
2
Graduate University for Advanced Studies, Hayama, Kanagawa 240-0193, Japan
3
Institute of Biochemistry II, Goethe University School of Medicine, Theodor-Stern-Kai
7, D-60590 Frankfurt (Main), Germany
4
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK

Modification of proteins by ubiquitin is critical for regulation of multiple cellular functions.
NEMO (NF-κB essential modulator) as a regulator of the NF-κB signaling is in turn regulatedby binding to ubiquitylated substrates. This study reveals that NEMO UBAN (ubiquitin
binding in ABIN proteins and NEMO) motif specifically recognizes linear (head-to-tail)ubiquitin chains and this specific recognition is required for NF-κB activation by TNF-α andother agonists in vivo. NEMO UBAN motif itself adopts a homo-dimer coiled-coil structure
which forms a hetero-tetrameric complex with linear diubiquitins. Each NEMO dimer
symmetrically accommodates two linear diubiquitin molecules, one on either side of thestructure. In each diubiquitin the distal ubiquitin is recognized through the canonical Ile44
surface and the proximal one through a novel surface which is adjacent but not overlapping- 73 -

AsCA’09

Invited and Oral

with the hydrophobic surface. The linker of the two ubiquitin moieties formed by the
C-terminal tail of the distal ubiquitin provides interaction core with the UBAN motif.
Interactions made to all four ubiquitin moieties are essential for efficient activation of NF-κB
signaling by NEMO explaining the detrimental effects of mutations in UBAN leading to
X-linked ectodermal dysplasia and immunodeficiency.

The atomic structure of granulovirus polyhedrin at
1.8Å resolution

MS13-4

Elaine Chiu1, Shin-Mei Yeh1, Richard Bunker1, Clemens Schulze-Briese and Peter
Metcalf1
1
School of Biological Sciences, University of Auckland, Thomas Building 110, 3A
Symonds Street, Auckland, New Zealand (peter.metcalf@auckland.ac.nz)
2
Swiss Light Source at Paul Scherrer Institute, Villigen 5232, Switzerland(clemens.schulze@psi.ch)

Granulovirus (Cydia pomonella betabaculovirus, CpGV) sprays are widely used as specificbiological control agents to control codling moth in apple orchards. The environmental
stability of CpGV is a result of a unique 70nm thick crystalline surface layer surrounding themembrane of each virus particle. This crystalline layer consists mainly of the 248 aminoacid protein CpGV polyhedrin, 50% identical to the amino acid sequence of the polyhedrin
produced by Autographa Californica Multicapsid Nucleopolyhedrovirus (AcMNPV), the typespecific baculovirus. In AcMNPV and other alphabaculoviruses, polyhedrin in the nucleus of
infected cells forms larger cubic crystals, which contain numerous virus particles. CpGV areabout 400nm long and contain only a few thousand unit cells surrounding a single virus
particle. In spite of the small size, CpGV diffract X-rays to at least 3.2Å resolution in powder
experiments. We expressed CpGV polyhedrin in insect cells obtaining intracellular
micro-crystals, which were used to determine the atomic structure at 1.8Å resolution. The talkwill describe the structure of crystalline surface layer of granulovirus, determined using both
single crystal micro-crystallography and powder methods.

Crystal structure of human REV7 in complex with
REV3 fragment

MS13-5

Kodai Hara1, Toshiyuki Shimizu1, Yoshiki Murakumo2, Shunsuke Kobayashi3,
Toshiaki Kogame3, Satoko Akashi1, Satoru Unzai1, Tomo Hanafusa4, Haruo
Ohmori4, Shunichi Takeda3, Mamoru Sato1, Hiroshi Hashimoto1
1
Yokohama City University, Graduate School of Nanobioscience, 1-7-29 Suehiro-cho,
Tsurumi-ku, Yokohama 230-0045, Japan (hash@tsurumi.yokohama-cu.ac.jp)
2
Nagoya University, Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku,
Naogya 466-8550, Japan
3
Kyoto University, Graduate School of Medicine, Konoe Yoshida, Sakyo-ku, Kyoto
606-8501
4
Kyoto University, Institute of Virus Research, 53 Shogoin, Kawara-cho, Sakyo-ku,
Kyoto 606-8507, Japan

Trans-Lesion DNA synthesis (TLS) is one strategy of DNA damage tolerance mechanisms toallow continuation of DNA synthesis at damaged template. TLS consists of two major- 74 -

AsCA’09

Invited and Oralprocesses, nucleotide insertion at the lesion site and extension. DNA polymerase ζ (Polζ ) is
one of key player in TLS and it acts as both inserter and extender. Polζ is composed of
catalytic REV3 and regulatory REV7 subunits. Furthermore, REV7 also interacts with REV1,
which is also a key DNA polymerase in TLS. In addition, REV7 involves in multiple
protein-protein interactions in various cellular functions including transcription and cell-cycle
check point. For instance, REV7 interacts with ELK1 and a phosphorylated form of JNK in
response to DNA damage and cell stress. Several studies also suggest that REV7 can inhibit
the anaphase promoting complex (APC) through interactions with CDH1 in G2/M phase.
Recently, it has been reported that a Shigella effector IpaB interferes the inhibition of APC byinteracting with REV7, thereby causing cell-cycle arrest. Although REV7 plays a role of an
adopter protein in various cellular functions, the mechanism of those interactions by REV7
still unknown. Here we report the crystal structure of human REV7 in complex with human
REV3 fragment. The structure of REV7-REV3 complex revealed that the C-terminal regionof REV7 wrapped the REV3 fragment, thereby adopting a knot structure. Furthermore, we
performed the pull down assay by using REV7 mutants and REV3 and revealed themechanism of the interaction of REV7 with REV3.

High-Pressure Synthesis and Superconducting
Properties of Oxygen-deficient Oxypnictide
Superconductors LnFeAsO1-y

MS14-1

H. Eisaki1,5, K. Miyazawa1,2, M. Nakajima1,3,5, S. Ishida1,3,5, M. Ishikado1,4,5, K.
Kihou1,5, P. M. Shirage1, C. H. Lee1,5, N. Takeshita1,5, R. Kumai1,5, Y. Tomioka1,5, H.
Kito1,5, K. M. Kojima3,5, T. Ito1,5, S. Shamoto4,5, S. Uchida3,5, A. Iyo1,2, 5
1National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Central
2, Umezono, Tsukuba, Ibaraki, 305-8568, Japan. (h-eisaki@aist.go.jp)
2
Department of Applied Electronics, Tokyo University of Science, 2641 Yamazaki, Noda,
Chiba 278-3510, Japan.
3
Dept. of Physics, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
4
Quantum Beam Science Directorate, Japan Atomic Energy Agency, Tokai, Naka,
Ibaraki, 319-1195, Japan.
5JST, Transformative Research-Project on Iron Pnictides (TRIP), 5, Sanbancho,
Chiyoda, Tokyo 102-0075, Japan.

We have synthesized a series of oxygen-deficient, fluorine-free oxypnictide superconductor,
LnFeAsO1-y (Ln: rare-earth) using high-pressure technique. Superconductivity shows up by
introducing oxygen deficiency and sharp superconducting transition with their transition
temperature higher than 50K is observed for heavier Ln’s (Nd, Sm, Gd, Tb, and Dy). The
effects of oxygen deficiency, variation of Ln ions, and the external pressure on Tc indicate thestrong influence of the crystal structure on the superconducting properties of the oxypnictide
superconductors.

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MS14-2Invited and Oral

Diffraction study on the Fe-based high temperature
superconductors
Wei Bao
Department of Physics, Renmin University of China, 59 Zhongguancun Ave., Haidian
District, Beijing, 100872, China (wbao@ruc.edu.cn)

High temperature superconductivity has been discovered recently in the ZrCuSiAs, ThCr2Si2
and PO structures, with the FeAs(Se) antifluorite layer as the common structural building
block [1]. We will present our neutron diffraction study on crystal and magnetic structures of
NdFeAs(O,F) [2], BaFe2As2 [3] and Fe(Se,Te) [4] superconductor systems. The NdFeAsO
and BaFe2As2 share the same in-plane magnetic structure. But the rare-earth magnetic ion Nd
alters the interlayer magnetic moment alignment from antiparallel to parallel. Such a result
was also later found to be the case for Ce or Pr materials of the ZrCuSiAs family. The FeTe
has a very different in-plane magnetic order than that for the previous two systems. Since all
three systems have the similar Fermi surface geometry, the prevailing spin-density-wave
nesting Fermi surface mechanism proposed for antiferromagnetic order in these materials
does not look as convincing as before our results of FeTe was reported. And localized
magnetism mechanism should deserve a better evaluation.
Combined x-ray and neutron diffraction techniques, we demonstrate for the first time thecoexistence of antiferromagnetic order and superconductivity in the ThCr2Si2 family ofmaterials, using (Ba,K)Fe2As2 as samples [5]. This differs from cuprate high temperature
superconductors, for which long-range antiferromagnetic order and superconductivity exist
side-by-side. The coexistence would provide constraint on the possible superconducting orderparameter. Our result has been since confirmed in other Ni or Co doped BaFe2As2 systems
by other groups.
References[1] Y. Kamihara et al., J. Am. Chem. Soc. 130, 3296 (2008); M. Rotter et al., Phys. Rev. Lett. 101, 107006(2008); F.-C. Hsu et al., PNAS 105, 14262 (2008).
[2] Y. Qiu et al., Phys. Rev. Lett. 101, 257002 (2008).
[3] Q. Huang et al., Phys. Rev. Lett. 101, 257003 (2008).
[4] W. Bao et al., Phys. Rev. Lett. 102, 247001 (2009).
[5] H. Chen et al., Europhys. Lett., 85, 17006 (2009).

MS14-3

Electric Polarization Flop and Magnetic Phase
Transition Induced by Magnetic Field in Multiferroic
RMn2O5 (R = Tm, Yb)
Hiroyuki Kimura1, Yuma Sakamoto1, Mamoru Fukunaga1, Yukio Noda1, Nobuyuki
Abe1, Kouji Taniguchi1, Taka-hisa Arima1, Shuichi Wakimoto2, Kazuhisa Kakurai2
1
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University,
Katahira 2-1-1, Aoba, Sendai 980-8577, Japan (kimura@tagen.tohoku.ac.jp)
2Japan Atomic Energy Agency

Multiferroic RMn2O5 (R = rare-earth, Bi, Y) is well known as an antiferromagnetic,
ferroelectric material showing a colossal magnetoelectric (CME) effect. This system has arich variety of dielectric responses induced by the application of magnetic field, of which- 76 -

AsCA’09

Invited and Oral

behaviors strongly depend on the type of rare-earth ions. Recently, we have found that in
TmMn2O5, electric polarization flops from b-axis to a-axis with decreasing temperature underzero-magnetic field [1]. Previous report on TmMn2O5 shows that the polarization along b-axis
was induced by applying magnetic field [2]. These facts indicate that the polarization flopfrom a-axis to b-axis can be induced by magnetic field in this material. To confirm thispolarization flop, we conducted polarization measurement under magnetic field, resulting thatthe polarization flop occurs around H = 0.6 T as magnetic field is applied parallel to c-axis.
We also found the electric polarization flop from b-axis to a-axis in YbMn2O5, which occurs
at T = 4.2 K under H = 1.75 T as well as at T = 5.5 K under H = 0 T. Neutron diffraction
measurements for TmMn2O5 and YbMn2O5 showed that the magnetic phase transition
concomitantly takes place at the transition of polarization flop. We also discovered theMicroscopic magnetic phase boundaries completely agree with dielectric phase boundaries intemperature-Magnetic field phase diagram, suggesting that the flop of electric polarization istriggered by magnetic phase transition.
This work has been supported by a Grant-In-Aid for Scientific Research (A), No. 21244051,
and Grant-In-Aid for Scientific Research on Priority areas ``Novel States of Matter Induced
by Frustration'', No. 19052001, from the Ministry of Education, Culture, Sports, Science andTechnology.

Effect of Ga3+ Substitution for Mn3+ on Magnetic andDielectric Properties in Multiferroic YMn2O5

MS14-4

Yuma Sakamoto1, Hiroyuki Kimura1, Satoru Horio1, Arno Fey1, Mamoru
Fukunaga1, Ryoji Kiyanagi1, Yukio Noda1, and Hiraka Haruhiro2
1
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University,
Katahira 2-1-1, Aoba, Sendai 980-8577, Japan (yuma@mail.tagen.tohoku.ac.jp)
2
Institute of Materials Research, Tohoku University Katahira 2-1-1, Aoba, Sendai
980-8577, Japan

Multiferroic RMn2O5 (R = rare-earth, Bi, Y) shows ferroelectric and antiferromagnetic
ordering simultaneously and a colossal magnetoelectric effect (CME). This suggests strong
correlation between the magnetism and dielectricity. The magnetic phases of YMn2O5 include
a two-dimensional incommensurate (2D-ICM) phase, a 1D-ICM phase, a commensurate (CM)phase and another low temperature 2D-ICM (LT2D-ICM) phase. The ferroelectric (FE) phaseis first realized in the CM phase, and then changes to the so-called weak ferroelectric (WFE)
phase in the LT2D-ICM phase. We revealed that a transverse spin spiral structure of Mn4+O6
octahedron chains along the c-axis is established in the CM phase [1] and in the LT2D-ICM
phase [2], and then two independent Mn4+O6 chains are connected by Mn3+O5 pyramid. From
the Si x Si+1 mechanism, this chiral spin structure along the c-axis produces macroscopic
electric dipolemoment along the b-axis. On the other hand, antiferromagnetic interaction in
the ab-plane plays another possible origin to produce the electric dipolemoment due to theso-called magnetoelastic coupling.
In order to understand the roles of the magnetic moments of Mn4+ and Mn3+ ions,non-magnetic ions, Ga3+, were introduced at the site of Mn3+ (YMn4+(Mn1-xGax)3+O5),
diluting the mean magnetic moment at that site. Thus, we expect the nonmagnetic Ga3+ ion- 77 -

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will disconnect the interaction between Mn4+O6 octahedron chains. In turn, the role of Mn4+O6
octahedron chains becomes clear.
Neutron diffraction and electric measurements show steep decrease of the FE and CM phaseas the concentration of Ga3+ increases. Meanwhile the phase transition temperature of
LT2D-ICM remains almost unchanged. Therefore the Ga-doping was found to suppress the
FE and CM phase. This means that the FE and CM phase is produced by the interaction
between Mn4+O6 octahedron chains, while the WFE and LT2D-ICM phase is produced by thechiral spin structure of Mn4+O6 octahedron along the c-axis.
This work has been supported by a Grant-In-Aid for Scientific Research (A), No. 21244051,
and Grant-In-Aid for Scientific Research on Priority areas ``Novel States of Matter Induced
by Frustration'', No. 19052001, from the Ministry of Education, Culture, Sports, Science andTechnology.
References[1] Y. Noda, H. Kimura, Y. Kamada, T. Osawa, Y. Fukuda , Y. Ishikawa, S. Kobayashi, Y. Wakabayashi,
H. Sawa, N. Ikeda and K. Kohn, Physica B 385-386 (2006) 119-1122.
[2] J.-H. Kim, S.-H. Lee, S. I. Park, M. Kenzelmann, A. B. Harris, J. Schefer, J.-H. Chung, C. F. Majkrzak,
M. Takeda, S. Wakimoto, S. Y. Park, S-W. Cheong, M. Matsuda, H. Kimura, Y. Noda, and K. Kakurai,
Phys. Rev. B78(2008) 245115(10pp).

MS15-1

Electron Microscopy of Low-Dimensional
Nanomaterials
Fangfang Xu
Shanghai Institute of Ceramics, Chinese Academy of Sciences, 1295 Dingxi Road,
Shanghai, 200050, China (ffxu@mail.sic.ac.cn)

Crystallography in micro- or nano-scale could be resolved via electron microscopy (EM)taking advantages of its high spatial resolution, variety of electron diffraction (ED) techniques,
and local chemical information. Revealing the micro-crystallography can bring about a lot of
useful informations of materials including the formation mechanism, growth habit, andspecifically, the nature of properties. Here, we present our work during the past few years on
the EM of low-dimensional nanomaterials which have exhibited promising applications in
nanoelectronics, nanophotonics and biotechnology.
The researches to be introduced include a new tubular structure of graphite-type nanotubes1,2,
new polytypes of graphitic BN3, crystallography of Co@BN nanocables4, growth mechanismof one-dimensional (1D) nanomaterials generated without any catalysts or templates5, anddefect structures in niobate nanosheets6. Electron diffractions discovered a new tubular
structure of hexagonal BN showing an Archimedes spiral geometry (Fig.1). Complete
structural models have been established for this new tubular form, taking into account of
disclination angles, coincidence site lattices and centers of disclination operation. The specificconical helix structures of BN nanotubes have been found to exhibit some interesting
structural and mechanical properties, i.e. the structural parameters could be tailored via heat
treatment and the nanotubes behaved like a metallic spring. New polytype structures ofgraphitic BN, i.e. 12R and 24R, have been observed in BN fibers as revealed by EDs and high- 78 -

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Invited and Oral

resolution electron microscopy (HREM). EM of Co@BN nanocables figured out the
crystallography of Co-B phase inside the small volume of nanotubes and the structural
relations between the metal core and tubular shell. HREM and structural modeling revealed
1D growth of crystals dominated by pseudo-screw packing of polyhedral growth units in avapor-phase (VP) kinetics (Fig.2). Crystallography of niobate nanosheets have been studied
focusing on the defect and surface structures. Dynamics of defects have been examined via
in-situ EM, induced by either heating or electron irradiation. These researches proved that EMshould be a powerful and effective tool for the analysis of crystallography in very small scale.

Fig. 1 Structures of tubular conical helix.

Fig. 2 1D growth mechanism in VP processes.

References
1. F. F. Xu, Y. Bando, R. Ma, D. Golberg, Y. Li and M. Mitome, J. Am. Chem. Soc., 125 (26) 8032-8038(2003).
2. F. F. Xu and Y. Bando, Acta Crystallogr. A, 59, 168-171 (2003).
3. F. F. Xu, Y. Bando and M. Hasegawa, Chem. Commun., 14, 1490-1491 (2002).
4. F. F. Xu, Y. Bando, D. Golberg, M. Hasegawa and M. Mitome, Acta Mater., 52 (3) 601-606 (2004).
5. F. F. Xu, L. L. Zhang, X. F. Du and Y. C. Zhu, Cryst. Growth Des., 8 (7) 2574-2580 (2008).
6. F. F. Xu, Y. Ebina, Y. Bando and T. Sasaki, J. Phys. Chem. B, 107 (28) 6698-6703 (2003), 107 (36)9638-9645 (2003).

3 Dimensional Coherent Electron Difractive Imagingof Nanoparticle

MS15-2

Fu-Rong Chen1,2, Roman Dronyak,1,2, Keng S. Liang2
1
Department of Engineering and System Science, National Tsing Hua University,
Hsinchu 30013, Taiwan (frchen@ess.nthu.edu.tw)2
National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan(dronyak@nsrrc.org.tw)

The electron diffraction pattern from a faceted MgO nanoparticle was phased using coherent
diffractive imaging (CDI) technique. The primary limitations of the accurate and reproducible
inversion of the electron diffraction pattern are due to the difficulty in treating experimental
noises, substrate scattering and partial spatial coherence of the incident beam. Furthermore,
the reconstruction of the complex-valued exit wave function requires sufficiently tightboundary of the sample called “support”. In this work, we present the phase recovery
procedure that utilizes guided hybrid input-output (GHIO) algorithm with dynamic support toreconstruct the stable and reproducible solution by optimizing feedback parameter of thealgorithm and threshold value for dynamic support. To quantify the spatial accuracy ofrecovered result the deviation map was obtained as a relative standard deviation of the- 79 -

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Invited and Oral

averaged solution. The result shows that the reproducible solution can be deduced fromdiffraction patterns only, without information from TEM image [1-2].
Figure 1 shows recovered shape and exit wave of the sample with their deviation maps. The
contrast decay at the edges and corners of the sample is due to the thickness decrease of the
faceted nanoparticle. The region of low accuracy in the exit wave is comparable with theresolution of the recovered shape function. It may be due to the large amount of missed weak
scattering signals in the recorded diffraction patterns. Therefore, it complicates imaging the
local structure at atomic resolution, such as for single-atom defects. The optimization analysis
and effects of the incident illumination on the phase recovery technique will be discussed indetail.
Tree dimensional diffraction data around Bragg peak of {020} were recorded by rotating
nano-particle along [220] axis every 0.1 degree. As shown in Fig. 2, the 3 dimensional CDI
exit wave was reconstructed using from 34 diffraction data spanned 3.4 degree. The
reconstruction algorithm and result will be discussed in detail.

Fig.1 the reconstructed exit wave of MgO nanoparticle

Fig.2 the 3-D reconstructed EW

References[1] R. Dronyak, C.-K. Feng, K. S. Liang and F.-R. Chen. Electron diffractive imaging of the MgOnano-particle: towards atomic-resolution. XXI IUCr Congress and General Assembly, Osaka. Acta
Cryst. A64, C130 (2008).
[2] This work was supported by the National Science Council (NSC 97-2112-M-213-001 and NSC
95-2221-E-007-093) and the Thematic Project of Academia Sinica of Taiwan.

MS15-3High-resolution Structural Analysis of Membrane
Proteins by Electron Crystallography
Kaoru Mitsuoka
Biomedicinal Information Research Center (BIRC), National Institute of Advanced
Industrial Science and Technology (AIST), 2-41-6 Aomi, Koto-ku, Tokyo, 135-0064,
Japan (kaorum@ni.aist.go.jp)

Transmission electron microscopy at low temperatures, cryoEM, of biological specimens
provides several unique possibilities such as obtaining a very broad spatial informationinterval reaching from cellular to atomic dimensions, understanding functionally relevant
conformational changes from heterogeneous samples and localization of individualcomponents in large systems. It is also possible to study biomolecules in a close to naturalenvironment, e.g. membrane proteins in a lipid bilayer. The branch of cryoEM that is using- 80 -

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periodically assembled biomolecules in the form of two-dimensional (2D) crystals is termed
electron crystallography and can provide structural information at a resolution level whichallows building of atomic models.
The superfamily of proteins called Membrane Associated Proteins in Eicosanoid andGlutathione metabolism (MAPEG) are relatively small membrane-bound enzymes. The
substrates of these proteins are in most cases hydrophobic molecules and the active sites arelocated in the lipid embedded parts of the polypeptide chains. Thus, in order to obtain adetailed understanding of the mechanism and to determine interactions with substrates andinhibitors it is of fundamental importance that the enzymes are located in a lipid bilayer
environment during experiments. Electron crystallography is thought to be a suitable method
because of this reason.
We have chosen to study MAPEG members and their interaction with small molecules
because of human health relevance in general and particularly since several of these proteins
constitute potential drug targets against common diseases. Moreover, we know from previous
work that they are prone to form 2D crystals suitable for high-resolution electron
crystallographic analysis. The detoxification enzyme microsomal glutathione transferase 1,
MGST1, was the first MAPEG structure to be determined (1). The structure of rat MGST1, at
3.2 Å resolution, solved in complex with glutathione, defines the active site location and acytosolic domain involved in enzyme activation.
More recently we have also obtained an atomic model of microsomal prostaglandin E
synthase 1, MPGES1 (2). This MAPEG member is of particular importance in medicine since
it is the inducible, terminal enzyme in the cascade of events that leads to the formation of
prostaglandin E2, a potent mediator of pain, fever and inflammation. Together with resultsfrom site-directed mutagenesis and activity measurements, we can thereby demonstrate therole of specific amino acid residues. Glutathione is found to bind in a U-shaped conformation
at the interface between subunits in the protein trimer. It is exposed to a site facing the lipid
bilayer, which forms the specific environment for the oxidoreduction of PGH2 to PGE2 after
displacement of the cytoplasmic half of the N-terminal transmembrane helix. Hence, insight
into the dynamic behavior of MPGES1 and homologous membrane proteins in inflammationand detoxification is provided.
In addition, we will discuss about our recent efforts to improve the resolution of structural
analysis of aquaporin 1, a water channel, whose atomic model was first determined byelectron crystallography (3).
References
1.
2.
3.

Holm, P. J., Bhakat, P., Jegerschold, C., Gyobu, N., Mitsuoka, K., Fujiyoshi, Y., Morgenstern, R.,
Hebert, H. (2006) J. Mol. Biol. 360, 934-945.
Jegerschöld, C., Pawelzik, S. C., Purhonen, P., Bhakat, P., Gheorghe, K. R., Gyobu, N., Mitsuoka,
K., Morgenstern, R., Jakobsson, P. J., Hebert, H. (2008) Proc. Natl. Acad. Sci. USA. 105,
11110-11115.
Murata, K., Mitsuoka, K., Hirai, T., Walz, T., Agre, P., Heymann, J. B., Engel, A., Fujiyoshi, Y.
(2000) Nature, 407, 599-605.

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Invited and Oral

Strain mapping near Si/SiGe interfaces using HOLZ
line CBED patterns

MS15-4

Koh Saitoh1, Maiko Hamabe2, Nobuo Tanaka1
1
EcoTopia Science Institute, Nagoya University, Furo-cho, Chikusa-ku, Nagoya
464-8603, Japan (saitoh@esi.nagoya-u.ac.jp)
2
Department of Crystalline Materials Science, Nagoya University, Furo-cho,
Chikusa-ku, Nagoya 464-8603, Japan

Lattice strain is one of the important parameters, which influences the physical properties ofcrystalline materials, especially in the modern semiconductor industry. Convergent-beamelectron diffraction (CBED) may provide one of the best solutions for such industrial
requirements, due to its high spatial-resolution and accuracy. In the lattice parameter
determination by CBED, the positions of higher-order Laue zone (HOLZ) lines in the 000
disc are fitted between the experimental and simulated patterns. However, the splitting of
HOLZ lines, which are often observed in CBED patterns taken at a vicinity to interfaces andsurfaces, prevents the conventional technique (Fig. 1). It has been reported that the splitting of
HOLZ lines is caused by a bending distortion of the lattice and can be determined by thefitting of intensity profiles across the HOLZ lines in experimental CBED patterns todynamical simulations. Such dynamical simulations, however, are unsuitable for practicaluse because of its huge calculation cost.
In the present study, we propose a simple method to determine the bending strain of a lattice
together with lattice constants on the basis of the kinematical diffraction theory and theHough transform technique. The method is applied to determine bending strains in a Si
substrate region close to a Si/SiGe interface.
Fig. 2 shows a schematic diagram of a lattice with a bending strain. Each lattice point isdisplaced in the x-direction, whose displacement magnitude depends on the z-coordinate (thedirection of incident electron). It is found that the scattering amplitude, which is originallypeaked at the reciprocal lattice points in the non-bended lattice, shows a split of the peaks in
the kz-direction, resulting in the splitting of HOLZ lines. We confirmed that the width of the
splitting is approximately proportional to |g•R|, inner product of the lattice displacement
vector R and the reciprocal lattice vector g. Figs. 3(a) and 3(b) show simulations of the Si[320] HOLZ line pattern without a bending strain and with a bending strain with R//[001],
respectively. By a fitting of the experimental and simulated patterns using the Houghtransform technique for a series of HOLZ line patterns taken from a region near the Si/SiGeinterface, a two-dimensional strain distribution is visualized.

Fig.1: Si [320] HOLZ line
pattern taken from a region
near a Si/SiGe interface.

Fig.2: Model of a latticewith a bending strain.

- 82 -

Fig.3 HOLZ line patterns simulated from lattices
without a bending strain (a) with a bending strain (b).

AsCA’09

MS15-5Invited and Oral

Visualization of the orbital-ordered state of FeCr2O4
using the CBED method
Daisuke Morikawa, Kenji Tsuda, Shintaro Ohtani and Takahisa Arima
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University,
Japan, 2-1-1 Katahira, Aoba-ku, Sendai, 9808577,Japan(morikawa@mail.tagen.tohoku.ac.jp)

A structure analysis method using convergent-beam electron diffraction (CBED), which wasdeveloped by Tsuda and Tanaka[1,2], enables us to directly determine the electrostatic
potential from a nanometer-scale specimen area. The electron density distribution can be also
obtained from the electrostatic potential through the Poisson's equation. We have applied themethod to a spinel oxide FeCr2O4, which undergoes a structural phase transformation at 135K
from a cubic spinel structure of the high-temperature phase to a tetragonal structure of the
low-temperature phase with Jahn-Teller (JT) distortion [3]. A ferro-type orbital-ordering of 3delectrons of the Fe atoms is expected to occur in the low-temperature phase [4].
FeCr2O4 single crystals were grown by the chemical vapor transport (CVT) method.
Energy-filtered CBED patterns of the low-temperature phase were obtained at specimen
temperature of 90K using an energy-filter transmission electron microscope (EFTEM)
JEM-2010FEF with an accelerating voltage of 100kV. Atom positions, Debye-Waller factors
and low-order structure factors were refined by nonlinear least squares fitting between theexperimental CBED patterns and dynamical diffraction calculations using analysis software
MBFIT [1]. The electrostatic potential and electron density distributions were reconstructedfrom the refined parameters.
Figure (a) shows the result of the present CBED analysis, the 4e/Å3 isosurface of the electron
density colored with electrostatic potential at the Fe-O tetrahedron. Clear anisotropy of theelectrostatic potential has been found in the c-direction, being attributed to the ferro-type
3z2-r2 orbital ordering.
For comparison, the electrostatic potential and electron density of the orbital-ordered state has
been simulated using non-spherical scattering factors for the Fe 3z2-r2 orbital [5]. The
non-spherical scattering factors were applied to the same low-order structure factors as thosedetermined in the CBED experiments. It is seen that the simulated result of Fig. (b) shows
very good agreement with the experimental one.

Figures (a) and (b): 4e/Å3 isosurfaces of electron density colored with electrostatic potential at Fe-O
tetrahedral, obtained from (a) the present CBED analysis and (b) the simulation using non-sphericalscattering factors.
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Invited and Oral

References[1] K. Tsuda & M. Tanaka, Acta Cryst. A55, 939-954 (1999).
[2] K. Tsuda et al., Acta Cryst. A58, 514-525 (2002).
[3] G. Shirane & D. E. Cox, J. Appl. Phys. 35, 954 (1964).
[4] T. Arima et al., J. Magn. Magn. Mat. 310, 807 (2007).
[5] R. J.Weiss & A. J.Freeman, J. Phys. Chem. Solids. 10, 147 (1959)- 84 -

AsCA’09

RS-1

PosterSynthesis, structures and properties of modulated
fresnoites
Patryck K. K. Allen, Siegbert Schmid
School of Chemistry, University of Sydney, NSW 2006, Australia

In response to the negative environmental impact of lead-based materials, recent European
Union and Japanese legislation has introduced severe restrictions on the use of hazardous
substances in electronic equipment, creating a demand for lead-free electronic materials,
particularly piezoelectrics [1, 2]. A comprehensive understanding of the relationship between
the structural chemistry and physical properties is vital for the design and development of new,environmentally friendly electronic materials.
The fresnoite family of modulated structures, A2TiM2O8 (A = Ba, Sr; M = Si, Ge), has beenshown to exhibit excellent piezoelectric properties [3, 4], making them one of several possible
alternatives to replace PZT and other lead-based electroceramic materials. A wide range oftechniques including synchrotron X-ray diffraction, neutron powder diffraction, electron
diffraction, and differential scanning calorimetry have been used to investigate the structural
behaviour of selected members of the Ba2-2xSr2xTiSi2O8 solid solution, including temperatureand compositionally induced phase transitions.
8.42

a (P4bm)a (Cmm2)b (Cmm2)

8.40
8.38
8.36

Cell Parameter (?

This contribution will discuss a variety of thediverse aspects of this ongoing project, including
the non-trivial synthesis of the Ba2xSr2-2xTiSi2O8
series, the use of a modulated structure approach tocharacterise powder diffraction data using
Jana2006, and new evidence of the phase transition
that removes the structural modulation in
Ba2TiSi2O8.

8.34
8.32
8.30
8.28
8.26
8.24
8.22
100

Recent evidence for the coexistence of two
incommensurately modulated Sr2TiSi2O8 phases atroom temperature and results from variabletemperature X-ray powder diffraction (Figure 1)
will also be presented.

200

300

400

500

600

700

800

Temperature (K)Figure 1: Change in cell parameters a andb in Sr2TiSi2O8 when heated from 125–823 K.

References
1.
2.
3.
4.

Y. Li, K. S. Moon, C. P. Wong, Science, 2005, 308, (5727), 1419-1420.
Y. Saito, H. Takao, T. Tani, T. Nonoyama, K. Takatori, T. Homma, T. Nagaya, M. Nakamura, Nature,
2004, 432, (7013), 84-87.
Asahi, T. Osaka, J. Kobayashi, S. C. Abrahams, S. Nanamatsu, M. Kimura, Phys. Rev. B, 63, 2001, (9),1-13.
Halliyal, A. S. Bhalla, S. A. Markgraf, L. E. Cross, Ferroelectrics, 1985, 62, 27-38.

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AsCA’09

Poster

Structural and Spin Phase Transitions in the
Polymeric Hybrid Organic-Inorganic Materials

RS-2

Kittipong Chainok1,2, Stuart R. Batten3, Keith S. Murray3, A. David Rae4, Ian D.
Williams5, Kenneth J. Haller1
1
School of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon
Ratchasima 30000, Thailand (ken.haller@gmail.com)
2
Department of Chemistry, Faculty of Science, Rangsit University, Pathumtani 12000,
Thailand (Kittipong.C@rsu.ac.th)
3
School of Chemistry, Institute of Science, Monash University, Clayton, Victoria 3800,
Australia (Keith.Murray@sci.monash.edu.au, Stuart.Batten@sci.monash.edu.au)
4
Research School of Chemistry, Australian National University, Canberra, ACT 0200
Australia (rae@rsc.anu.edu.au)
5
Department of Chemistry, Hong Kong University of Science and Technology, Clear
Water Bay, Kowloon, Hong Kong, P. R. China (chwill@ust.hk)

Phase transitions in polymeric hybrid organic-inorganic materials are present. The
order-disorder structural phase transition was observed in the polymeric isomorphous
compounds of formula [M(Im)4V2O6]∞, where M = Mn, Co, Ni, Im = imidazole.[1] The phasetransition was studied by single crystal X-ray diffraction between 100 and 295 K. It wasobserved that the room temperature P42/n disordered phase is reversibly transformed to theI41/a ordered phase below 281 K for Mn and 175 K for Co. The ordered phase of Ni wasfound to have space group P2/n at 100 K. The phase transition mechanisms of thesecompounds were affected by a change of the hydrogen bond connectivity. Anotherparticularly interesting phase change is the magnetic spin-crossover (SCO) behavior found in
the 3-D framework of formula [Fe(AIBN)3](MCl4)2 where M = FeIII and InIII, AIBN =2,2'-azobisisobutyronitrile.[2] The SCO transitions were characterized by use of temperaturedependent magnetic susceptibility (2−300 K) and Mössbauer effect spectral measurements(4.2, 77 and 295 K) together with single crystal X-ray crystallography (103 and 233 K). The
data revealed that the AIBN compounds exhibit incomplete “half” SCO phenomena with noaccompanying crystallographic phase change. Taking into account for the solid state phasetransition, in the cases of formal [M(Im)4V2O6] and the later [Fe(AIBN)3](MCl4)2 compounds
are considered to be crystallographic first order phase transition and magnetic spin transition
between two electronic states (high spin → low spin) in molecular chemistry, respectively, as
evidence through careful investigation on such methods mentioned above. In addition, areview on X-ray crystal structures of another hybrid materials that have formed in attempts tobridge different aspects of solid state supramolecular chemistry and molecular crystal
engineering, and also to understand their magnetostructure correlations are also proud todescribe.[3,4]References
1.
2.
3.

Chainok, K.; Haller, K. J.; Rae, A. D.; Willis, A. C.; Williams, I. D. Investigation of the structure andphase transitions of the polymeric organic-inorganic hybrids: [M(Im)4V2O6]∞, M = Mn, Co, Ni, Im =imidazole. To be submitted to Acta Cryst. B., 2009.
Chainok, K.; Neville, S. M.; Moubaraki, B.; Batten, S. R.; Murray, K. S.; Forsyth, C. M.; Cashion, J.
D.; Haller, K. J. Synthesis, structures and spin crossover properties of infinite 3-D framework iron(II)containing organodinitrile bridging ligands. To be submitted to Dalton Trans., 2009.
Chainok, K.; Neville, S. M.; Moubaraki, B.; Batten, S. R.; Murray, K. S.; Haller, K. J.
Antiferromagnetic coupling in 3-D network NiII−NiII cyanide-bridged homometallic compounds of[Ni(CN)4Ni(en)]·2H2O and [Ni(CN)4Ni(tn)]·H2O·MeOH. To be submitted to Dalton Trans., 2009.
- 86 -

AsCA’09
4.

Poster

Chainok, K.; Neville, S. M.; Moubaraki, B.; Batten, S. R.; Murray, K. S.; Forsyth, C. M.; Cashion, J.
D.; Haller, K. J. Synthesis, structures and magnetic properties of novel cyanide-bridged FeII−MII
heterometallic compounds, MII = Mn, Ni, Cu. To be submitted to Inorg. Chem., 2009.

Charge Density Study on Metal Complexes with
Non-Innocent Ligand

RS-3

Yu-Chun Chuang1, Chou-Fu Sheu1, Gene-Hsiang Lee2, Yu Wang1,2
1
Department of Chemistry, National Taiwan University, Taipei, Taiwan(d94223006@ntu.edu.tw)
2
Instrumentation Center, National Taiwan University, Taipei, Taiwan

High resolution X-ray diffraction experiments and atom-specific X-ray absorption
experiments are combined to investigate a series of square planar complexes containing M-Sbonds. Studies on complexes of (pyH)z[M(mnt)2]-z, where M = Ni or Cu and z= 2 and 1,
pyH=C5NH6+, mnt= S2C2CN22-, are undertaken to identify the site of one electronoxidation-reduction to be at either the metal or the ligand due to the non-innocent character ofthe mnt (maleonitriledithiolate) ligand. Interestingly it is nicely demonstrated that the one
electron redox reaction of Ni and Cu series is a ligand-based and a metal-based respectively.
The metal K-, L-edge and the S K-edge X-ray absorption spectroscopy unambiguously
indicate the site of oxidation and also provide some bonding characters of the M-S bond. The
differences in geometries and in bonding characters in terms of topological properties
associated with the bond critical points will be discussed between the oxidized form (2-) andthe reduced form(1-). In the case of Ni complexes, the formal oxidation state of Ni remains as
Ni(II) and each mnt ligand carries 2- in the [Ni(mnt)2]2-; but only one of the mnt is reduced inthe [Ni(mnt)2]1-. On the contrary, in the case of Cu complexes, the mnt remains as 2- in both[Cu(mnt)2]2- and [Cu(mnt)2]1-, but the formal oxidation state of Cu is Cu(II) and Cu(III)respectively. Bond characterizations and d-orbital populations will be presented in a combined
study of experiment and theory. The complimentary results of XAS, XRD and DFT
calculations are to be discussed. The conclusion on the redox behavior will be firmly
established; the accompanied changes in M-L bonding will be illustrated.

RS-4

Topological features of short Cl…Cl contacts via
experimental and theoretical charge density analysis
Venkatesha R. Hathwar, T. N. Guru Row
Solid State and Structural Chemistry Unit, Indian institute of Science Bangalore 560012,
India (venkatesh@sscu.iisc.ernet.in)

Studies on halogen…halogen contacts in organic compounds using ab initio calculations1 andcrystallographic studies2 show that these interactions are controlled by electrostatics. Indeed,
these are represented as C-X1···X2-C moieties (where θ1=C- X1···X2 and θ2=X1···X2-C;
Rij=X1···X2 distance). Cl…Cl contacts are directive and are either attractive or repulsive basedon the geometry of contact 2. In order to decipher the specific interaction profiles of Cl…Cl
contacts in the presence of other weak O-H…N, C-H…N and C-H…O hydrogen bonds,
charge density analysis of 2-chloroquinolin-3-yl methanol and 2-chloro-3- 87 -

AsCA’09

Posterchloromethyl-8-methylquinoline have been carried out using high resolution X-ray diffraction
data (resolution, sinθ/ λ = 1.08 Å-1) collected on good quality crystals at 100 K.

Figure1. Packing diagram highlighting Cl..Cl contacts along with the
Laplacian map depicting the (3, -1) bond critical point.

The intermolecular interactions were analyzed based on Bader’s QTAIM theory3 incorporated
in XD2006 package4. Theoretical calculations of charge density analysis were carried out
using CRYSTAL065 for the comparison of observed results. The Cl…Cl short contact isobserved as a ‘closed shell’ van der Waals interaction with the (3, -1) bond critical point(Figure 1) for 2-chloroquinolin-3-yl methanol displaying Type I interaction. On the other hand,
2-chloro-3-chloromethyl-8-methylquinoline displays a type II contact and the topologicalfeatures suggest a nucleophile-electrophile interaction as observed earlier6. Further, thetopological features associated with one electron properties were analyzed in both thecompounds.
References
1.
2.
3.
4.
5.
6.

F. F. Awwadi, R. D. Willett, K. A. Peterson and B. Twamley, Chem. Eur. J. 2006, 12, 8952.
(a) K. Gnanaguru, N. Ramasubbu, K. Venkatesan, and V. Ramamurthy, J. Org.Chem., 1985, 50, 2337. (b) G.
R. Desiraju and R. Parthasarathy, J. Am. Chem.Soc. 1989, 111, 8725. (c) N. Ramasubbu,
R. Parthasarathy, and P. Murray-Rust, J. Am. Chem. Soc., 1986, 108, 4308.
R. F. W. Bader, Atoms in Molecules-A Quantum Theory, Oxford: Clarendon, 1990.
Volkov, P. Macchi, L. J. Farrugia, C. Gatti, P. Mallision, T. Richter and T. Koritsanszky, XD2006, 2006.
R. Dovesi, V. R. Saunders, C. Roetti, R. Orlando, C. M. Zicovich-Wilson, F. Pascale, B. Civalleri, K. Doll,
N. M. Harrison, I. J. Bush, Ph D’Arco and M. Linuell, CRYSTAL06, University of Torino, 2006.
T. T. Thu Bui, S. Dahaoui, C. Lecomte, G. R. Desiraju, E. Espinosa, Angew. Chem. Int. Ed. 2009, 48, 3838.

Three-dimensional structures of Gram-positivebacterial pilins

RS-5

Hae Joo Kang1, Neil G. Paterson1, Ton-That Hung2, Edward N. Baker1
1
Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences,
University of Auckland, Private Bag 92019, Auckland, New Zealand(ted.baker@auckland.ac.nz)
2
Department of Microbiology and Molecular Genetics, University of Texas Health
Science Center, 6431 Fannin St., Houston, TX 77030, USA

Bacterial pili are filamentous appendages that are critically involved in adhesion to host cells,
leading to colonization of host tissues and establishment of infections. They are built fromprotein subunits called pilins; the backbone of the pilus is formed by hundreds of copies of amajor pilin, while several minor pilins with specialized functions are associated with the- 88 -

AsCA’09

Posterbackbone. While pili of Gram-negative bacteria such as E. coli have been extensively studied,the pili on Gram-positive organisms have only recently discovered and are fundamentallydifferent in that the pilins are held together by covalent isopeptide (amide) bonds formed bysortase enzymes.
We previously determined the first atomic structure of a Gram-positive major pilin, Spy0128
from Streptococcus pyogenes (Group A Streptococcus; GAS) (1). The crystal structure of
Spy0128 showed an elongated molecule comprising two Ig-like domains. This structure also
revealed a previously unknown mechanism for stabilizing proteins, in the form of
self-generated isopeptide (amide) bonds. This brought significantly new understanding of theassembly of Gram-positive bacterial pili. The major pilins of different Gram-positive bacteria
show wide variations in size and sequence, however, making it difficult to predict whether the
structural principles seen in Spy0128 apply also to other Gram-positive pili. Here we present
the high resolution crystal structure of a major pilin from Corynebacterium diphtheriae. Thisreveals a similar modular structure of Ig-like domains, yet with several variations from
Spy0128. Two of its domains contain internal Lys-Asn isopeptide bonds which are somewhat
different from those found in Spy0128. These are strategically located to give strength andstability to the pilin subunits and also facilitate proper assembly of pilus. We also confirm, by
mass spectrometry of native pili, the identity of the residue used in pilus polymerization andnote a pilus-like assembly of this C. diphtheriae pilin molecules in the crystal. These results
point to a likely common architecture for the shafts of many Gram-positive pili, with several
variations that can account for their functional differences.
Reference
Hae Joo Kang, Fasséli Coulibaly, Fiona Clow, Thomas Proft and Edward N. Baker (2007), Stabilizing
isopeptide bonds revealed in Gram-positive bacterial pilus structure, Science, 318, 1625-1628.

RS-6

Crystal Structure determination of a non-Pfam protein
AF1514 by S-SAD using a Cr X-ray source
Yang Li, Neil Shaw,Gaojie Song,Chongyun Cheng ,Jie Yin, Zhi-Jie Liu
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of
Sciences, Beijing, China

Most of the targets selected by many structure genomics centres are from Pfam protein
families. Many Pfam sequences have significant biological meaning, while the functions ofmost non-Pfam sequences are unknown to date. However, this does not mean that non-Pfam
sequences are biologically less meaningful. Some non-Pfam sequences and structures are
predicted to play important roles for the uniqueness of these organisms. The present work
describes the structure determination of AF1514, a non-Pfam protein from Archeoglobus
fulgidus with unknown function, solved at 1.8 Å resolution by using anomalous signal ofsulphur atoms generated by chromium X-rays (wavelength = 2.29Å).

- 89 -

AsCA’09

Poster

New Water Clusters Hosted by Diamondoid MOFs

RS-7

Mohammad Hedayetullah Mir, Jagadese J Vittal
National University of Singapore, Department of Chemistry, 3 Science Drive 3,
Singapore 117543, Singapore (g0600472@nus.edu.sg)

Water constitutes the most abundant compound on the earth, covering 71% of the planet’s
surface, mostly in oceans and other large bodies of water. Water is essential for livingorganisms as it plays an important role in many biological and chemical systems. It exhibits awide spectrum of physical and chemical properties in various forms. Although scientists havestudied the structure of water extensively, the structure of bulk water is understood poorly.
The presence of water molecules in solid-state structures can play an important role instabilising some supramolecular structures. A number of discrete water clusters have been
structurally characterised with varying numbers of water molecules from 3 to more than 30 ina variety of inorganic and organic crystal hosts. However, in the discrete water clusters, thestructure of cyclic water heptamer was elusive. The electron-water heptamer is one of the magic
numbers in the mass spectra of electron-water clusters.
We discovered the structure of discrete cyclic water heptamer at 296 K in the 3D metalorganic framework (MOF) having daimondoid topology. When the single crystal is cooled to223 K, it undergoes Single-Crystal to Single Crystal (SCSC) phase transition from monoclinic
C2/c to P21/c space group accompanied by structural transformation from cyclic (H2O)7 tobicyclic water heptamer containing edge sharing pentamer and tetramer rings (Fig. 1 Left).
When the anion is changed from BF4¯¯ to ClO4¯¯ anion, the cyclic water heptamer transforms
to another heptamer composed of cyclic pentamer ring buttressed by an acyclic dimer via
SCSC transformation. Interestingly, a small change in the structure of the backbone of the
MOF from 1,10-phenanthroline to 2,2'-bipyridine ligand transforms the cyclic water heptamer
to a new acyclic form of water aggregate, viz., helicate (H2O)7 which has been trapped
between the ClO4¯ anions in the diamondoid channels (Fig. 2 Right). Our studies provide
new insights into the properties and behavior of bulk water where the water molecules interact
with the surface of the containers through weak interactions.

Fig. 1. Structural transformations of water heptamer (left). Structure of water helicate (right)

References
1. M. H. Mir and J. J. Vittal, Angew. Chem. Int. Ed. 2007, 46, 5925–5928.
2. M. H. Mir and J. J. Vittal, Cryst. Growth Des. 2008, 8, 1478–1480.
3. M. H. Mir, L. Wang, M. W. Wong and J. J. Vittal, Chem. Commun., 2009, 4539 - 4541.

- 90 -

AsCA’09

PosterLaser assisted deposition of AgInSe2 films on Si(100)RS-8Dinesh Pathak1, R. K. Bedi1 and Davinder Kaur2
1
Material Science Laboratory, Department of Physics, Guru Nana k Dev University,
Amritsar – 143005, India.
2
Department of Physics and Centre of Nanotechnology(dineshpathak80@gmail.com)

Laser ablation has attracted special interest for the formation of thin films Compared withother formation technique . A distinctive feature of laser ablation is that it allow highquality and stochiometry of films of even very complex element material. In thispresentation laser ablation of AgInSe2 chalcopyrite semiconductor will be discussed in which
it is difficult to maintain stochiometry by conventional method. High Quality AgInSe2 (AIS)
films were grown on Si(100) substrates by the ultra-high-vacuum pulsed laser deposition
technique from the AIS target synthesized from high-purity materials. The X-ray diffraction
studies of the films show that films are textured in (112) direction. .The substrate temperatureappears to influence the properties of films. Increase in substrate temperature results in moreorder structure .Compositional analysis has been carried out by EDAX. It is observed thatcompositional stochiometry is maintained to the more extent by PLD technique than othertraditional methods like thermal evaporation. The optical studies of the films show that the
optical band gap is about 1.20 eV.

New Structural Model of Malaria Pigment

RS-9

Ratchadaporn Puntharod1,2, Bayden R. Wood3, Evan G. Robertson3, Kenneth J.
Haller1
1
School of Chemistry, Suranaree University of Technology, Nakhon Ratchasima, 30000,
Thailand, (ratchada_aim@hotmail.com)
2
Department of Chemistry, Maejo Unviersity, Chiangmai 50290, Thailand.
3
Biospectroscopy Centre, Monash University, Clayton, Victoria, 3800, Australia.

The crystal structure of five-coordinate high-spin iron(III) Fe(OEP)picrate has been studied asa model system for malaria pigment due to intense interest the molecular structure of malaria
pigment (hemozoin) which is indistinguishable with β-hematin. To examine the conformationof porphyrin plane and ethyl groups substituted in beta-pyrrole positions with a picrate asaxial ligand was studied by single crystal X-ray crystallography and resonance Raman
spectroscopy. The macrocyclic porphyrin structure is the out-of-plane normal deformations of
the saddle-shaped. The axial ligand orientation is the role in controlling the unequal distanceof Fe−N bond (2.040(2), 2.028(2), 2.055(2), and 2.053(2) Å). The distance of axial Fe−O
bond is 1.93(2) Å. The Fe(OEP)picrate molecules interact in pairs via π−π stacking
interaction and nitro-nitro interaction. Fe(OEP)picrate exhibits the enhancement of totallysymmetric oxidation state marker band, ν4 at 1370 cm−1 for ν(pyr half ring) when usingnear-IR excitation laser and the characteristic bands of beta substituted hemes in the ranges of1621−1639 for ν(CαCm)asym and 750−756 cm−1 for ν(pyr breathing) similar with β-hematin.
Crystal data for Fe(OEP)picrate: C42H46FeN7O7, monoclinic space group C2/c, a =26.3997(20), b = 13.7806(18), c = 25.4126(20) Å, β = 119.955(9)°, V = 8010.2(14) Å3, Z = 8
at 298 K.
- 91 -

AsCA’09

Poster

Structural insight into acute intermittent porphyria

RS-10

Gaojie Song1, Yang Li1, Chongyun Cheng1, Yu Zhao1, Ang Gao1, Rongguang
Zhang2, Andrzej Joachimiak2, Neil Shaw1, Zhi-Jie Liu1
1
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academyof Sciences, Beijing 100101, China.
2
Structural Biology Center, Advanced Photon Source, Argonne National Laboratory, IL
60439 USA.

Acute intermittent porphyria (AIP), an inherited disease of heme biosynthesis, is one of themost common type of the porphyrias. Reduced activity of the enzyme porphobilinogendeaminase (PBGD), which catalyses the sequential condensation of 4 molecules ofporphobilinogen to yield preuroporphyrinogen, has been linked to the symptoms of AIP. We
have determined the three dimensional structure of human PBGD at 2.2 Å resolution.
Analysis of the structure revealed a dipyrromethane cofactor molecule covalently linked to
Cys261, sitting in a positively charged cleft region. In addition to the critical catalytic Asp99,
a number of other residues are seen hydrogen bonded to the cofactor and play a role incatalysis. Sequential entry of 4 pyrrole molecules into the active site is accomplished by
movement of the domains around the hinges. Interestingly, some of the mutations of thehuman PBGD documented in patients suffering from AIP are located far away from the activesite. The structure provides insights into the mechanism of action of PBGD at the molecularlevel and could aid the development of potential drugs for the up-regulation of PBGD activity
in AIP.
Keywords: human porphobilinogen deaminase, X-ray structure, heme biosynthesis,
porphobilinogen，hinge

Accurate measurements of anomalous dispersion
effect shows there is no chloride ion between Fe andCu ions in the reduction site of oxidized Cytochromec Oxidase

RS-11

Michihiro Suga1, Kazumasa Muramoto2, Eiki Yamashita1, Masao Mochizuki2,
Kazunori Maeda2, Kyoko Ito-Shinzawa1, Shinya Yoshikawa2 and Tomitake
Tshukihara1, 2
1Institute of Protein Research, 3-2, Yamadaoka, Suita, Osaka, 565-0871, JAPAN(m-suga@protein.osaka--u.ac.jp)
2
Department of Life Science, University of Hyogo, 3-2-1 Koto, Kamighori, Akoh, Hyogo
678-1297, JAPANCytochrome c oxidase (CcO) is a key component of the respiratory chain that catalyzes
dioxygen reduction coupled with a proton-pumping process. The O2 reduction site includes ahigh-spin heme A (heme a3) and a copper ion (CuB) with 3 histidine imidazoles as the ligand.
An existence of peroxide bridge between Fe and Cu ions in the reduction site of the fully
oxidized CcO was reported [H., Aoyama, et al. Proc. Natl. Acad. Sci. USA 106:2165-2169(2009)]. However, other groups insist that a chloride ion exists in the dioxygen reduction site.
It is true that if Cl- ion binds to heme a3 or CuB with occupancy of 0.5 each, the electron- 92 -

AsCA’09

Posternumber would be fitted. To overcome this possibility, we performed an X-ray experiment.
We collected the dataset using X-rays of 1.7470Å wavelength, where f’’Fe=0.47, f’’Cu=0.74,
f’’P=0.55, f’’S=0.70 and f’’Cl=0.88. The data were collected on the beamline BL44XU at theSPring-8. In order to reduce the deterioration of peroxide structure by the X-ray irradiation,
the experiment was carried out at 40K temperature using the He cryostat, and four crystals
were used. A dataset was collected at 3.0Å resolution with Rmerge value of 18.4, acompleteness 100.0%, and averaged redundancy of 31.4, and I/sigma(I) of 34.4 in the highest
3.03 - 3.00Å resolution shell. To improve the accuracy of the Bijvoet difference, the intensity
data were collected in the inverse-beam mode, which records Friedel pairs on two consecutive
images to reduce the influence of radiation damage on the Bijvoet difference. For accurate
phase determination, reference data was also collected using X-ray at 0.9Å wavelength with
an isomorphous crystal.
In the anomalous Fourier map, most of the Sulfur atoms in the Met and Cys residues
exhibited electron distribution at higher than 5.0 sigma, and some phosphorus atoms in thelipids were also observed. One the other hand, no prominent peaks were observed in the
reduction center. This result excluded the possibility that a chloride ion exists between CuB
and heme a3.

Anomalous difference Fourier map calculated at 3.0Å resolution using X-rays of 1.7470Å wavelength andcontours were drawn at 4.0σ. (1σ=0.0048e-/Å3)

Perakine Reductase, The First AKR Superfamily
Member Involved In Indole Alkaloids Biosynthesis :Characterization, Crystallization And X-Ray Analysis

RS-12

Lianli Sun1,2*, Meitian Wang3, Santosh Panjikar4, Joachim Stöckigt1,2*
1
Institute of Materia Medica, College of Pharmaceutical Sciences, Zhejiang University,
388 Yu Hang Tang Road, Hangzhou, Zhejiang Province, 310058, P.R. China(lianlisun80@yahoo.com.cn)
2
Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes
Gutenberg-University Mainz, Staudinger Weg 5, D-55099 Mainz, Germany(stoeckig@uni-mainz.de)3
Swiss Light Source PX III, Paul Scherrer Institute, CH-5232 Villigen, Switzerland
4
European Molecular Biology Laboratory, Hamburg Outstation Deutsches
Elektronen-Synchrotron, Notkestrasse 85, D-22603 Hamburg, Germany

Perakine reductase (PR) catalyzes an NADPH-dependent conversion of perakine toraucaffrinoline (Figure), representing a side-branch of the biosynthetic pathway of theantiarrhythmic alkaloid ajmaline in plant cell suspension cultures of the Indian medical plant- 93 -

AsCA’09

PosterRauvolfia serpentina [1].
OAc

OAc

N
N

CH3

NADP+

NADPH
PR

H

N
N

CH3

H
CHO

CH2OH

Perakine

Raucaffrinoline

Figure. Perakine reductase catalyzes the enzymatic reaction from perakine to raucaffrinoline in presence ofthe reduced cofactor NADPH.

PR was functionally expressed in Escherichia coli as the N-terminal His6-tagged enzyme andwas purified to homogeneity. Sequence alignments studies define PR as a novel member of
the aldo-keto reductase (AKR) superfamily, exhibiting the conserved catalytic tetrad Asp52,
Tyr57, Lys84, His126. Site-directed mutagenesis of each of these functional residues to an
alanine residue results in > 97.8% loss of enzyme activity. PR represents the first example ofthe large AKR-family which is involved in the biosynthesis of plant –derived monoterpenoid
indole alkaloids. In addition to a new esterase, PR significantly extends the Rauvolfia alkaloid
network to the novel group of peraksine alkaloids. Surprisingly, PR displays also an unusual
broad substrate acceptance, reducing small benzaldehyde analogs, medium cinnamic aldehyde
derivatives, up to bulky indole alkaloids. The relatively low substrate specificity anddelivering de-toxified alcohols from compounds with reactive aldehyde groups also suggests
a chemical defence and self-protecting function of PR [2].
The best crystals of methylated His6-tagged PR were obtained by the hanging-drop
vapor-diffusion technique. The crystals diffracted to 2.30 Å and belong to space group C2221,
one asymmetric unit cell contains one molecule. The final 3D-structure elucidation of PR ispresently under progress.
References
1.

2.

Ruppert M, Ma X, Stöckigt J. Alkaloid biosynthesis in Rauvolfia – cDNA cloning of major enzymesof the ajmaline pathway Curr. Org. Chem., 2005, 9, 1431-1444.
Sun L, Ruppert M, Sheludko Y, Warzecha H, Zhao Y, Stöckigt J. Purification, cloning, functional
expression and characterization of perakine reductase – the first example from the AKR enzyme
family, extending the alkaloidal network of the plant Rauvolfia. Plant Mol. Biol., 2008, 67, 455-467.

- 94 -

AsCA’09

Poster

3-D Structure and Enzymatic Mechanism of
Polyneuridine Aldehyde Esterase: from C10- to C9Skeleton in Ajmaline Biosynthesis
Liuqing Yang1,2, Marco Hill2, Meitian Wang3, Santosh Panjikar4, Joachim
Stöckigt1,2,*
1, Institute of Materia Medica, College of Pharmaceutical Sciences, Zhejiang University,
383 Yu Hang Tang Road, Hangzhou, Zhejiang Province, 310058, P.R. China(yangliuqing1984@hotmail.com)
2, Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes
Gutenberg-University Mainz, Staudinger Weg 5, D-55099 Mainz, Germany(Hill@uni-mainz.de)3, Swiss Light Source PX III, Paul Scherrer Institute, CH-5232 Villigen, Switzerland(meitian.wang@psi.ch)
4, European Molecular Biology Laboratory, Hamburg Outstation Deutsches
Elektronen-Synchrotron, Notkestrasse 85, D-22603 Hamburg, Germany(panjikar@embl-hamburg.de)*Corresponding author: joesto2000@yahoo.com

RS-13

Polyneuridine aldehyde esterase (PNAE , EC 3.1.1.78) plays a central role in the biosynthesisof alkaloids in the Indian medicinal plant Rauvolfia serpentina (L.) Benth. ex Kurz. PNAE is
localized in the middle of the pathway transforming polyneuridine aldehyde to
epi-vellosimine, which is a precursor for the synthesis of the monoterpenoid indole alkaloid
ajmaline (an important therapeutic to treat antiarrhythmic heart disorders). The enzyme
catalyses the following reaction:
OHC

OHC
COOCH 3N
N
H
H

Polyneuridine aldehyde

PNAE

R2
COOH
N

N
N

N

CO 2

H

H

Polyneuridine aldehyde acid

R1

H
H

epi-Vellosimine ( R 1 =H, R 2 =CHO)
Vellosimine ( R 1 =CHO, R 2 =H )Figure : Transformation of polyneuridine aldehyde catalyzed by PNAE.

After heterologous expression of PNAE-cDNA in Escherichia coli , the N-terminal
His6-tagged PNAE was purified to homogeneity and crystallized for the first time. Sequencealignment and the 3D structure placed the enzyme as a new member into the α/β hydrolase
superfamily.
PNAE exhibits an extraordinary high substrate specificity. In order to provide a structuralevidence of this specificity and to analyze the structure of the binding site, cDNA of aknock-out mutant (His224Ala) was expressed in E.coli. The mutant enzyme was crystallized
and soaked with its substrate polyneuridine aldehyde. The generated enzyme-productcomplexes were investigated by X-ray analysis. The results reveal now the complex
enzymatic mechanism and explain the biosynthesis of C9- from the C10-monoterpenoid
alkaloids stage.
Since the cap domain and the architecture of the binding pocket of PNAE determining which
compound is accepted, low substrate specificity can probably be attained due to the rational
structure-based redesign of PNAE, and the generation of novel alkaloids can be used in future
for biological screening.
- 95 -

AsCA’09

Poster

References
1.
2.
3.

E. Dogru, H. Warzecha, F. Seibel, S. Haebel, F. Lottspeich, J. Stöckigt, Eur. J. Biochem. 2000. 267,
1397-1406.
E. Mattern-Dogru, X. Ma, J. Hartmann, H. Decker, J. Stöckigt, Eur. J. Biochem. 2002. 269,
2889-2896.
L. Yang, M. Hill, M. Wang, S. Panjikar, J. Stöckigt, Angew. Chem. Int. Ed. 2009. (in press).

Structural Basis and Catalytic Mechanism for the
Dual Functional Endo-β-N-Acetylglucosaminidase A

RS-14

Jie Yin1, Lei Li2, Neil Shaw1, Yang Li1, Lai-Xi Wang3, Peng Wang3, Zhi-Jie Liu1
1
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academyof Sciences, Beijing, China (yinjie@moon.ibp.ac.cn)
2
Departments of Biochemistry and Chemistry, The Ohio State University, Columbus,
Ohio, United States of America
3Institute of Human Virology and Department of Biochemistry and Molecular Biology,
University of Maryland School of Medicine, Baltimore, Maryland, United States ofAmericaEndo-β-N-acetylglucosaminidases (ENGases) are dual specificity enzymes with an ability tocatalyze hydrolysis and transglycosylation reactions. Recently, these enzymes have become
the focus of intense research because of their potential for synthesis of glycopeptides. We
have determined the 3D structures of an ENGase from Arthrobacter protophormiae (Endo-A)in 3 forms, one in native form, one in complex with Man3GlcNAc-thiazoline and another incomplex with GlcNAc-Asn. The carbohydrate moiety sits above the TIM-barrel in a cleft
region surrounded by aromatic residues. The conserved essential catalytic residues - E173,
N171 and Y205 are within hydrogen bonding distance of the substrate. W216 and W244
regulate access to the active site during transglycosylation by serving as “gate-keepers”.
Interestingly, Y299F mutation resulted in a 3 fold increase in the transglycosylation activity.
The structure provides insights into the catalytic mechanism of GH85 family of glycosidehydrolases at molecular level and could assist rational engineering of ENGases.
Keywords: Endo-A / X-ray structure / glycoprotein / Man3GlcNAc-thiazoline / GlcNAc-Asn
References
Yin J et al. (2009) Structural Basis and Catalytic Mechanism for the Dual Functional Endo-β-NAcetylglucosaminidase A. PLoS ONE 4(3): e4658.

- 96 -

AsCA’09

Poster

Structural insights into the chemotactic pathway inHelicobacter pylori

P-1

Kwok Ho LAM1, Thomas King Wah LING2 and Shannon Wing Ngor AU1
1
Centre for Protein Science and Crystallography, Department of Biochemistry andMolecular Biotechnology Program, Faculty of Science, The Chinese University of Hong
Kong, Hong Kong.
2
Department of Microbiology, The Chinese University of Hong Kong, Hong Kong.
(shannon-au@cuhk.edu.hk)

Helicobacter pylori is a gram negative microaerophilic bacterium that colonizes humanstomach and is related to gastritis, peptic ulcer, adenocarcinoma and gastric cancer. The
chemotactic pathway is an important virulence trait in H. pylori and is featured with four
additional CheY-like containing proteins - one CheY2 and three CheVs. CheY2 modulates thelevel of phosphor-CheY1 in retrophosphorylation while the roles of CheVs are unknown. All
CheY-like proteins are phosphorylated by CheA, but the rate of phosphotransfer is in theorder of CheY1 > CheY2 > CheVs.
Here we report the crystal structures of CheY1 in complex with SO42- and BeF3- from H.
pylori. Interestingly, the sulfate-bound form mimics the transient state of phosphorylation andfurther suggests the functional significance of Thr84 in the phospotransfer reaction. On theother hand, interaction of CheA-P2 domain with CheY1, but not other CheY/CheV proteins
underlines the preferential recognition to CheY1 by CheA in phosphotransfer reaction. Pull
down assay, qualitative surface plasmon resonance and size exclusion chromatography
analysis demonstrated that only CheY1 interacted with CheA-P2 domain, indicating that thedifferential phosphotransfer was attributed by the P2 domain. Homology modeling of CheV1
and CheY2 suggested that the distinctive characteristics at the α4β5α5 surface were
responsible for the specific CheA-CheY interaction. Our result has provided the firststructural insight into the features of chemotactic system in epsilon proteobacteria and further
our knowledge on how the bacterium evolved to different chemotactic pathway.

Solid-liquid interface method (SLIM): A new
crystallization method for proteins

P-2

Erik Brostromer, a, Jie Nan,
Lan-Fen Li a and Xiao-Dong Su a,b*aNational Laboratory of Protein Engineering and Plant Genetic Engineering, College ofLife Sciences, Peking University, Beijing 100871, People’s Republic of China,b
Shenzhen Graduate School of Peking University, Shenzhen 518055, People’s Republicof China§a,§Despite impressive advances in theories, methods and technologies, crystallization still
remains a serious bottleneck in structural determination of macromolecules. Here we present a
novel solid-liquid interface method (SLIM) for protein crystallization, based on the
pre-adding and drying of a crystallization reagent, and thereafter the dispensing of a protein
solution to the dried media to initiate crystallization from the solid-liquid interface. Not only
quick and easy to perform, the method also allows for a less concentrated protein solution for
setting up crystallization trials.

- 97 -

AsCA’09

P-3

Poster

Structural Basis for the Nucleotide-dependent
Domain Rearrangement of 70-kDa Heat Shock
Proteins
1,2

2

1

1

Yi-Wei Chang , Yuh-Ju Sun , Chung Wang , Chwan-Deng Hsiao
1
Institute of Molecular Biology, Academia Sinica, Taipe 11529i, Taiwan(yiwei@imb.sinica.edu.tw, mbcw@gate.sinica.edu.tw, hsiao@gate.sinica.edu.tw)
2Institute of Bioinformatics and Structural Biology, National Tsing Hua University,
Hsinchu 300, Taiwan (yjsun@life.nthu.edu.tw)

The 70-kDa heat shock proteins (Hsp70s) are highly conserved ATP-dependent molecularchaperones composed of an N-terminal nucleotide binding domain (NBD) and a C-terminal
protein substrate binding domain (SBD) in a bilobate structure. Interdomain communicationand nucleotide-dependent structural motions are critical for Hsp70 chaperone functions. Our
understanding of these functions remains elusive due to insufficient structural information on
intact Hsp70s that represent the different states of the chaperone cycle. We report here thecrystal structures of DnaK from Geobacillus kaustophilus HTA426 bound with ADP-Mg2+-Pi
at 2.37 Å and the 70-kDa heat shock cognate protein from Rattus norvegicus bound with
ADP-Pi at 3.5 Å. The NBD and SBD in these structures are significantly separated from eachother, and they might depict the ADP-bound conformation. Moreover, a Trp reporter was
introduced at the potential interface region between NBD and the interdomain linker of
GkDnaK to probe environmental changes. Results from fluorescence measurements support
the notion that substrate binding enhances the domain-disjoining behavior of Hsp70
chaperones.

P-4

Complex structure of tarocystatin-papain andcharacterization of tarocystatin proposed the role ofC-terminal domain of group-2 phytocystatin
Ming-Hung Chu1, Kai-Lun Liu1, Kai-Wun Yeh1 and Yi-Sheng Cheng1,21Institute of Plant Biology, National Taiwan University, Taipei, 106 Taiwan
2
Department of Life Science, National Taiwan University, Taipei, 106 Taiwan(chengys@ntu.edu.tw)

Tarocystatin (CECPI) is a member of group-2 phytocystatin. It shared a conserved N-terminal
cystatin (CY) domain with group-1 phytocystatin, but composed of an extended C-terminal
domain. The complex structure of tarocystatin-papain has been resolved at a resolution 2.03Å.
Interestingly, the C-terminal domain cannot be observed in the complex structure with only
N-terminal domain in complex of papain. For further characterizing the tarocystatin, threesegments of tarocystatin, including full length (FL), N-terminal domain (NtD) and C-terminal
domain (CtD), were prepared to analyze the domain-domain interaction and inhibitory
property. The domain-domain interaction by glutaraldehyde cross-linking and yeast two
hybrid were carried out and showed the results that a weak interaction could be observed
between NtD and CtD. The tarocystain also could form homodimer via the interaction of
NtDs. In the inhibitory activity assay, the GST-fused FL showed the best inhibitory activity,and GST-NtD and FL showed almost the same inhibitory property. On the contrary, GST-CtD
showed an enhanced activation activity of papain than CtD or GST, respectively. It means- 98 -

AsCA’09

Posterthat the inhibitory activity of CY domain could be enhanced by fused GST or CtD.
Consequently, structural models of tarocystatin with the intermolecular interaction of NtD and
NtD to form homodimer, or the intramolecular interaction of NtD and CtD to form
latexin-like were proposed.

Study on Structural Biology in Disease/structurebased Drug Design

P-5

Ki Joon Cho1, Ji-Hye Lee2, Intekhab Alam2, Yi Ho Park2, and Kyung Hyun Kim2
1
School of Life Sciences & Biotechnology, Korea University, Seoul 136-701, Korea(c-azna@korea.ac.kr)
2
Department of Biotechnology & Bioinformatics, College of Science & Technology,
Korea
University,
Chungnam339-700,
Korea(jihyelee@korea.ac.kr;
Intekhab@korea.ac.kr; ballashe@naver.com; khkim@korea.ac.kr )Helicobacter pylori is the causative agent of chronic gastritis, duodenal ulcer, gastriccarcinoma and gastric lymphoma. Iron is essential for the survival of the bacteria and proteins
involved in iron metabolism are suggested as the major determinants of virulence. Among
those proteins, ferritin has a role in storage of up to 4,500 irons inside the protein shell. In
order to get a structural insight of the mechanism of iron uptake and release, crystal structuresof H.pylori ferritin have been solved at resolutions 1.3Å-2.1Å as apo, low-iron bound,intermediate, and high iron bound states. As the iron content increased, significant
conformational changes have been observed at the 4-fold symmetry channel in intermediateand high iron bound states, while no such change was observed in low and apo states. At highmagnetic fields, the magnetic moment of the high-iron bound state was approximately 10
times higher than that of the low-iron state. Exposure of the crystals to a magnetic field of as
high as 3 Tesla triggered the conformational change at the 4-fold channel at the apo andlow-iron structures, identical to that found at the intermediate and high-iron structures. Our
results provide the structural evidence of the translocation of Fe ions through the 4-foldchannel and magnetic properties of ferritin in the presence of a magnetic field are described.

P-6

Crystal Structure of Carboxynorspermidine
Decarboxylase from Helicobacter pylori
Chen-Hsi Chu, Chin-Yi Chen, and Yuh-Ju Sun
Institute of Bioinformatics and Structural Biology, National Tsing Hua University, 101,
Section 2 Kuang Fu Road, Hsinchu 30013, Taiwan (d928216@oz.nthu.edu.tw)

Carboxynorspermidine decarboxylase (CANSDC) belongs to group IV pyridoxal
5’-phosphate (PLP)-dependent decarboxylase. CANSDC catalyzes the decarboxylation ofcarboxynorspermidine to norspermidne in polyamine biosynthesis. The cofactor, PLP, makes
a covalent bond with the catalytic lysine residue to form a Schiff base. CANSDC from
Helicobacter pylori (HpCANSDC) has been overexpressed and purified with the endogenous
PLP. The binding of HpCANSDC and norspermidine was characterized by a CD and UV/Vis
spectrum. The HpCANSDC crystal structure was determined by multiwavelength anomalous
dispersion (MAD) method at 2.1 Å resolution. HpCANSDC functions as a dimer in solution- 99 -

AsCA’09

Posterand folds as a head-to-tail dimer in crystal. The overall structure of HpCANSDC contains an
N-terminal TIM-like β/α barrel domain and a C-terminal β-barrel domain. The binding pocketof HpCANSDC is built by the active site loop (loop β6α6) and a specificity element (α10).
Loop β6α6 situates a rather “down” conformation and it might protect the substrate/productfrom solvent to be bound in the active site. The α10 is at the relatively backward position inorder to accommodate the longer substrate, carboxynorspermidine.

Crystallographic Studies of Manihot esculenta
hydroxynitrile lyase mutants
a

P-7

c

a

Charles B.C. Cielo , Mohammad Dadashipourb, Tatsuo Hikage , Atsuo Suzuki ,
b
a
a,d
b
Tsunehiro Mizushima , Hidenobu Komeda , Yasuhisa Asano , Takashi Yamane *aDepartment of Biotechnology, School of Engineering, Nagoya University, Chikusa-Ku,
Nagoya 464-01, Japan (yamane@nubio.nagoya-u.ac.jp)
bDepartment of Biotechnology, Faculty of Engineering, Toyama Prefectural University,
Toyama 939-0398, JapancHigh Intensity X-ray Laboratory, Nagoya University, Chikusa-Ku, Nagoya 464-01,
Japan
dPresent address; Department of Structural Biology and Biomolecular Engineering,
Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya
467-8603, Japan

Cassava (Manihot esculenta) is a major root crop that contains potentially toxic levels of
cyanogenic glycosides that provide the plant with protection from herbivory as well asfunction in amino acid catabolism. Free Manihot esculenta hydroxynitrile lyase (MeHNL)
catalyzes the stereospecific production of (S)-ketone cyanohydrins, an industrially importantintermediate for fine chemicals and pharmaceuticals. The effective production of MeHNL via
Escherichia coli expression systems has previously been demonstrated. However,improvements in protein yield are necessary for its feasible industrial application. Several
MeHNL mutants have demonstrated significantly increased enzyme solubility and yield. It is
the aim of this study to establish structural bases for this improvement.
We solved the structure of the MeHNL mutant K176P via molecular replacement using wild
type MeHNL (wtMeHNL) as the molecular search model (PDB ID: 1E8D). Although the
crystals of the K176P mutant and the wild-type enzyme are non-isomorphous, no major
deviations in structure were observed between the two enzymes. It was of particular interest
to note that crystals of two MeHNL mutants (K176P, H103M) formed under identicalcrystallization conditions producing isomorphous crystals. In contrast with wtMeHNL, 4
molecules were assigned to a single asymmetric unit for K176P, suggesting a tetramericquarternary structure. Furthermore, in K176P, 2 glycerol molecules were found in themonomer-monomer interface located in essentially identical positions and in proximity of themutated residue in the two dimers found in the asymmetric unit of the crystal.
We propose that the mutations contribute to improving protein solubility by affecting
quarternary structure formation.

- 100 -

AsCA’09

P-8

Poster

The Effects of UV Irradiation of Protein Crystals
Angela R. Criswell, Pierre LeMagueres, Bret Simpson
Rigaku Americas Corp, 9009 New Trails Dr., The Woodlands, TX 77381 USA(angela.criswell@rigaku.com)

Automation of crystallization experiments enables sampling of large crystallization spaces bycoarse and fine screening. The result is an increased number of crystallization experimentsthat require visual inspection. Consequently, crystallographers further rely on automation tomonitor crystal growth and to identify crystals for additional diffraction screening. Comparedto visible light inspection alone, ultraviolet (UV) image inspection has proven useful for
protein crystal identification through exploitation of the fluorescence responses of aromatic
amino acid residues such as tryptophan. Results show UV imaging to be an efficient method
to single out protein crystals from other non-protein solid materials within crystallization
drops.
Due to the increased use of UV irradiation there is greater attention given to the impact of UV
irradiation on crystallographic samples. To date, little is known about the effects of UV
irradiation on protein crystals and even less is known about the effects on crystallization
experiments. This work examines the effects of UV irradiation on protein crystals in drops
and in loops. Experiments show that one can detect and measure trends in both X-ray
diffraction experiments and in the 3-dimensional protein structure of crystals. As expected,
the trends are more observable as the UV exposure time increases. These experiments also
investigate the effects of UV exposure at different stages during crystallization to examine theimpact on crystal formation and nucleation.

Excitation coupling in bioluminescence: combined
X-ray and NMR determination of the clytin-GFP
topology

P-9

Yingang Feng1, Maxim Titushin1,2，Yang Li1，Jinfeng Wang1, Eugene Vysotski2，
Zhi-Jie Liu1
1
National Lab of Biomacromolecules, Institute of Biophysics, Chinese Academy of
Sciences, Beijing 100101, China
2
Institute of Biophysics, Russian Academy of Science, Siberian Branch, Krasnoyarsk
660036, Russia

Bioluminescence in medusa Clytia gregarium is Ca2+-induced and involves two distinct
proteins, clytin and green fluorescent protein (GFP). Clytin contains one tightly boundcoelenterazine molecule, which becomes available for reaction with O2 only subsequent toCa2+ binding. Clytin belongs to the EF-hand super-family of Ca2+-binding proteins andcontains three "EF-hand" Ca2+-binding sites. When clytin is in the excited state, the energy istransferred to GFP through so called “bioluminescence resonance energy transfer (BRET)”
mechanism. But how these two molecules interact and facilitate the energy transfer is
unknown. This study reports the crystal structure determination of clytin and GFP by X-ray
crystallography method and the identification of protein-protein interaction surfaces by NMR
method. The energy transfer mechanism at atomic level will be discussed as well.
- 101 -

AsCA’09

Poster

References
1.
2.
3.
4.

Stepanyuk, G.A., Liu, Z.J*, Vysotski, E.S., Lee, Rose, J. and Wang, B.C. (2009). Structure based
mechanism of the Ca2+-induced release of coelenterazine from the Renilla binding protein. Proteins,
74(3):583-93
Liu, Z.J., Stepanyuk, G.A., Vysotski, E.S., Lee, J., Markova, S.V., Malikova, N.P., and Wang, B.C.
(2006). Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral
coelenteramide as the primary excited state. Proc Natl Acad Sci 103, 2570-2575.
Deng, L., Markova, S.V., Vysotski, E.S., Liu, Z.J., Lee, J., Rose, J., and Wang, B.C. (2004). Crystal
structure of a Ca2+-discharged photoprotein: implications for mechanisms of the calcium trigger andbioluminescence. J Biol Chem 279, 33647-33652.
Liu, Z.J., Vysotski, E.S., Chen, C.J., Rose, J.P., Lee, J., and Wang, B.C. (2000). Structure of theCa2+-regulated photoprotein obelin at 1.7 A resolution determined directly from its sulfur substructure.
Protein Sci 9, 2085-2093.

P-10

Structural study of FIH with CQ, HQ inhibitor complex
Sojung Han, Hyunjin Moon, Jungwoo Choe
University of Seoul, Siripdae-gil 13(jeonnong-dong 90), Daongdaemun-gu, Seoul
130-743 KOREA (jchoe@uos.ac.kr)

Mammalian cells have their own mechanism to survive the condition of low oxygen
concentration (hypoxia) by turning on hypoxic transcriptional factors. HIF (hypoxia-inducible
factor) is an αβ-heterodimeric-transcription factor that induces the expression of genes, suchas EPO (erythropoietin) and VEGF (vascular endothelial growth factor), under hypoxic
conditions. And the activity or the expression level of HIF is regulated by hydroxylases which
belong to 2OG (Oxoglutarate)- and Fe(II)- dependent dioxygenase superfamily, and are also
categorized into cellular oxygen sensors. FIH (factor inhibiting HIF) is one of thathydroxylases and play an important role in controlling the HIF activity underhypoxia.Structural studies of FIH have shown that it forms a homodimer, and each of its
subunit has the double-stranded β-helix core, a jellyroll-like-barrel embracing the conserved
Fe(II)-binding triad region, featuring it belonging to the 2OG dependent dioxygenasesuperfamily. NOG (N-Oxalylglycine) and its pro-form dimethyl N-oxalylglycine (DMOG) are
known as inhibitors of FIH. Structure of FIH with inhibitor complexes has been solved. These
inhibitors, however, are not appropriate to be used as drug, because they create negative
charges. So we focused on quinol family, such as Clioquinol, and Hydroxy quinol, whichhave similar structural feature and coordination with NOG, but are neutral in charge. Here we
made a structural an analysis with FIH and CQ, HQ complex crystals. And we defined thestructure with 2.6Ǻ resolution.

P-11

Structure of Maleylacetate Reductase from
Rhizobium sp. strain MTP-10005
Yasuo Hata1, Tomomi Fujii1, Masahiro Yoshida2, Tadao Oikawa2
1
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan(hata@scl.kyoto-u.ac.jp)
2
Kansai University, Suita, Osaka 564-8680, Japan, (oikawa@ipcku.kansai-u.ac.jp)

Maleylacetate reductases play a crucial role in the aerobic microbial degradation of aromatic- 102 -

AsCA’09

Postercompounds. In fungi and yeasts, the enzymes are involved in the catabolism of very common
compounds, such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria,
the enzymes contribute to the degradation of resorcinol, 2,4-dihydroxybenzoate (β-resorcylate)and 2,6-dihydroxybenzoate (γ-resorcylate), via hydroxyquinol and maleylacetate.
Maleylacetate reductases catalyze the NADH- or NADPH-dependent reduction of
maleylacetate or 2-chloromaleylacetate to 3-oxoadipate or of substituted maleylacetates tosubstituted 3-oxoadipates.
Maleylacetate reductase from Rhizobium sp. strain MTP-10005 (GraC) catalyzes the
reduction of maleylacetate to 3-oxoadipate and plays an important role in the catabolic
pathway of the resorcinol produced through decarboxylation of 2,6-dihydroxybenzoate. The
polypeptide chain of the enzyme consists of 351 amino acid residues with a mass of 36,405.
The structure of the present enzyme is expected to reveal structural features that may becommon to maleylacetate reductases from other aerobic microorganisms. Here, we report the
X-ray structure of maleylacetate reductase from Rhizobium sp. strain MTP-10005.
Expression and purification of the C-terminally His-tagged protein were performed according
to the method of Yoshida et al. Initial crystallization experiments were performed by thehanging-drop vapour-diffusion method using Crystal Screens (CSs) (Hampton Research, CA,
USA) at 293 K. Small crystals were obtained after several days using 8 mg ml-1 protein
solution (50 mM Tris-HCl buffer, pH 8.0) and the reservoir solution CS II #32. The
crystallization conditions were optimized based on those of the CS II #32 solution in
conjunction with Additive Screen (Hampton Research). The final conditions produced
rhombohedron-shaped crystals with approximate dimensions of 0.25 × 0.20 × 0.1 mm at 293
K in 3 d using the sitting-drop vapour-diffusion method. Drops prepared by mixing 1 μl
protein solution at 6 mg ml-1 (in 50 mM Tris-HCl buffer, pH 8.0) and 1 μl reservoir solution
were equilibrated against 500 μl reservoir solution consisting of 1.3 M ammonium sulfate, 0.1
M sodium chloride, 2% (w/v) benzamidine HCl, and 0.1 M NaHEPES (pH 7.5). The drops
were microseeded with the original crystals grown in CS II#32 before crystallization.
Data collection was performed at beamline BL-6A, Photon Factory, Tsukuba, Japan. Before
data collection, each crystal was soaked into a cryoprotectant solution consisting of 1.4 M
ammonium sulfate and 25%(v/v) glycerol for less than one minute, and flash-cooled in anitrogen stream at 100 K. The native data set was collected up to 1.96 Å resolution, and the 3Å MAD data sets with four different wavelengths for a Hg-derivative crystal. All diffraction
images were processed with the program HKL2000. The crystal belongs to space group C2,
with unit-cell parameters a = 56.85, b = 121.13, c = 94.09 Å, β= 101.48°. The VM value is
2.18 Å3 Da-1 for four dimeric molecules in the unit cell. An initial electron density map was
obtained at 3 Å resolution using MAD phases and interpreted with the help of the structure oflactaldehyde reductase (PDB ID=1RRM) which is homologous in sequence to GraC. The
structure was refined at 1.96 Å resolution up to R=0.165 and Rfree=0.216.
GraC is dimeric in the crystal. Its subunit consists of two domains: the N-terminal
NAD-binding domain adopting an α/β structure and the C-terminal α-helical domain. The
active site is located in the cleft between the domains of the subunit. The two subunits (Sub A& Sub B) have a little bit different structures from each other in the present crystal. Sub A- 103 -

AsCA’09

Posterbinds 2 SO42- ions, 1 benzamidine molecule, and 1 glycerol molecule, and has a closed
conformation, whereas Sub B binds no ligand except 1 SO42- ion and has an open
conformation. Thus, the present crystal structure of GraC reveals the structures ofmaleylacetate reductase both in the substrate-binding state and in the ligand-free state.

Current status and developments of macromolecular
crystallography beamlines at the Photon FactoryP-12

Masahiko Hiraki, Leonard Chavas, Yusuke Yamada, Naohiro Matsugaki, Noriyuki
Igarashi and Soichi Wakatsuki
Structure Biology Research Center, Photon Factory, Institute of Materials Structure
Science, High Energy Accelerator Research Organization (KEK), Oho 1-1, Tsukuba,
Ibaraki, 305-0801, Japan (masahiko.hiraki@kek.jp)

Structural Biology Research Center at the Photon Factory is currently operating fivemacromolecular crystallography beamlines (Table 1). BL-5A, BL-17A, AR-NW12A and
AR-NE3A are insertion device (ID) beamlines, while BL-6A is a conventional bending
magnet beamline. Among these ID beamlines, major purpose of the beamlines, BL-5A,
AR-NW12A and AR-NE3A is high-throughput. The new beamline AR-NE3A was constructed
for fully-automated data collection [1] supported by Astellas Pharma Inc. and has been
opened in April, 2009. A micro-focus beamline BL-17A was designed for micro-crystal
structure analysis. In addition, the lower energy beam at around 6 keV is used for structure
determination by SAD phasing with light atoms.
We are now building a new micro-focus beamline BL-1A supported by Targeted Protein
Research Program C of the Ministry of Education, Culture, Sports, Science and Technologyof Japan. The aim of BL-1A is to deliver brilliant lower energy beam at around 4-5 keVdedicated to sulphur SAD experiments and more photon flux at around 12 keV than that of
BL-17A. BL-1A will be opened to users in April, 2010.
For further high-throughput protein crystallography, we facilitate automation of beamline
operation, with developments of sample exchange robots PAM [2], automated sample
centering system and unified beamline control software. These developments based on stablebeamlines and reliable network will allow for the goal of fully-integrated structure
determination pipeline.
BL-6A

PF macromolecular crystallography beamlines
High-throughput beamlines
BL-5A
AR-NW12A
AR-NE3A

0.7-1.9

0.9-1.3

0.7-1.9

0.7-1.9

1x10-32.5x10-4

2.5x10-4

2.5x10-4

2.5x10-4

1.0x1010@1.0A
0.23 x 0.15
Q4R

1.5x1011@1.0A
0.2 x 0.2
Q315r

2.0x1011@1.0A
0.2 x 0.2
Q210r

1.3x1012@1.0A
0.2 x 0.2Q270

6.6x109 @1.0A
1.3x1010@2.0A
0.02 x 0.02
Q270

120

14

14

24

24

-

PAM

PAM

PAM

PAM

Table 1
Beamline
Wavelength range(Å)
Energy reso.
(ΔE/E)
Photon flux
(phs./sec)
Slit size (mm)Detector
Typical datacollection time(min)
Sampleexchanger- 104 -

Micro-focus beamline
BL-17A
0.95-1.33
1.6-2.2

AsCA’09

Poster

References
1.
2.

Yusuke Yamada, et al., Fully automated data collection system at the macromolecular crystallography
beamlines in the Photon Factory, AsCA2009.
Masahiko Hiraki, et al., J. Synchrotron Rad. (2008) 15, 300-303.

A new beamline at SPring-8 dedicated to protein
micro-crystallography

P-13

Kunio Hirata1, Go Ueno1, Atsushi Nisawa1, Nobutaka Shimizu1,2, Takashi
Kumasaka1,2, Yoshiaki Kawano1, Takaaki Hikima1, Takashi Tanaka1,2, Sunao
Takahashi1,2, Kunikazu Takeshita1,2, Hirokatsu Yumoto2, Haruhiko Ohashi1,2, Shunji
Goto1,2, Hideo Kitamura1, Toru Ohata1,2, Yukito Furukawa1,2, Masaki Yamamoto1
1. RIKEN/SPring-8 Center, (hirata@spring8.or.jp)
2. JASRI/SPring-8

Structure determinations of proteins are often hindered by the small size of the available
crystals. However, proteins involved in recent target of crystallography, such as membraneproteins or protein complexes, tend to show difficulties in growing their crystal size. Thus,
demands for achieving protein micro-crystallography are getting larger and larger. A new
undulator beamline at SPring-8 dedicated to protein micro-crystallography, BL32XU, hasbeen constructing.
In order to realize the protein micro-crystallography, we designed a micro-focus beamline at
SPring-8. The beamline should provide spatially brilliant and small beam of the order of a few
or several micro-meters. A ray trace simulation based on our optical design shows achievablebeam size at sample position corresponds to 1 x 1 μm2 with 6 x 1010 photons/sec/μm2. The
beam size will be changeable up to the maximum size of 20 x 20 μm2 according to size ofsample crystals or experimental conditions. Design concepts of a sample environment
suppressing background noise and a mirror chamber stabilizing both intensity and position of
the micron-sized beam at sample position will be presented.
Possible ways to utilize the micro beam not only for micro-crystals but for ‘low-quality’ ones
will also be introduced. One of them is probing single-crystal volumes from a heterogeneous
protein crystal using the micro-beam. In exchange of such kind of spatial advantages,
radiation damage of crystals should be considered more carefully when micro beam is utilized.
Both of the expert system for data collection strategy and the ‘on-the-fly’ monitoring systemof radiation damage are also under development.
Some experimental results of R&D for high-precision diffractometer, highly efficient CCD
detector, and hopefully, the first result of commissioning of the beamline will be presented.
The new beamline will largely benefit users by cutting off their time to optimize
crystallization conditions especially for smaller and lower quality crystals. The beamline will
be operated mainly for the National Project, named “Targeted Proteins Research Program”,
from 2010.

- 105 -

AsCA’09

P-14

Poster

Molecular Interplay Between Replicative Helicase
DnaC and Its Loader DnaI from Geobacillus
kaustophilus
Chwan-Deng Hsiao1, Kuang-Lei Tsai1,2, Yu-Hua Lo1,2, Yuh-Ju Sun2
1
Institute of Molecular Biology, Academia Sinica, Taipei, 115, Taiwan(hsiao@gate.sinica.edu.tw)
2Institute of Bioinformatics and Structural Biology, National Tsing Hua University,
Hsinchu, 300, Taiwan

Helicase loading factors are thought to transfer the hexameric ring-shaped helicases onto thereplication fork during DNA replication. However, the mechanism of helicase transfer onto
DNA remains unclear. In Bacillus subtilis, the protein DnaI, which belongs to the AAA+
family of ATPases, is responsible for delivering the hexameric helicase DnaC onto DNA.
Here we investigated the interaction between DnaC and DnaI from Geobacillus kaustophilus
HTA426 (GkDnaC and GkDnaI) and determined that GkDnaI forms a stable complex with
GkDnaC with an apparent stoichiometry of GkDnaC6-GkDnaI6 in the absence of ATP. Surface
plasmon resonance analysis indicated that GkDnaI facilitates loading of GkDnaC onto
single-stranded DNA (ssDNA) and supports complex formation with ssDNA in the presenceof ATP. Additionally, the GkDnaI C-terminal AAA+ domain alone could bind ssDNA, andbinding was modulated by nucleotides. We also determined the crystal structure of the
C-terminal AAA+ domain of GkDnaI in complex with ADP at 2.5 Å resolution. The structure
not only delineates the binding of ADP in the expected Walker A and B motifs but also reveals
a positively charged region that may be involved in ssDNA binding. These findings provide
insight into the mechanism of replicative helicase loading onto ssDNA.

Crystal structure of CRN-4: implications for domainfunction in apoptotic DNA degradation

P-15

Yu-Yuan Hsiao*1,2 and Hanna S. Yuan2, 31
Institute of Bioinformatics and Structural Biology, National Tsing Hua University,(hanna@sinica.edu.tw)
2Institute of Molecular Biology, Academia Sinica,3
Graduate Institute of Biochemistry and Molecular Biology, National Taiwan University,
Taipei, Taiwan

Programmed cell death (apoptosis) is an essential biological process for the development andmaintenance of appropriate cell number and for the defense against virus infection. One of the
major biochemical features of apoptosis is chromosome DNA fragmentation. Cell death
related nuclease 4 (CRN-4) is one of the apoptotic nucleases involved in DNA degradation in
Caenorhabditis elegans. CRN-4 contains an N-terminal DEDDh exonuclease domain and a
C-terminal domain of unknown function. To reveal the molecular basis of DNA
fragmentation in apoptosis, we analyzed CRN-4’s biochemical properties and determined its
crystal structures in apo-form, Mn2+-bound active form and Er3+-bound inactive form. CRN-4
is a dimer with both metal-dependent DNase and RNase activities. It prefers to cleave
double-stranded over single-stranded DNA, with optimal DNase activity in apoptotic saltconditions and pH ranges. Comparison of the Mn2+-bound and Er3+-bound CRN-4 structures
revealed the geometry of the functional nuclease active site in the N-terminal DEDDh domain.
- 106 -

AsCA’09

Poster

The C-terminal domain bound to a structural zinc ion, termed the Zn-domain, is folded into anovel mixed α/β structure, containing basic surface residues ideal for RNA/DNA recognition.
Site-directed mutagenesis further confirmed the catalytic residues in the N-terminal DEDDh
domain and the DNA-binding residues in the Zn-domain. The structural comparison of
CRN-4 to a number of dimeric DEDDh family nucleases, PARN, TREX2 and RNase T,
further demonstrated that CRN-4 both dimerizes and interacts with DNA in a unique way.
Combining all these data, we suggest a structural model where DNA is bound at the
Zn-domain and cleaved at the DEDDh nuclease domain in CRN-4 when the cell is triggered
for apoptosis.

The Crystal Structures of 2-aminobenzothiazolebased Inhibitors in Complexes with the
Urokinase-type Plasminogen Activator

P-16

Longguang Jiang1,2 , Haiyang Yu3, Cai Yuan1, Jundong Wang 3, LiQing Chen 4 ,Edward J.Meehan4, Zixiang Huang 1, Mingdong Huang 1
1
Fujian Institute of Research on the Structure of Matter, The Chinese Academy of
Sciences, Fuzhou, Fujian 350002, China (mhuang@fjirsm.ac.cn)
2Graduate School of the Chinese Academy of Sciences, Beijing 100039, China(jianglg07@gmail.com)
3
University of FuZhou, FuZhou, 350108, China( yhyang198@gmail.com)
4
University of Alabama in Huntsville, Huntsville, AL 35899, USA(chenlq@uah.edu)

Urokinase-type plasminogen activator (uPA) plays a crucial role in the regulation ofplasminogen activation, tumor cell adhesion and migration[1]. The inhibition of uPA activity is
a promising mechanism for anti-cancer therapy[2]. Most current uPA inhibitors employ ahighly basic group (either amidine or guanidine group) to target the S1 pocket of uPA active
site, which leads to poor oral bioavailability[3]. Here we study the possibility to use less basic
2-aminobenzothiazole (ABT) as S1 pocket binding group. We report the crystal structures of
the complexes of uPA with ABT or with 2-amino-benzothiazole-6-carboxylic acid ethyl ester(ABTCE). The inhibitory constants of these two inhibitors were measured by a chromogenic
competitive assay, and it was found that ABTCE is a better inhibitor for uPA (Ki = 656μM)
than ABT (Ki = 5.03mM). This work shows that the 2-amniobenzothiazole can be used as P1
group which may have better oral bioavailability than the commonly used amidine or
guanidine group. We also found the ethyl ester group occupies the characteristic oxyanion
hole and contacts to uPA 37- and 60-loops. These works provides structural information forfurther improvements of potency and selectivity of this new class of uPA inhibitor.
References
1.
2.
3.

Fazioli, F. and F. Blasi, Urokinase-type plasminogen activator and its receptor: new targets foranti-metastatic therapy? Trends Pharmacol Sci, 1994. 15(1): p. 25-9.
Andreasen, P.A., et al., The urokinase-type plasminogen activator system in cancer metastasis: areview. Int J Cancer, 1997. 72(1): p. 1-22.
Rockway, T.W. and V.L. Giranda, Inhibitors of the proteolytic activity of urokinase type plasminogenactivator. Curr Pharm Des, 2003. 9(19): p. 1483-98.

- 107 -

AsCA’09

Poster

Structural and biochemical characterization of yeast
monothiol glutaredoxin Grx6/YDL010W

P-17

Ming Luo1, Yong-Liang Jiang1, Xiao-Xiao Ma1, Ya-Jun Tang1, Yong-Xing He1,
Jiang Yu1, Rong-Guang Zhang2, Yuxing Chen1 and Cong-Zhao Zhou1
1
Hefei National Laboratory for Physical Sciences at Microscale and School of Life
Sciences, University of Science and Technology of China, Hefei, Anhui, 230027,
People’s Republic of China
2
Structural Biology Center, Argonne National Laboratory, 9700 South Cass Avenue,
Argonne, IL 60439 USA

Glutaredoxins (Grxs) represent a ubiquitous family of proteins which could reduce thedisulfide bonds of their substrate proteins with reduced glutathione. Saccharomyces cerevisiae
Grx6 is a monothiol Grx whose active-site sequence (CSYS) is reminiscent of CPYC
active-site sequence of classic dithiol Grxs. Grx6 contains an N-terminal signal sequence(M1-I36) and localizes at the endoplasmic reticulum and Golgi compartments. We found thatGrx6 is able to dimerize through its N-terminal domain (K37-T110) and could further be
bridged by a putative [2Fe-2S] cluster to form tetramer. We also demonstrate that Grx6 is thefirst monothiol Grx showing both glutathione-disulfide oxidoreductase activity andglutathione S-transferase activity. In the crystal structure of Grx6 C-terminal domain(K111-N231) we solved, a novel two-stranded antiparallel β-sheet motif was revealed besides
the classic Grx domain. This novel motif is unique among all known structures of Grxs, which
may characterize a novel Grx subfamily. Moreover, we suggest an active site motif without
tryptophan and proline residues which could lead to the identification of further Fe-S cluster
binding Grxs.

Structure and Interaction of Ubiquitin-AssociatedDomain of Human Fas Associated Factor 1

P-18

Joon Kyu Park1,2, JinSue Song3, Jae-Jin Lee4, Yun-Seok Choi3, Kyoung-Seok Ryu3,
Jae-Hong Kim2, Kong-Joo Lee4, Young-Ho Jeon3 and Eunice EunKyeong Kim1*
1Life Sciences Division, Korea Institute of Science and Technology, 39-1,
Hawolgok-dong, Sungbuk-gu, Seoul, Korea 136-791; (Eunice@kist.re.kr)
2School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu,
Seoul, Korea 136-701;
3
Korea Basic Science Institute, 804-1 Yangchung-Ri, Ochang, Chungbuk, Korea
363-883;
4
College of Pharmacy and Division of Life & Pharmaceutical Sciences, Ewha Womans
University, Seoul, Korea 120-750;

Fas associated factor 1 (FAF1) is a multi-domain protein that was first identified as a memberof the Fas death-inducing signaling complex, but later found to be involved in various
biological processes. Although the exact mechanisms are not clear, FAF1 appears to play animportant role in cancer, asbestos-induced mesotheliomas, and Parkinson’s disease. It
interacts with poly-ubiquitinated proteins, Hsp70, p97/VCP in addition to the proteins in theFas-signaling pathway. We have determined the crystal structure of the ubiquitin associateddomain of human FAF1 (hFAF1-UBA) and examined its interaction with ubiquitin andubiquitin-like proteins using NMR. The hFAF1-UBA revealed a canonical three-helicalbundle, and it selectively binds to mono- and di-ubiquitin (Lys48-linked), but not to SUMO-1- 108 -

AsCA’09

Posterand NEDD8. The interaction between the hFAF1-UBA and di-ubiquitin involves thehydrophobic interaction accompanied by a transition in the di-ubiquitin conformation. These
results provide structural insight into the mechanism of polyubiquitin recognition by
hFAF1-UBA
Acknowledgements: This work was supported by grants from the Functional Proteomics
Center, the 21C Frontier Research & Development Program of the Korea Ministry of Scienceand Technology, the Korea Institute of Science and Technology Institutional Program Grant.

P-19

New design platform for malonyl-CoA-acyl carrier
protein transacylase
Seung Kon Hong, Kook Han Kim, and Eunice EunKyeong Kim
Life Sciences Division, Korea Institute of Science and Technology, 39-1,
Hawolgok-dong, Sungbuk-gu, Seoul, Korea 136-791;(eunice@kist.re.kr)

The biosynthesis of fatty acids is a fundamental component of the cellular metabolic pathway,
since fatty acids are the essential building blocks for membrane phospholipid formation.
Since most bacteria and plants synthesize fatty acids using a discrete and highly conserved
group of enzymes called the type II fatty acid synthase (FAS II) system that is different fromyeast and animal which utilize the type I fatty acid synthase (FAS I), type II FAS system havebeen receiving enormous attention as possible antibiotic targets. Among them ismalonyl-CoA-acyl carrier protein transacylase (MCAT; FabD; EC2.3.1.39) which is
responsible for transferring the malonyl group from malonyl-CoA to the holo acyl carrier
protein (ACP). We have obtained the crystal structure of MCAT from Streptococcus aureus
and S. pneumoniae which are major pathogens at 1.46 and 2.0Ǻ resolution, respectively. The
data obtained could be used in aiding the process of novel inhibitor design.
Acknowledgements: This work was supported by grants from the Functional Proteomics
Center, the 21C Frontier Research & Development Program of the Korea Ministry of Scienceand Technology, the Korea Institute of Science and Technology Institutional Program Grant.

Structural Studies of Two PHP-like Tyrosine
Phosphatases, CpsB from Streptococcus
pneumoniae and YwqE from Bacillus subtilis

P-20

Hyoun Sook Kim1, Sang Jae Lee1, Do Jin Kim1, Hye-Jin Yoon1, Soon-Jong Kim3,
and Se Won Suh1,2
1
Department of Chemistry, College of Natural Sciences, Seoul National University,
151-747, Seoul, Korea (sewonsuh@snu.ac.kr)
2
Department of Biophysics and Chemical Biology, College of Natural Sciences, Seoul
National University, 151-747, Seoul, Korea (sewonsuh@snu.ac.kr)
3
Department of Chemistry, Mokpo National University, 534-729, Mokpo, Korea(sjkim@mokpo.ac.kr)

CpsB from Streptococcus pneumoniae and YwqE from Bacillus subtilis are therepresentatives of the novel bacterial manganese-dependent protein tyrosine phosphatases- 109 -

AsCA’09

Poster(PTPs), which are different from Cys-based eukaryotic and prokaryotic PTPs including
low-molecular-weight phosphotyrosine protein phosphatases. Influencing on pneumococcal
virulence and invasive disease of S. pneumoniae, CpsB regulates capsular polysaccharide
biosynthesis with CpsC and CpsD via tyrosine phosphorylation of CpsD, its cognate protein
tyrosine kinase. Recent reports show that YwqE acts toward various substrates including
single-stranded DNA-binding proteins and is involved in diverse functions such as bacterial
DNA metabolism or UDP-glucuronate biosynthesis. To gain insight into function at themolecular level, we have purified and crystallized CpsB and YwqE. X-ray diffraction data
were collected to high resolution, 2.0 Å and 1.6 Å, respectively. Two proteins are folded into a
TIM-barrel motif with a binuclear metal center. Our structural analyses support theclassification of these novel PTPs into the PHP (DNA polymerase and histidinol
phosphate)-related amidohydrolase superfamily and allows us to propose a reaction
mechanism of these enzymes.

P-21

Crystal structure and functional implications of thehuman Rad9-Hus1-Rad1 DNA damage checkpointcomplexJin Seok Kim, Sun Young Sohn, Gwang Hyeon Gwon and Yunje Cho
National Creative Initiatives for Structural Biology and Department of Life Science,
Pohang University of Science and Technology, Hyo-ja dong, San31, Pohang,
KyungBook, South Korea (yunje@postech.ac.kr)

Three evolutionarily conserved proteins, Rad9, Hus1, and Rad1, form a heterotrimeric 9–1–1
complex that plays critical roles in cellular responses to DNA damage by activating
checkpoints and by recruiting DNA repair enzymes to DNA lesions. We have determined the
crystal structure of the human Rad9 (residues 1–272)–Hus1–Rad1 complex at 2.5 Åresolution. The 91–272–1–1 complex forms a closed ring, with each subunit having a similar
structure. Despite its high level of similarity to proliferating cell nucleus antigen in terms ofoverall structure, the 91–272–1–1 complex exhibits notable differences in local structures,
including interdomain connecting loops, H2 and H3 helices, and loops in the vicinity of thehelices of each subunit. These local structural variations provide several unique features to the
9–1–1 heterotrimeric complex—including structures of intermolecular interfaces and theinner surface around the central hole, and different electrostatic potentials at and near theinterdomain connecting loops of each 9–1–1 subunit—compared to the proliferating cell
nucleus antigen trimer. We propose that these structural features allow the 9–1–1 complex tobind to a damaged DNA during checkpoint control and to serve as a platform for baseexcision repair. We also show that the 91–272–1–1 complex, but not the full-length 9–1–1
complex, forms a stable complex with the 5′ recessed DNA, suggesting that the C-terminal
tail of Rad9 is involved in the regulation of the 9–1–1 complex in DNA binding.

- 110 -

AsCA’09

P-22

Poster

Structural Basis for the Substrate Specificity andReaction Mechanism of Bacterial Aminopeptidase
Kyeong Kyu Kim1, Minh Hai Ta1, HyeJin Park1, Sangho Lee2
1
Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine,
Suwon 440-746, Korea (kkim@med.skku.ac.kr)
2
Department of Biological Science, Sungkyunkwan University, Suwon 440-746, Korea.

Aminopeptidases play an important role in diverse physiological processes including thecleavage of N-terminal methionine and the catabolic turnover of peptides into amino acids.
Their substrate specificities must be tightly regulated because unnecessary peptide cleavages
can result in the loss of essential cellular functions and cell death. PepS, a key
metallopeptidase in the protein turnover, shows specificity towards small peptides possessing
arginine or aromatic amino acids at the N-terminus, however, the mechanisms underlying thisspecificity and reaction are not clearly understood.
Using crystal structures of PepS and its complexes with substrate or inhibitors, we are able toelucidate how PepS differentiates its substrates from other functional proteins and how ithydrolyzes them. PepS consists of two domains and depending on their relative movements,
the conformation can be closed or open. The closed conformation of PepS prevents thesubstrate entry, but the open conformation accommodates the substrates into its binding
pocket that is a hole with 20 Å depth and 10 Å width. However, the enzyme can be fully
activated only in the closed conformation since the catalytic residues are rearranged into
active configuration in the close state. Taken these structural data together, we propose that
PepS alternates between open and closed conformations by domain movements during eachcatalytic cycle; opening for swallowing the substrates, closing for the hydrolysis of the boundsubstrates, and opening again for product release.

Structural study of Enhanced Intracellular Survival
protein, Eis protein from Mycobacterium tuberculosis

P-23

Kyoung Hoon Kim1, Ji Young Yoon1, Hyoun Sook Kim1, Sang Jae Lee1, Do Jin
Kim1, Hye-Jin Yoon1, and Se Won Suh1,2
1
Department of Chemistry, College of Natural Sciences, Seoul National University,
Seoul 151-742, Korea (sewonsuh@snu.ac.kr)
2
Department of Biophysics and Chemical Biology, College of Natural Sciences, Seoul
National University, Seoul 151-742, Korea (sewonsuh@snu.ac.kr)

Mycobacterium tuberculosis, the causative agent of tuberculosis, is one of the oldest
pathogens known to human and is responsible for the death of over 1.8 million people every
year. The pathogenic mycobacteria have developed strategies to circumvent the major killingmechanisms employed by macrophages and take advantage of the enclosed environment
within its host cell to avoid humoral and cell-mediated immune responses. Secretory proteinsplay a major role in host-pathogen interactions. The eis gene of Mycobacterium tuberculosis
has been shown to play a role in the survival of the avirulent Mycobacterium smegmatis
within the macrophage. Eis is present in cytosolic and cell envelope fractions of M.
tuberculosis. It is released into culture supernatants and into the cytoplasm of infected
macrophages. In one study, sera from 40% of pulmonary tuberculosis patients were positive- 111 -

AsCA’09

Posterfor anti-Eis antibody, indicating that the protein is antigenic. Eis reduces TNF-alpha and IL-4
production by mitogen-stimulated human T-cells, indicating that Eis affects T-cell function.
However, the eis mutant shows no growth defect in a macrophage cell line or in mice.
Bioinformatic analyses suggest that Eis is an acetyltransferase. Additional evidence indicatesthat it modulates the host immune response but the precise function of Eis is unclear.
To gain insight into the Eis protein function at the molecular level, we have purified andcrystallized Eis protein. X-ray diffraction data were collected to 2.85 Å using synchrotron
X-rays. The native crystal belongs to the monoclonal space group P21, with unit cellparameters of a = 108.13 Å, b = 150.19 Å, c = 184.38 Å, and α = γ = 90°, β = 103.05°. The
asymmetric unit contains twelve monomers, giving a crystal volume per protein mass (Vm) of
2.53 Å3 Da-1 and a solvent content of 51.5%. The structure was solved by single-wavelength
anomalous diffraction method and has been refined to crystallographic Rwork and Rfree valuesof 22.8% and 28.2%, respectively.

P-24

Study on Structural biology in disease
Myung-Il Kim, Woo-Suk Jung, Sangkee Rhee
School of Agricultural Biotechnology, Seoul National University, Seoul, Korea(mikim01@snu.ac.kr)

Amylosucrase from Neisseria polysaccharea (NpAS) is a transglucosidase of family 13
glycoside hydrolase which catalyzes the synthesis of amylase-like polymer by hydrolase andglucosyltransferase activity using sucrose as a substrate. Recently, a novel enzyme from
Xanthomonas axonopodis pv. glycines, with a high sequence similarity of 57% with that of
NpAS, was characterized as a member of the newly defined carbohydrate utilization locus
which regulates the utilization of plant sucrose in phytopathogenic bacteria. Interestingly, theenzyme named sucrose hydrolase (SUH) exhibits exclusively the hydrolase activity not a
glucosyltransferase activity. In order to elucidate structural and functional features of SUH,
we carried out crystallographic and site-directed mutagenesis. Four different crystal structuresof SUH, including the free enzyme, SUH-sucrose complex, and SUH-glucose complex, reveal
structural snapshots along the catalysis. Structural comparisons with NpAS provide that an
overall structure of SUH is essentially identical with that of NpAS, and that the active site of
SUH in the SUH-sucrose for the Michaelis complex is a pocket-type formed by
conformational change, while NpAS has a tunnel-type active site with no indication of theconformational changes by the binding of sucrose. Site-directed mutagenesis was performed
such that the active site residues in SUH were replaced with residues crucial for a
glucosyltransferase activity in NpAS. Our structural and functional analysis suggests that apocket-shaped active site and the identity of residues in the vicinity of the active site of SUH
are designed to be optimal for the unique hydrolytic activity of sucrose.

- 112 -

AsCA’09

Poster

Structural insights into TDP-43, a new player inneurodegenerative diseases

P-25

Pan-Hsien Kuo1,2, Lyudmila G. Doudeva2, Yi-Ting Wang1,2,3, Che-Kun James Shen2
and Hanna S. Yuan2,3,4,*
1
Institute of Bioinformatics and Structural Biology, National Tsing Hua University,
2
Institute of Molecular Biology, Academia Sinica,3
Taiwan International Graduate Program, Chemical Biology and Molecular Biophysics,
Academia Sinica,4
Graduate Institute of Biochemistry and Molecular Biology, National Taiwan University,
Taipei, Taiwan

TDP-43 is a pathogenic protein: its normal function in binding to UG-rich RNA is related tocystic fibrosis, and inclusion of its C-terminal fragments in brain cells is directly linked tofrontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). We
determined the crystal structure of the C-terminal RRM2 domain of TDP-43 in complex witha single-stranded DNA at a resolution of 1.65 Å. We show that TDP-43 is a dimeric proteinwith two RRM domains, both involved in DNA and RNA binding. The crystal structure
reveals the basis of TDP-43’s TG/UG preference in nucleic acids binding. It also reveals that
RRM2 domain has an atypical RRM-fold with an additional β-strand involved in making
protein-protein interactions. This self association of RRM2 domains produced thermal-stable
RRM2 assemblies with a melting point greater than 85oC as monitored by circular dichroismat physiological conditions. These studies thus characterize the recognition between TDP-43
and nucleic acids and the mode of RRM2 self association, and provide molecular models forunderstanding the role of TDP-43 in cystic fibrosis and the neurodegenerative diseases related
to TDP-43 proteinopathy.

- 113 -

AsCA’09

PosterP-26

Pushing low-resolution data to the limit - thestructure of the third component of the ligand bindingsite of the human insulin receptor
John G. Menting, Brian J. Smith, Colin W. Ward, Michael C. Lawrence
The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville,
Victoria 3052, Australia (lawrence@wehi.edu.au)

Despite the structure of insulin being known for over forty years1, the structural detail of themanner in which it binds to its receptor and effects signalling remains elusive. Our crystal
structure2 of the apo-form of the human insulin receptor ectodomain homodimer at 3.8 Å
resolution revealed that the ligand binding site is formed by a juxtaposition of the first leucinerich-repeat domain (L1) of one monomer with the first and second fibronectin domains of thealternate monomer. Such a mode of assembly of the ligand binding site was, in particular,consistent with the symmetric, alternative cross-linking model of insulin binding to its
receptor and thus provided the first structural basis for the negative cooperativity of ligand
binding displayed by the receptor3.
However, absent from the resolved structure was the C-terminal region of the receptor
α-chain. This segment of sixteen residues (the "αCT peptide", residues 704-719) lies within adisordered segment of the receptor and is known to be absolutely essential for ligand binding4.
Strikingly, addition of this peptide in exogenous form is able to restore ligand binding ability
to certain domain-minimised receptor fragments that are otherwise devoid of such ability5.
The crystal structure of the apo-form of the receptor did, however, contain a tube-likesegment of difference electron density lying on the insulin-binding surface of L1 and at thetime resisted all attempts at interpretation, though we surmised that it might have arisen fromthe αCT peptide2.
We have now devised techniques that have led to a clear interpretation of the electron density
segment as arising from residues within the C-terminal region of the receptor α-chain (seeFigure).

Figure Schematic view of the C-terminal segment of the insulin receptor α-chain

We thus have obtained the first view of the mode of assembly of all three components of theinsulin binding site. The implications are profound. (1) The structure creates an entirely newparadigm about how insulin might bind to its receptor. (2) Combined with our isothermal
titration calorimetry data, the structure explains the mode of binding of the so-called Site 1class of insulin mimetic peptides which have been developed to bind to the insulin receptor
with high affinity6. (3) The findings carry over directly to the type 1 insulin-like growth factor
receptor system, suggesting that the αCT peptide binding site on L1 may in fact be a target for
anti-cancer therapeutics.
- 114 -

AsCA’09

Poster

References:[1]. Harding, M.M., et al., J. Mol. Biol. 16, 212-26 (1966).
[2]. McKern, N.M. et al., Nature 443, 218-21 (2006).
[3]. De Meyts, P. Diabetologia 37 Suppl. 2, S135-48 (1994).
[4]. Ward, C.W. & Lawrence, M.C. Bioessays 31, 422-34 (2009).
[5]. Kristensen, C., et al., J. Biol. Chem. 277, 18340-5 (2002).
[6]. Schäffer, L. et al. PNAS 100, 4435-9 (2003).

Crystal structures of aprotinin and its complexs

P-27

Ji-Hye Lee1, In Seok Yang1, Ki Joon Cho2, Intekhab Alam1, Yi Ho Park1, and Kyung
Hyun Kim1
1
Department of Biotechnology & Bioinformatics, College of Science & Technology,
Korea University, Chungnam 339-700, Korea
graduate@korea.ac.kr;
Intekhab@korea.ac.kr;(jihyelee@korea.ac.kr;
ballashe@naver.com; khkim@korea.ac.kr )2School of Life Sciences & Biotechnology, Korea University, Seoul 136-701, Korea(c-azna@korea.ac.kr)

Aprotinin has been shown to decrease heparin binding to platelets. Heparin which is a highly
sulfated glycosaminoglycan is an anticoagulant produced by mast cells. In addition, heparansulfate is known to be able to facilitate formation of the protofilament for amyloid
fibrillogenesis. The crystal structures of aprotinin complexed with sucrose octasulfate (SOS)and Val-Phe-Phe (VFF) were determined at 1.7 and 1.6 Å resolutions, respectively. The
crystal structure of aprotinin complexed with SOS, a polysulfated heparin analog, showed
three aprotinin molecules per one SOS in the asymmetric unit. However, five aprotinins seemto be randomly arranged to form a complex with one SOS molecule. The sulfate groups of
SOS interact with positively charged residues Lys and Arg, from which a binding mode ofheparin to aprotinin is described. A tripeptide VFF was accidently observed at themonomer-monomer interface in a decameric form of aprotinin at acidic pH, which was
confirmed by cocrystallization with a synthesized VFF tripeptide. Although there is no direct
evidence for the origin of VFF, a hydrophobic region including VFF in amyloid beta is known
to play a critical role in nucleation of amyloid formation. The interaction of aprotinin with thetripeptide is described.

P-28

Crystal Structure of the Glycosyltransferase Domain
of Cholesterol-α-Glycosyltransferase from
Helicobacter pylori
Sang Jae Lee1, Hyoun Sook Kim1, Do Jin Kim1, Kyoung Hoon Kim1, Ji Young
Yoon1, Jun Young Jang1, Hye-Jin Yoon1, Se Won Suh1,2
1
Department of Chemistry, College of Natural Sciences, Seoul National University,
151-747, Seoul, Korea (sewonsuh@snu.ac.kr)
2
Department of Biophysics and Chemical Biology, College of Natural Sciences, Seoul
National University, 151-747, Seoul, Korea (sewonsuh@snu.ac.kr)

Helicobacter pylori infection causes gastric pathology such as ulcer and carcinoma. H. pylori
follows a cholesterol gradient and extracts the lipid from plasma membranes of humanstomach epithelial cells for subsequent glucosylation by cholesterol-α-glycosyltransferase.
- 115 -

AsCA’09

PosterCholesterol-α-glycosyltransferase abrogates phagocytosis of H. pylori and subsequent T cell
activation. Thus the development of antibiotics could be possible based on the inhibition ofcholesterol glucosylation. To provide the structural basis for inhibitor discovery, we havedeterminedthecrystalstructureoftheglycosyltransferase
domainofcholesterol-α-glycosyltransferase from H. pylori. X-ray diffraction data were collected to 1.5
Å using synchrotron X-rays. The native crystals are triclinic, belonging to the space group P1,
with unit-cell parameters a = 35.79 Å, b = 40.71 Å, c = 53.74 Å, and α = 101.44°, β = 94.87°,
γ = 90.58°. The asymmetric unit contains two monomers, giving a crystal volume per protein
mass (VM) of 1.91 Å3 Da-1 and a solvent content of 35.7%. The structure was solved bymulti-wavelength anomalous diffraction method and has been refined to crystallographic Rwork
and Rfree values of 19.2% and 23.3%, respectively.

P-29

A Novel 'in situ' Inhibitor Elongation Strategy
Produces a Stable Covalent Intermediate With Human
Pancreatic Alpha-Amylase
Chunmin Li1, Ran Zhang2, Leslie K. Williams1, Brian P. Rempel2, Stephen G.
Withers2, Gary D. Brayer1
1
Department of Biochemistry and Molecular Biology, University of British Columbia,
Vancouver, BC V6T 1Z3, Canada (chunmin.li@gmail.com)
2
Chemsitry Department, University of British Columbia, Vancouver, BC V6T 1Z1,
CanadaHuman pancreatic α-amylase (HPA) is a key endoglycosidase involved in the digestion of
dietary starch in the gut. Control of the activity of HPA thus provides a valuable therapeutic
approach for diseases such as diabetes and obesity. Despite extensive mechanistic studies of
HPA, determination of a detailed structure of a trapped covalent glycosyl-enzyme
intermediate has proven elusive. To remedy this situation we have developed a new in situ
strategy for trapping and subsequent structural elucidation of HPA glycosyl-enzyme
intermediates. In particular, our structural studies unambiguously show the covalentattachment of a 5-fluoro-α-L-idosyl moiety in the chair conformation to the side chain of thecatalytic nucleophile D197. The elongated versions of this intermediate complex are found tobind in the high affinity -2 and -3 binding subsites, where they form extensive hydrogenbonding interactions. Comparison of these structural results with the related non-covalent
complex formed by acarbose highlights the structural rigidity of the enzyme surface and the
key role that substrate conformational flexibility plays during catalysis. Collectively, ourstructural results provide insight into several key catalytic steps.

- 116 -

AsCA’09

PosterCrystallization and preliminary X-ray crystallographic
studies of O-methyltransferase from the Anabaena
Pcc 7120

P-30

Guoming Li 1,3, Zhenting Tang1,2, Geng Meng1,2, Kesheng Dai3, Jindong Zhao1,2,
Xiaofeng Zheng1,2*
1
National Laboratory of Protein Engineering and Plant Genetic Engineering,2
Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking
University, Beijing, 100871, .China,(gml_1002@yahoo.com.cn, xiaofengz@pku.edu.cn* )3School of Biological Science and Medical Engineering, Beihang University, Beijing
100191, P.R.China.

O-methyltransferase (OMT) is a ubiquitous enzyme that exists in bacteria, plants and humans,
which catalyzes a methyl transfer reaction using S-adenosyl-L-methionine-(AdoMet) as amethyl donor and a wide range of phenolics as acceptor. To investigate the structure andfunction of OMTs, omt from the Anabaena Pcc 7120 was cloned into expression vector
pET21 and expressed in soluble form in Escherichia coli strain BL21(DE3). The recombinant
OMT protein was purified to homogeneity through a two-step strategy. A preliminary crystal
image of OMT was provided using hanging-drop vapor diffusion method. The crystals of
OMT diffracted to a resolution of 2.4 Å and belong to C2221 space group. The unit cellparameters are a=131.620 Å, b=227.994 Å, c=150.777 Å, α=β=γ=90°. There may be 8
molecules per asymmetry unit.

P-31

Crystallographic study of NQO2 and structure-based
ligand design
Yazhuo Li, Cristina de Matteis
School of Pharmacy, Center for Biomolecular Sciences, The University of Nottingham,
University Park, Nottingham, NG7 2RD, UK. (paxyl1@nottingham.ac.uk)

NQO2, which is one of flavoprotiens also known as QR2, was discovered decades ago[1-3].
Its sequence and tissue distribution has been studied widely, and results suggest that
distribution depends on the species. The role of NQO2 has also been investigated, and current
opinion is that NQO2 is one of the detoxifying enzymes in Phase II; it shows a sequence
identity with its analogue NQO1, another detoxifying enzyme, of about 49% and it alsofunctions to carry out two-electron transfer to reduce quinones to stable intermediates such ashydroquinones [3. However, this was challenged by experimental data obtained when
menadione was tested in both wild type and NQO2 knocked out mice. Menadione which is
supposed to undergo one-electron reduction to produce semiquinone to damage tissues
appeared to be not toxic in the absence of NQO2 in the knocked out model. We know a little
about the structure of NQO2 until its apo-structure was published in 1999. But theunderstanding of binding mode of its substrates and inhibitors with enzyme is still very
limited.
Protein-ligand complexes have been successfully co-crystallized, including substrates andinhibitors. High-resolution datasets have been collected at Synchrotron. Atomic structures ofcomplexes have been built to reveal the binding mode of the ligands. Density map indicated- 117 -

AsCA’09

Posterthe presence of ligands in the binding pockets, and the orientations and positions of theligands are quite clear. On the other hand, because NQO2 is one of the heated targets forcancer therapy, the NQO2 structure-based ligand design was carried out through screening
chemical database in order to find novel inhibitors or substrates of NQO2 on the basis ofmodes interpreted from the crystal structure since its ambiguity on function. One of the highresolution crystal structures (PDB entry: 1SG0) from Brookhaven database was used as thetarget model, the docking suite GOLD and Gold scoring function were adopted to screen thelibrary to identify the compound as candidates to cure cancer and other diseases, the active
site was refined by molecular dynamic simulation. In addition, preliminary enrichment of its
natural inhibitors was done; one of its predicted modes has been confirmed by its crystal
structure. Sub library was built, which the potential substrates or inhibitors were filtered byphysical or chemical properties. Their bioactivities need to be measured as to categorize in the
future.
References
1.
2.
3.

Liao, S. and H.G. Williams-Ashman, Inhibition of the enzymic oxidation of some dihydropyridines bypolycyclic aromatic hydrocarbons. Biochemical Pharmacology, 1961. 6(1-2): p. 53-54.
Liao, S. and H.G. Williams-Ashman, Enzymatic oxidation of some non-phosphorylated derivatives ofdihydronicotinamide. Biochemical and Biophysical Research Communications, 1961. 4(3): p.
208-213.
Liao, S., J.T. Dulaney, and H.G. Williams-Ashman, Purification and Properties of a Flavoprotein
Catalyzing the Oxidation of Reduced Ribosyl Nicotinamide. 1962. p. 2981-2987.

P-32

Insights into the Alkyl Peroxide Reduction Pathway of
Xanthomonas campestris Bacterioferritin
Comigratory Protein from Trapped
Intermediate/Ligand Complex Structures
Shu-Ju Liao1, Chao-Yu Yang1, Ko-Hsin Chin3, Andrew H.-J. Wang2 & Shan-Ho
Chou1, 3
1
Institute of Biochemistry, National Chung-Hsing University, Taichung, 40227, Taiwan
2
Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan
3
National Chung Hsing University Biotechnology Center, Taichung, 40227, Taiwan,(shchou@nchu.edu.tw)

Considerable insights into the alkyl peroxide oxidoreduction activity of Xanthomonas
campestris bacterioferritin comigratory protein (XcBCP) have been obtained from trappedintermediate/ligand complex structures determined by X-ray crystallography. Multiple
sequence alignment and enzyme assay indicated that XcBCP belongs to a subfamily of
atypical 2-Cys peroxiredoxins (Prxs), containing a strictly conserved peroxidatic cysteine(CP48) and an unconserved resolving cysteine residue (CR84). Crystals at different states, i.e.
Free_SH state, Intra_SS state, and Inter_SS state, were obtained by screening the XcBCP
proteins from a double C48S/C84S mutant, a wild-type, and a C48A mutant, respectively. A
formate or an alkyl analog with two water molecules that mimic an alkyl peroxide substrate
was found close to the active site of the Free_SH or Inter_SS state, respectively. Their global
structures were also found to contain a novel substrate binding pocket capable ofaccommodating an alkyl chain no less than 16 carbons. In addition, in the Intra_SS or- 118 -

AsCA’09

PosterInter_SS state, substantial local unfolding or complete unfolding of the CR-helix was detected,
with the CP-helix remaining essentially unchanged, which is in sheer contrast with theobservation before that the CP-helix exhibits local unfolding during disulfide bond formation
in typical 2-Cys Prxs. These rich experimental data have enabled us to draw a pathway on
how XcBCP carries out its oxidoreduction activity through the alternate opening and closingof the substrate entry channel and the disulfide-bond pocket.
References
Liao S-J, Yang C-Y, Chin K-H, Wang AH-J, Chou S-H. Insights into the Alkyl Peroxide Reduction Pathway
of Xanthomonas campestris Bacterioferritin Comigratory Protein from Trapped Intermediate/Ligand
Complex Structures. J Mol Biol 2009; in press

P-33

Crystal Structure of the Cytoplasmic Domain of theType II Secretion System Component EpsL of Vibrio
parahaemolyticus
Li-Ying Lin1, Nien-Tai Hu1, and Nei-Li Chan1, 21Institute of Biochemistry, College of Life Sciences, National Chung Hsing University,
Taichung, Taiwan.(sparklingstonelin@gmail.com)
2
Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan
University, Taipei, Taiwan. ( nlchan@ntu.edu.tw)

The type II secretion system (T2SS) is used for the translocation of fully folded extracellular
proteins across the outer membrane of Gram-negative bacteria. At least 12 distinct protein
components are required for the functioning of T2SS by forming a secretion nano-machinethat spans both the outer and inner membranes, providing a direct connection between thecytoplasm and outer membrane. Such a trans-envelop assembly couples ATP hydrolysis,taking place exclusively in the cytoplasm, to protein translocation. In T2SS, the cytosolic
secretion ATPase EpsE is recruited to the membrane-associated secretion complex byinteracting with the cytoplasmic membrane proteins EpsL. Therefore, EpsL serves as a criticallink between ATP utilization and exoprotein secretion. To provide a structural understandingof this critical interaction, we have determined the crystal structure of cytoplasmic domain of
EpsL from V. parahaemolyticus at 2.6 Å resolution by the multiwavelength anomalous
diffraction (MAD) method. The analysis of the structure will be presented during the meeting.

P-34

Crystal Optimization of a Secondary Transporter
Membrane Protein to 4.5 Å Resolution
Xiangyu Liu1,2, Pontus Gourdon1, Xiaodong Su2, Poul Nissen1
1Center of Structural Biology, Department of Molecular Biology, Aarhus University,
Science Park, Gustav Wieds Vej 10C, 8000 Aahus, Denmark (xyliu@bioxray.au.dk)
2School of Life Sciences, Peking University, Beijing100871, China

Integral membrane proteins represent about 20–30% of the total proteins of various organisms.
Despite their important physiological roles, they are highly underrepresented in the protein
data bank (PDB), due to the difficulties in overproducing, purifying, stabilizing andcrystallizing them. This is mainly due to their amphipathic character; the existence of a
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AsCA’09

Posterhydrophobic surface requires detergent micelles to make them soluble in an aqueous solution,
but frequently this treatment also adversely affects their activity (due to e.g. loss of cofactors,
lipids or subunits) as well as the chances to acquire well-diffracting crystals (due to e.g.
hindrance of potential crystal contacts).
The formate transporter FocA, which belongs to the formate-nitrite transporter (FNT) family,
exists in several bacteria, archaea and yeasts. In general, FocA homologs are 250-300 residues
in length with 6 putative transmembrane helices and they share no apparent similarity withany structures in the PDB. The first FocA protein was found in E.coli and it is believed to be
involved in formate influx and/or efflux while using protons as the symport counter ions(Suppmann B & Sawers G., 1994, Mol Microbiol. 11(5): 965-82). As such, FocA may be a
key protein in regulating the intracelullar formate concentration during cell anaerobic growth.
Pyruvate formate-lyase (PFL) converts pyruvate to formate and acetyl CoA under anaerobic
conditions (Becker A & Kabsch W, 2002, J Biol Chem. 277(42): 40036-42). Hence the levelsof these products have to be tightly controlled; the concentration of formate is also importantas the substance may trigger various transcription regulators (such as FHLA) and its
accumulation could furthermore result in cytoplasmic acidification and an uncoupled proton
gradient (R.G. Sawers, 2005, Biochem Soc Trans, 33, 42). A high resolution model of FocA
would help to elucidate the substrate binding and transport mechanism of the entire FNT
family.
We have cloned and expressed a bacterial FocA. Specific truncations were made to prevent
spontaneous degradation and a His-tag was added to facilitate purification. The solubilization
detergent and concentration was optimized, and the protein was purified with Ni2+ affinity andSuperdex 200 size-exclusion chromatography. For the subsequent crystallization experiments,
the most suitable protein buffer and detergent, as judged by multiple Superdex 200 PC gel
filtration runs, was selected after a relatively large screen of conditions. Initial crystallization
hits were obtained following screening with several detergents, but the size and diffraction
properties were limited. Optimized crystals grew to larger size (0.2 mm * 0.15 mm * 0.1mm)
and the best ones diffracted to 4.5 Å at MAXLAB (Sweden). However, the crystals still sufferfrom anisotropy, and display diffuse scattering and high mosaicity. We will report on thesubtle modifications of the preparation protocol that enabled the initial crystals to form. In
addition, the careful and systematic approach to optimize these crystals from the first small
diffracting entities to the current resolution will be presented. We will also show how we wish
combat the existing diffraction obstacles and improve the resolution beyond 4.5 Å in the near
future. We believe that several of these approaches may be of general interest for otherprojects where crystals of membrane proteins are sought for.

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P-35

PosterThe crystal structure of a replicative hexamerichelicase DnaC and its complex with single-strandedDNA
Yu-Hua Lo1,2, Kuang-Lei Tsai1,2, Yuh-Ju Sun2, Wei-Ti Chen1, Cheng-Yang Huang1
and Chwan-Deng Hsiao1
1Institute of Molecular Biology, Academia Sinica, Taipei, 115, Taiwan(d948227@oz.nthu.edu.tw)
2Institute of Bioinformatics and Structural Biology, National Tsing Hua University,
Hsinchu, 300, Taiwan

DNA helicases are motor proteins that play essential roles in DNA replication, repair, andrecombination. In the replicative hexameric helicase, the fundamental reaction is theunwinding of duplex DNA; however, our understanding of this function remains vague due toinsufficient structural information. Here, we report two crystal structures of the DnaB-family
replicative helicase from Geobacillus kaustophilus HTA426 (GkDnaC) in the apo-form andbound to single-stranded DNA (ssDNA). The GkDnaC-ssDNA complex structure reveals thatthree symmetrical basic grooves on the interior surface of the hexamer individually encircle
ssDNA. The ssDNA-binding pockets in this structure are directed toward the N-terminal
domain collar of the hexameric ring, thus orienting the ssDNA towards the DnaG primase tofacilitate the synthesis of short RNA primers. These findings provide insight into themechanism of ssDNA binding and provide a working model to establish a novel mechanism
for DNA translocation at the replication fork.

Structures of yeast glutathione S-transferase Gtt2
reveal a new catalytic type of GST family

P-36

Xiao-Xiao Ma, Yong-Liang Jiang, Yong-Xing He, Rui Bao, Yuxing Chen andCong-Zhao Zhou*
Hefei National Laboratory for Physical Sciences at Microscale, and School of Life
Sciences, University of Science and Technology of China, Hefei, Anhui, 230027,
People’s Republic of China (zcz@ustc.edu.cn)

Glutathione S-transferases (GSTs) are ubiquitous detoxification enzymes which catalyze theconjugation of electrophilic substrates to glutathione (GSH). Here we solved thethree-dimensional structures of Saccharomyces cerevisiae Gtt2 in apo- and two ligand-boundforms at 2.23, 2.20 and 2.10 Å, respectively. Despite sharing a similar overall structure toother GSTs, lack of any classic catalytic essential residues (Tyr, Ser and Cys) distinguishes
this first fungal GST structure from all cytosolic GSTs of known structures. Subsequentsite-directed mutagenesis in combination with activity assays reveal that a water moleculestabilized by Ser129 and His133 works as the deprotonator towards GSH sulfur atom insteadof the classic catalytic residues. Moreover, due to the stereo-hindrance between helix α1 and
GSH, only glycine and alanine are permitted at the N-terminus of helix α1. Taken together,yeast Gtt2 represents a novel atypical-type of cytosolic GSTs which are dominantly
distributed in lower organisms.

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P-37

PosterFragment-based screening by X-ray crystallography:
discovery of novel inhibitors targeting theadrenaline-synthesising enzyme
Jennifer L Martin1, Nyssa Drinkwater1, Gary Grunewald2 and Michael McLeish3
1
Institute for Molecular Bioscience, University of Queensland Brisbane QLD 4072;
2
Kansas University Lawrence Kansas USA;
3
IUPUI Indiana USA

Fragment-based lead discovery is a relatively new approach to drug design that involves
screening libraries of compounds that are significantly smaller (typically 120-250 Da) thandrug molecules (typically up to 500 Da) [1-3]. The rationale is that “drug-like” fragments
represent individual binding epitopes whereas larger “drug-like” compounds found inconventional high throughput screen (HTS) libraries represent combinations of binding
epitopes. Drug-like fragments that bind would have lower affinities than drug-like compounds,
but would be more “efficient” ligands – and therefore better starting points for leaddevelopment - because a greater proportion of atoms are involved in favourable receptor
contacts.
A major advantage of fragment-screening is that it more efficiently samples chemical spacethan traditional screening approaches [4-5] and therefore requires significantly fewer
compounds to be screened. For example, a library of 400 fragments screened on a two
sub-site receptor samples chemical space as efficiently as a library of drug-like compounds
containing all possible linked combinations of the fragments (400x400 or 160,000
compounds). Consequently, fragment libraries typically contain a few hundred fragments,
whereas HTS libraries may contain hundreds of thousands of compounds.
Hits from a fragment library have Kd values lower than those of hits from HTS libraries, andtypically in the range of 1 mM-10 μM [3, 5]. As a consequence they would often not registeras hits in the functional assays used for HTS. Therefore fragment-screening approaches use
highly sensitive techniques, such as X-ray crystallography, that can detect low-affinity
binding and which can directly identify the binding site, the binding orientation andfavourable interactions formed by the fragment. This level of detail is exploited in subsequent
steps to optimise potency and selectivity using standard medicinal chemistry techniques.
We have used fragment-based screening by X-ray crystallography to identify fragments thatbind to PNMT, the adrenaline-synthesising enzyme. Inhibitors of PNMT have the potential to
be used in the treatment of hypertension and will also represent novel pharmacological tools
to probe the role of adrenaline in the central nervous system. We screened a commercial
library of 384 compounds, as cocktails of 4 compounds. and identified 12 hits (ie drug-likefragmetns that bound to PNMT). Nine of these hits were further characterised by ITC andfound to have dissociation constants in the micromolar to sub-millimolar range. The binding
affinity of the remaining three hits was too low to be detected by ITC. Using simple medicinal
chemistry modifications we were able to improve the binding affinity of the best hits by
10-fold whilst maintaining a high ligand efficiency. The inhibitory effect of the modified
compounds on PNMT enzyme activity was also investigated using a standard radio-assay.
The efficiency and speed of the fragment-based screening approach for discovery anddevelopment of new drug leads is highlighted by the fact that all of the research - spanning- 122 -

AsCA’09

Posterprotein expression to crystallography, ITC, medicinal chemistry and enzyme kinetics - wasperformed by one PhD student over a period of 18 months.
References
1.
2.
3.
4.
5.

Lesuisse, D. et al. J Med Chem 45, 2379-87 (2002).
Hartshorn, M. J. et al. J Med Chem 48, 403-13 (2005).
Rees, D. C., Congreve, M., Murray, C. W. & Carr, R. Nat Rev Drug Discov 3, 660-72 (2004).
Andrews, P. R., Craik, D. J. & Martin, J. L. J Med Chem 27, 1648-57 (1984).
Carr, R. A., Congreve, M., Murray, C. W. & Rees, D. C. Drug Discov Today 10, 987-92 (2005).

Crystal structure of PACSIN 1 F-BAR domain reveals
a novel membrane curvature sensing mechanism

P-38

Geng Meng1,2, Xiaoyun Bai1,2,Guoming Li2, Yong Liu1,2, Ming Luo3, Xiaofeng
Zheng1,2*
1National Laboratory of Protein Engineering and Plant Genetic Engineering,2
Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking
University, Beijing, 100871, .China, (mengg@pku.edu.cn, xiaofengz@pku.edu.cn* )3Department of Microbiology, University of Alabama at Birmingham, Birmingham,
Alabama, 35294,USA.

Protein kinase C and casein kinase 2 substrate in neurons (PACSIN), also named sydapin, is a
protein family involved in the vehicle transportation and endocytosis. The characteristic of
this family is the Fer-CIP4 homology-BAR (F-BAR) domain in the N terminus with asubsequent SCH domain. F-BAR (FCH-BAR) domain proteins have been found withmembrane-deforming properties and could form membrane invaginations or tubulation
through the dimerized crescent-shaped molecules. The curvature of the membrane tubules
depends on the BAR domain structure and the oligomerization of the proteins. Unlike anyother F-BAR domain that generates low curvature tubules, PACSIN protein could not only
generate the common tubules but also lead to high curvature tubules and tubules fission. In
order to investigate the novel tabulation mechanism of the PACSINs, we crystallized andsolved the structure of the F-BAR domain of PACSIN 1. The structure reveals a unique loop
extrudes from the protein surface and influences the curvature of membrane bending mediatedby the protein. This extruded loop lead to the small tubules’ formation and suggests the
profound function of PACSINs in vesiculation and endocytosis difference with other F-BAR
domain proteins.

Stabilization mechanism by Hyp-Thr-Gly sequence incollagen-helix

P-39

Keita Miyama1, Tatsuya Morimoto1, Koichi Masakiyo1, Tatsuya Kawaguchi1, Kenji
Okuyama1, Kazunori Mizuno2, Hans Peter Bächinger2
1 Department of Macromolecular Science, Graduate School of Science, Osaka
University, Toyonaka 560-0043, JAPAN (okuyamak@chem.sci.osaka-u.ac.jp)
2 Shriners Hospital for Children, Research Department, Portland, Oregon 97239, USA

Collagen is the most abundant protein found in animals. It has a charactistic amino acidsequence; Gly at every third position and high content of imino acid (Pro and Hyp). Therfore,- 123 -

AsCA’09

Posterits amino acid sequence has been designated by (Xaa-Yaa-Gly)n, where the X and Y positions
are frequently occupied by Pro and Hyp, respectively. Because of this sequence constraint,collagens adopt a triple-helical structure. For the last two decades, it was believed that only
the Hyp residues in the Y position stabilize the collagen-helix. However, it was shown
recently that the Hyp residues in the X position also stabilize the triple-helical structure in the
Hyp-Hyp-Gly and Hyp-Thr-Gly sequences. Especially, the latter sequence seems to be
utilized for the stabilization of cuticle collagen of Riftia pachyptila [1]. To understand thestabilization mechanism of this sequence, we analyzed high resolution structures of host-guest
peptides, (Pro-Pro-Gly)4-Hyp-Yaa-Gly- (Pro-Pro-Gly)4 (hereafter, OYG) (Yaa = Thr, Val,
Ser).
Crystals of OTG, OVG and OSG peptides were obtained by a hanging- or sitting-drop vapor
diffusion method. The diffraction data were collected at SPring-8 (BL41XU and BL44XU) at
100K. Crystals of OTG and OVG peptides exhibited pseudo-merohedral twinning, while the
OSG peptide grew as a single crystal with similar lattice parameters as those of other two.
Structures of these peptides were obtained by the molecular replacement method and refinedby SHELXL at high resolution (< 1.2 Å).

Fig.1 Inter-atomic distances between Hyp213 (X) and Thr114 (Y) of the OTG peptide

Detailed structures in the guest regions revealed the importance of interaction between Hyp in
the X position and Yaa of the adjacent strand in the same molecule (Hyp(X):Yaa stackingpair). As an example, Hyp(X):Thr (Y) stacking pair is shown in Fig.1. By adopting gauche+
conformation, the plane of Thr side chain defined by Cα, Cβ, Cγ and Oδ atoms faced the ringplane of imino acid with van der Waals contacts between them. Similar interaction was also
observed in the OVG crystal. This interaction seems to be important for the stabilization on
the triple-helical structure in these peptides.
Reference
K. Mann et al. J. Mol. Biol., 261, 255(1996)- 124 -

AsCA’09

PosterProtein Function Annotation from Sequences andStructures with Tools at PDBj

P-40

Daron M. Standley1, Mieszko Lis2, Akira R. Kinjo3, Haruki Nakamura4
1
Immunology Frontier Research Center, Osaka University, 3-2 Yamadaoka, Suita,
Osaka 565-0871, Japan (standley@ifrec.osaka-u.ac.jp)
2
MIT Computer Science and Artificial Intelligence Laboratory, 32 Vassar street,
Cambridge, MA, USA (mieszko@csail.mit.edu)
3
PDBj, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka
565-0871, Japan (akinjo@protein.osaka-u.ac.jp)
4PDBj, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka
565-0871, Japan (harukin@protein.osaka-u.ac.jp)

The aim of structural genomics is to characterize protein function at the residue and atomic
levels for target proteins without known function. More and more new protein sequences
continue to appear with the rapid development of genome analysis methods, and prediction offunction from only sequence information is highly desirable. We have developed a pipeline
system to annotate protein function from sequences (and, when available, structural
information), and make it available to the public from the PDBj web site[1](http://www.pdbj.org).
SFAS (Sequence to Function Annotation Server, http://www.pdbj.org/sfas/) is a web-based
tool for predicting the function of an amino acid sequence, using our new homology modelingservice, Spanner (http://www.pdbj.org/spanner/). Alternatively, Spanner can build models
from the results produced by the sequence-structure multiple-alignment system, MAFFTash(http://www.pdbj.org/ MAFFTash.3/), as well as several other external programs for sequencealignment and threading. The resulting 3D model is then used as an input template structureof SeSAW[2] (http://www.pdbj.org/ SeSAW/). SeSAW is based on sequence-weighted
structure alignments to protein folds, and uses sequence profiles for both the template and thequery to weight the structurally aligned residue pairs. The combination of sequence profiles
and structure alignments makes it possible to reliably detect functional similarities while
dealing with very distant homology. GIRAF[3] (http://giraf.pdbj.org/) is an efficient searchmethod for atomic alignments of possible ligand binding sites and protein-protein interfaces.
It is not constrained by sequence homology, sequence order or protein fold, and hence isapplicable to the cases where no structural homologs can be found.
Both SeSAW and GIRAF have been used to annotate structural genomics targets withunknown functions[2]. The most functionally similar proteins are often found not to be themost structurally similar ones, which highlights the importance of incorporating evolutionary
information via sequence profiles. They were also used to predict the function of a new andessential protein sequence, which was later experimentally confirmed[4].
References[1] Standley, D. M. et al. Brief. Bioinf. 9, 276-285 (2008),[2] Standley, D. M. et al., PROTEINS 72, 1333-1351 (2008),[3] Kinjo, A. R. & Nakamura, H. Structure 17, 234-246 (2009),[4] Matsushita, K. et al., Nature 458, 1185-1190 (2009)- 125 -

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Poster

Structural insights into a pyridoxal 5’-phosphatedependent fold-typeⅠ racemase, α-amino-εcaprolactam racemase from Achromobacter obae

P-41

Seiji Okazakia,b, Atsuo Suzukia, Koji Suzukia, Hidenobu Komedac, Yasuhisa
Asanoc, Takashi Yamane *aaDepartment of Biotechnology, Graduate School of Engineering, Nagoya University,
Nagoya 464-8603, Japan (yamane@nubio.nagoya-u.ac.jp)
bPresent address: Structural Biology Research Center, Photon Factory, Institute ofMaterials Structure Science, High Energy Accelerator Research Organization (KEK),
Tsukuba 305-0801, Japan (okazakis@post.kek.jp)
cDepartment of Biotechnology, Faculty of Engineering, Toyama Prefectural University,
Toyama 939-0398, Japan (asano@pu-toyama.ac.jp)

α-Amino-ε-caprolactam (ACL) racemase (ACLR, EC 5.1.1.15) is a 51 kDa enzyme thatcatalyzes the interconversion of L- and D-ACL. Recently, amino acid amide racemizing
activity was found in ACLR [1], and the combined method of ACLR with D-stereospecificamino acid amidase has been developed for D-amino acid production from D, L-amino acidamide [2]. To clarify the structure-function relationships of ACLR, the crystal structures of thenative and ε-caprolactam complex of ACLR were determined at 2.3 and 2.4 Å resolutions,
respectively [3]. This is the first structural report of racemase which belongs to fold-typeⅠ.
The structure of ACLR is composed of three segments; (1) an N-terminal segment (residues 1
to 43), (2) a large, pyridoxal phosphate (PLP) binding domain (residues 44 to 319) and (3) aC-terminal domain (residues 320 to 436). The C4' in PLP covalently bonded to the ε-aminogroup of Lys267 forming the internal aldimine. The substrate-binding site is assigned between
Trp49 and Tyr137 by the location of ε-caprolactam in the complex structure. For identifying
the catalytically important residues, the energy-minimized model of the L-ACL-PLP external
aldimine intermediate was produced. The carboxyl group of Asp210 is a reasonable candidatethat recognizes the nitrogen atom of lactam or amide in the substrate. From structuralcomparison with fold-typeⅢ alanine racemase, Tyr137 of ACLR plausibly plays as acid/basecatalytic residue which is essential for two-base mechanism in racemization.
References
1.
2.
3.

Asano, Y. & Yamaguchi, S. (2005). J. Mol. Catal. B. Enzym. 36, 22-29.
Asano, Y. & Yamaguchi, S. (2005). J. Am. Chem. Soc. 127, 7696-7697.
Okazaki, S., Suzuki, A., Mizushima, T., Kawano, T., Komeda, H., Asano, Y. and Yamane, T. (2009).
Biochemistry 48, 941-950.

P-42

Fluorescence-Based Screening for Soluble Human
Proteins by POET in Baculovirus-infected Insect
Cells for Structural Studies
Songying Ouyang, Zhijie Liu
Institute of Biophysics, Chinese, 15 Datun Road, Chaoyang District, Beijing, 100101,
China (ouyangsy@moon.ibp.ac.cn)

Production of structure-grade soluble proteins in substantial quantities takes a critical role inprotein structure research. Unfortunately, this has been impeded because a variety of proteins- 126 -

AsCA’09

Posterwere found insoluble, unstable or can not be purified in bacterial expression system.
Baculovirus expression vector system is a eukaryotic expression system and thus uses manyof the protein modification, processing, and transport systems present in higher eukaryotic
cells and usually provide very high levels of foreign gene production. The baculovirus/insect
cell expression system is a very attractive and powerful tool for the production ofheterogeneous gene products, especially expression of recombinant eukaryotic proteins. This
article describes an improved pooled open reading frame (ORF) expression technology(POET) that uses recombinational cloning and Liquid Chromatography Tandem mass
spectrometry (LC/MS) to identify proteins that yield high levels of soluble, purified protein
expressed in insect cells. Twenty-two human gene ORFs/fragments were subcloned into
baculovirus expression vector and positive recombinant bacmids were constructed, purified,
and transfected into Sf9 insect cells. After bulk expression and purification, 2 proteins wereidentified as soluble protein with higher expression level. By using this improved POET
method described here allows the expression characteristics of proteins to be quickly
determined in only once experiment in baculovirus expression system.
Keywords: POET; baculovirus; soluble protein

Crystal Structure of the Periplasmic Region of MacB,a Noncanonic ABC Transporter

P-43

Sun-Hee Park, § Yongbin Xu,§ Se-Hoon Sim,# Ki Hyun Nam,^ Xiao Ling Jin,§
Hong-Man Kim,# Kwang Yeon Hwang,^ Kangseok Lee,# and Nam-Chul Ha§College of Pharmacy and Research Institute for Drug Development, Pusan National
University, Busan 609-735, Republic of Korea,#Department of Life Science, Chung-Ang University, Seoul 156-756, Republic of Korea,and ^Division of Biotechnology and Genetic
Engineering, College of Life and Environmental Sciences, Korea University, Seoul
136-791, Republic of Korea

MacB is a noncanonic ABC-type transporter within Gram-negative bacteria, which is
responsible both for the efflux of macrolide antibiotics and for the secretion of heat-stableenterotoxin II.
In Escherichia coli, MacB requires the membrane fusion protein MacA and themultifunctional outer membrane channel TolC to pump substrates to the external medium.
Sequence analysis of MacB suggested that MacB has a relatively large periplasmic region.
To gain insight into how MacB assembles with MacA and TolC, we determined the crystal
structure of the periplasmic region of Actinobacillus actinomycetemcomitans MacB.
Fold matching program reveals that parts of the MacB periplasmic region have structural
motifs in common with the RND-type transporter AcrB.
Since it behaved as a monomer in solution, our finding is consistent with the dimeric nature offull-length MacB, providing an insight into the assembly in the tripartite efflux pump.

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P-44

Poster

Structure of an eIF4A - PDCD4 complex provides
insight into the inhibition of translation
Young Bong Park, Jihye Lee, Jeong Ho Chang and Yunje Cho
National Creative Initiatives for Structural Biology and Department of Life Science,
Pohang University of Science and Technology, Hyo-ja dong, San31, Pohang,
KyungBook, South Korea (yunje@postech.ac.kr)

Tumor suppressor programmed cell death protein 4 (PDCD4) inhibits the translation initiation
factor eIF4A, an RNA helicase that catalyzes the unwinding of secondary structure at the 5’
untranslated region (5’ UTR) of mRNAs, and controls the initiation of translation. Here we
determined the crystal structure of the human eIF4A and PDCD4 complex. The structure
reveals that one molecule of PDCD4 binds to the two eIF4A molecules through the twodifferent binding modes. While the two MA3 domains of PDCD4 bind to one eIF4A molecule,only the C-terminal MA3 (cMA3) domain of the same PDCD4 interacts with another eIF4A
molecule. The eIF4A-PDCD4 complex structure suggests that the MA3 domain(s) of PDCD4
binds perpendicular to the interface of the two domains of eIF4A, preventing the domain
closure of eIF4A and blocking the binding of RNA to eIF4A, both of which are required
events in the function of eIF4A helicase. The structure, together with biochemical analyses,
reveals insights into the inhibition mechanism of eIF4A by PDCD4, and provides aframework for designing chemicals that target eIF4A.

P-45

Crystal Structure of Bacterial Lysozyme Inhibitor
MliC, Complexed with c-type Lysozyme
Shunfu Piao, Soohwan Yum and Nam-Chul Ha
College of Pharmacy and Research Institute for Drug Development, Pusan National
University, Room #311, Pharmacy Building, Jangjeon-dong Geumjeong-gu, Busan609-735, Republic of Korea (hnc@pusan.ac.kr)

Lysozymes are an important component of the innate immune system of animals thathydrolyze peptidoglycan, the major bacterial cell wall constituent. Many bacteria havecontrived various means of dealing with this bactericidal enzyme, one of which is to produce
lysozyme inhibitors. Recently, a novel family of bacterial lysozyme inhibitors was identified
in various Gram-negative bacteria, named MliC (membrane bound lysozyme inhibitor of
C-type lysozyme). Here, we report the crystal structure of Pseudomonas aeruginosa MliC incomplex with chicken egg white lysozyme. Combined with mutational study, the complex
structure demonstrates that the invariant loop of MliC plays a crucial role in the inhibition of
the lysozyme by its insertion to the active site cleft of the lysozyme, where the loop forms
hydrogen and ionic bonds with the catalytic residues. Since MliC family members have been
implicated as putative colonization or virulence factors, the structures and mechanism ofaction of MliC will be of relevance to the control of bacterial growth in animal hosts.

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AsCA’09

Poster

Structural Basis of Transport of Lysophospholipids
by Human Serum Albumin

P-46

Shihui Guo1,2, Xiaoli Shi1,2, Mingdong Huang1,2
1. State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the
Structure of Matter, The Chinese Academy of Sciences, 155 Yang Qiao Xi Lu, Fuzhou,
Fujian, 350002, China (sxl_sharly@fjirsm.ac.cn)
2. Graduate School of Chinese Academy of Sciences, The Chinese Academy of Sciences,
Beijing 10039, China

Lysophospholipids play important roles in cellular signal transduction, and are implicated inmany biological processes, including tumorigenesis, angiogenesis, immunity, atherosclerosis,
arteriosclerosis, cancer, and neuronal survival. The intracellular transport oflysophospholipids is through fatty acid binding protein. Lysophospholipids are also found in
extra cellular space. However, the transport mechanism of lysophospholipids in extracellularspace is unknown. Human serum albumin (HSA) is the most abundant carrier protein in bloodplasma and plays important role in determining the absorption, distribution, metabolism, andexcretion of drugs. In this study, lysophosphatidylethanolamine (LPE) was used as the ligand
for analysis of the interaction of lysophospholipids with HSA by fluorescence quenching andcrystallography. Fluorescence measurement showed that LPE binds to HSA with adissociation constant (Kd) of 5.6 μM. The presence of fatty acid (myristate) reduces thisbinding affinity (Kd of 12.9 μM). Despite the relatively large size of this lysophospholipid, thebinding affinity between LPE and HSA is comparable to that of fatty acid. Moreover, we determinedthe crystal structure of HSA in complex with both a fatty acid (myristate) and LPE, andshowed that LPE binds at Sudlow site1 located in subdomain IIA. LPE occupies two of threesubsites in Sudlow site 1 with the LPE acyl chain occupying the hydrophobic bottom of Sudlow site 1
and the polar head group located at Sudlow site 1 entrance region pointing to solvent. Thisorientation of LPE in HSA suggests HSA is capable to accommodate other lysophospholipids andphospholipids. This study provides structural information on HSA-lysophospholipids

interaction and may facilitate the understanding of the transport and distribution oflysophospholipids.

P-47

Inactivation of Nucleoside Diphosphate Kinase-A
through a Conformational Change of the C-terminal
Loop Induced by Oxidation
Mi-Sun Kim, Dong-Hae Shin
Department of Pharmacy, Division of Life and Pharmaceutical Sciences, Ewha Womans
University, Seoul, Korea 120-750 (dhshin55@ewha.ac.kr)

Nucleoside diphosphate kinase (NDK) catalyzes the transfer of the γ-phosphoryl group from anucleoside triphosphate (NTP) to a nucleoside diphosphate (NDP) by using ATP as a major
phosphate donor through a conserved histidine residue. NDP kinases play a primary role not
only in maintaining cellular pools of all NTPs but also in the regulation of important cellular
processes. NDK-A (NM23-H1) acts as a metastasis suppressor for some tumor types. The
oxidation of NDK-A with 5 mM H2O2 for 1 hour nullify enzyme activity. We present here thecrystal structure of oxidized human NDK-A determined at 2.8 Å resolution. The crystals- 129 -

AsCA’09

Posterbelong to the cubic space group P213 with cell parameters a = b = c = 106.77 Å and theasymmetric unit contains a dimer. The overall structure is a hexamer, which can be viewed asa trimer of three dimers in this oxidation form. In the native form, Cys145 locates on theequatorial surface of the hexamer and is close to a neighboring Cys145 from another subunit.
However in the oxidation form, Cys145 makes a disulfide bridge with Cys4. This disulfide
bridge induces a large conformational change of C-terminal domain, which may result ininactivation of NDK-A. Here we also describe the enzyme activation and inactivation
mechanism based on the crystal structures.

P-48

Crystal Structure of Stenotrophomonas maltophilia
FeoA complexed with Zinc: A Unique Procaryotic SH3
Domain-like Protein Possibly Acts as a Bacterial
Ferrous Iron Transport Activating Factor
Yi-Che Su1, Ko-Hsin Chin1, Andrew H.-J. Wang2 & Shan-Ho Chou1, 31Institute of Biochemistry, National Chung-Hsing University, Taichung, 40227, Taiwan
2
Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan
3
National Chung Hsing University Biotechnology Center, Taichung, 40227, Taiwan,(shchou@nchu.edu.tw)

Iron is vital to the majority of prokaryotes, which, have therefore developed a variety of irontransport pathways to compete with the host for their iron supplies. The most common
pathways employed by bacteria appear to be those that transport ferric complexes, such as
ferric-siderophores, ferric-transferrin, ferric-citrate etc. However, ferrous iron is believed to be
the preferred form for iron uptake due to its much better solubility (0.1 M for Fe2+ vs. 10-18 M
for Fe3+ at pH 7). Interestingly, the major route for bacterial ferrous iron uptake was found tobe via a Feo (Ferrous iron transport) system that differs considerably from the ferric irontransport systems. Surprisingly, relatively little research was done on this important and novel
system. Nevertheless, the Feo system is now known to comprise three genes, which likely
form an operon of feoABC: FeoA is a small protein of approximately 75 residues withunknown function; FeoB is a large protein of 773 residues with an integral membrane domain
and is likely to act as a ferrous permease; and FeoC is another small protein containing a Fe-Scluster and possibly serves as a transcriptional regulator for the feoABC operon.
Stenotrophomonas maltophilia (Sm) has emerged as an important opportunistic pathogen in
the immunodepressed hosts. Recently, it has been described as a “superbug” that can resist
any antibiotics, which has caused tremendous difficulty in treating its infections. However,structural study of proteins encoded by this bacterium is still scarce. Here we report thetertiary structure of SmFeoA determined to a resolution of 1.7 Å from a Selenium-Methionine
single-wavelength anomalous dispersion (Se-SAD) approach. It bears weak similarity to the
C-terminal SH3 domain of bacterial DtxR (diphtheria toxin regulator protein) and
Iron-dependent regulator (IdeR). Although no clear sequence identity with eukaryotic
SH3-domain proteins can be found, the final structure of SmFeoA is indeed found to adopt a
SH3-domain fold similar to those of the eukaryotic proteins. Since eukaryotic SH3-domain iswell known for its capability to mediate protein-protein interactions, this has led to thesuggestion that FeoA may interact with FeoB to regulate the FeoB-dependent ferrous iron
- 130 -

AsCA’09

Posteruptake activity. In the current SmFeoA, it was found to adopt a unique dimer cross-linked by
two zinc ions coordinated by an aspartate residue, a histidine residue, and two chloride ions.
Since FeoB was found to contain a G-protein like domain, there is thus a possibility that FeoA
may interact with FeoB through the G-protein/SH3 domain interaction, with FeoA possibly
acting as a ferrous ion transport activating factor.

P-49

Single-stranded DNA-binding protein complex from
Helicobacter pylori suggests an ssDNA-binding
surface
Yuh-Ju Sun and Kun-Wei Chan
Institute of Bioinformatics and Structural Biology and 2Institute of Biotechnology
National Tsing Hua University, Hsinchu 300, Taiwan (yjsun@life.nthu.edu.tw)

Single-stranded DNA-binding protein (SSB) plays an important role in DNA replication,
recombination, and repair. SSB consists of an N-terminal single-stranded DNA-binding
domain with an oligonucleotide/oligosaccharide binding fold and a flexible C-terminal tailinvolved in protein-protein interactions. SSB from Helicobacter pylori (HpSSB) was isolated,
and the ssDNA-binding characteristics of HpSSB were analyzed by fluorescence titration andelectrophoretic mobility shift assay. Tryptophan fluorescence quenching was measured as61%, and the calculated cooperative affinity was 5.4 × 107 M–1 with an ssDNA binding lengthof 25-30 nucleotides. The crystal structure of the C-terminally truncated protein (HpSSBc) incomplex with 35-mer single-stranded DNA [HpSSBc-(dT)35] was determined at a resolutionof 2.3 Å. The HpSSBc monomer folds as an OB-fold with a Y-shaped conformation. The
ssDNA wrapped around the HpSSBc tetramer through a continuous binding path comprising
five essential aromatic residues and a positively charged surface formed by numerous basic
residues.

P-50

A novel pharmaceutical protein, crystal structures ofan anti-HIV actinohivin from an actinomycete, and its
complex with mannobiose
Masaru Tsunoda1, Kaoru Suzuki1, Tsubasa Sagara1, Atsushi Takahashi1, Junji
Inokoshi2, Satoshi Omura2, Takeshi Sekiguchi1, Haruo Tanaka1 and Akio Takénaka1
1
Iwaki-Meisei University, 5-5-1 Chuodai-Iino, Iwaki, 970-8551, Japan(atakenak@iwakimu.ac.jp)
2
Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo, 108-8641, Japan

Actionohivin (AH) has been isolated as a lectin from actinomycete Longispora albida
K97-0003T [1]. This protein inhibits HIV viral entry to human susceptive cells. As comparedwith cyanovirin-N, AH binds more specifically to the high mannose-type saccharide chains(HMTG) of HIV gp120 protein. AH is a small protein of 114 amino acid residues, being
arranged in a unique sequence repeated by three times tandemly. To reveal the structure of thespecific binding, X-ray analyses of the apo-form and its complex with mannobiose
Man1-α(1-2)-Man2 have been performed at 0.90 and 1.80 Å resolutions, respectively. In the
apo-form crystal, the protein structure is composed of the three modules similar to each other,- 131 -

AsCA’09

Posteras speculated from the tandem repeats in the sequence. Each module consists of a β-sheet offour β-strands, a long loop and a π-helix. The three modules are associated with a pseudo
three-fold symmetry, in which the three β-sheets form a triangular barrel. Inside of the barrel,hydrophobic residues form a stable core. On the outer surface, a long loop with a π-helix ineach module is running from the top to the bottom of the barrel. This loop and the preceding
two β-strands containing the carbohydrate-binding motifs LD-QXW form a valley with apocket for carbohydrate-binding. In the three sites of the complex-form, three mannobioses
are bound, respectively. In the first pocket of the module 1, the carboxyl group of Asp15
bridges between the two hydroxyl groups (OH3 and OH4) attached to the C3 and C4 atoms ofMan2, through hydrogen bonds. At the same time, OH3 forms another hydrogen bond withthe amide group of Asn28 and OH4 forms another hydrogen bond with the hydroxyl group of
Tyr23. In addition, the mannose ring of Man2 is sandwiched between Leu25 and Tyr32 byhydrophobic interactions. To stabilize the pocket formation, Gln33 forms double hydrogenbonds with the main chain amide group at Asn28 and the carbonyl group at Ala27. In thesecond and the third pockets, the mannobioses are also bound in the similar ways. The
structural features are completely consistent to the results of mutation experiments of theseamino acid residues. The Man1 group which is largely bent by the α(1-2) bond is protruded
into the solvent region. In this pocket, the mannobiose end of D1 branch of HMTG could beaccommodated in a way similar to the geometry described above, and the end of D2 or D3
branch might contact with a valley. Therefore, it is possible to speculate that each pocket
accepts the D1 and D2/D3 branches of HMTG. The three pockets are located to form analmost regular triangle at a distance of 17 Å between the pockets. This separation might bepossible to accept three HMTGs on a gp120 at the same time.
Reference
Tanaka H, Chiba H, Inokoshi J, Kuno A, Sugai T, Takahashi A, Ito Y, Tsunoda M, Suzuki K, Sekiguchi T,
Takenaka A, Umeyama H, Hirabayashi J, Omura S (2009) Action mechanism of the highly specific andpotent anti-HIV property of actinohivin, a microbial lectin with three sugar-binding pockets. PNAS 106, inpress.

The SARS-unique domain of SARS-CoV contains two
macrodomains that bind G-quadruplexes

P-51

Jinzhi Tan1, Clemens Vonrhein2, Oliver S. Smart2, Gerard Bricogne2, Michela
Bollati1,4, Yuri Kusov1, Guido Hansen1, Jeroen R. Mesters1, Christian L. Schmidt1,
Rolf Hilgenfeld1,31Institute of Biochemistry, Center for Structural and Cell Biology in Medicine,
University of Lübeck, Germany, (jztan@biochem.uni-luebeck.de)2
Global Phasing Ltd., Cambridge, UK, (gb10@globalphasing.com)
3
Laboratory for Structural Biology of Infection and Inflammation, c/o DESY, Hamburg,
Germany, (Hilgenfeld@biochem.uni-luebeck.de)4
on leave from Dept. of Biomolecular Sciences & Biotechnology, University of Milan,
Via Celoria, 26, 20133 Milano, Italy (michela.bollati@unimi.it)

The SARS coronavirus (SARS-CoV) is much more pathogenic for humans than any othercoronavirus. Therefore, protein domains encoded by the SARS-CoV genome that are absent
in other coronaviruses are of particular interest, because they may be responsible for the
extraordinary virulence. The most prominent such domain has been identified by- 132 -

AsCA’09

Posterbioinformatics as part of non-structural protein 3 (Nsp3) of the virus and appropriately named
the “SARS-unique domain” (SUD) [1]. Through the efforts of several laboratories around theworld, the structures of a number of non-structural proteins of the SARS coronavirus
replicase/transcriptase complex have been determined. However, the SUD has escaped all
attempts at crystallizing it because of its instability.
After construction of many fragments, we have managed to obtain the core of the SUD in a
crystalline form, and determined its X-ray structures at 2.2 and 2.8 Å resolution, respectively.
This revealed that SUDcore contains two copies of the so-called macrodomain. Furthermore,
we have shown that each of these, as well as the entire SUDcore and full-length SUD,
specifically bind to G-quadruplexes, both in the DNA and RNA form [2,3]. G-quadruplexes
occur in the 3’-nontranslated regions of mRNAs coding for several host-cell proteins involved
in apoptosis or signal transduction. By mutational studies, we could show that replacement ofpairs of lysine residues on the C-terminal subdomain of SUDcore abolished binding ofG-quadruplexes completely.
There is also a link to poly(ADP-ribose) polymerase (PARPs), as the structure of the SUD
subdomains show some distant similarity to the catalytic domain of these enzymes, and othermacrodomains have been shown to bind ADP-ribose (whereas SUD does not). Further,
PARP-1 also binds G-quadruplexes and PARP domains exist in the antiviral protein ZAP,
which is active against viruses containing a macrodomain (e.g. alphaviruses andcoronaviruses). We speculate that SARS-CoV could inactivate ZAP by competing with it for
G-quadruplex regions in RNA, suggesting a way for the SARS virus to fight the innate
immune system of the host cell.
References
1.
2.
3.

Snijder E.J., Bredenbeek P.J., Dobbe J.C., Thiel V., Ziebuhr J., Poon L.L.M, Guan Y., Rozanov M.,
Spaan W.J.M., Gorbalenya A.E. J. Mol. Biol., 331, 991-1004 (2003).
Tan J., Kusov Y., Mutschall D., Tech S., Nagarajan K., Hilgenfeld R., Schmidt C.L. Biochem. Biophys.
Res. Commun. 364, 877-882 (2007).
Tan J., Vonrhein C., Smart O.S., Bricogne G., Bollati M., Kusov Y., Hansen G., Mesters J.R., Schmidt
C.L., Hilgenfeld R. PLoS Path., 5, e1000428 (2009).

P-52

A crystallographic study of Tic110C protein from
Cyanidioschyzon merolae
Jia-Yin Tsai and Chwan-Den Hsiao
1
Institute of Molecular Biology, Academia Sinica. 128 Sec. 2, Academia Rd, Nankang,
Taipei 115, Taiwan, (jytsai@imb.sinica.edu.tw)

Tic110 (translocan of the inner envelope membrane) is an intergral membrane protein
containing a short N-terminal membrane anchor and a hydrophilic region (~98 kDa) that
extends into the plastid stroma. Here, the crystallization and preliminary analysis of the
C-terminal domain (659-1007) of Tic110 protein hydrophilic region from Cyanidioschyzon
merolae Tic110 (cmTic110C) are reported. The cmTic110C has been crystallized at 293 K
using PEG 400 as precipitant. The crystal structure has been determined by x-ray MAD
method. These crystals belong to the hexagonal space group P6522, with unit-cell parameters- 133 -

AsCA’09

Postera = b = 122.7, c = 243.2 Å. A 99.8% complete native data set from a frozen crystal has beencollected to 3.7 Å at 100 K with an overall Rmerge of 6.0%.

Crystal structure of the human FOXO3a-DBD/DNA
complex suggests the effects of post-translational
modification

P-53

Kuang-Lei Tsai1,2, Yuh-Ju Sun2, Cheng-Yang Huang1, Jer-Yen Yang3, Mien-Chie
Hung3 and Chwan-Deng Hsiao1,*1Institute of Molecular Biology, Academia Sinica, Taipei, 115, Taiwan(d948243@oz.nthu.edu.tw)
2Institute of Bioinformatics and Structural Biology, National Tsing Hua University,
Hsinchu, 300, Taiwan
3
Deaprtment of Molecular and Cellular Oncology, The University of Texas M. D.
Anderson Cancer Center, Houston, Texas 77030, USA

FOXO3a is a transcription factor of the FOXO family. The FOXO proteins participate inmultiple signaling pathways, and their transcriptional activity is regulated by several
post-translational mechanisms, including phosphorylation, acetylation, and ubiquitination.
Because these post-translational modification sites are located within the C-terminal basic
region of the FOXO DNA-binding domain, it is possible that these post-translational
modifications could alter the DNA-binding characteristics. To understand how
FOXO-mediated transcriptional activity, we report here the 2.7 Å crystal structure of the
DNA-binding domain of FOXO3a (FOXO3a-DBD) bound to a 13-bp DNA duplex containing
a FOXO consensus binding sequence (GTAAACA). Based on a unique structural feature in
the C-terminal region and results from biochemical and mutational studies, our studies may
explain how FOXO-DBD C-terminal phosphorylation by protein kinase B (PKB) or
acetylation by cAMP-response element binding protein (CBP) can attenuate the DNA-binding
activity and thereby reduce transcriptional activity of FOXO proteins. In addition, we
demonstrate that the methyl groups of specific thymine bases within the consensus sequence
are important for FOXO3a-DBD recognition of the consensus binding site.
References
1.
2.

FoxOs at the crossroads of cellular metabolism, differentiation, and transformation. Cell (2004)
117:421–426.
Crystal structure of the human FOXK1a–DNA complex and its implications on the diverse binding
specificity of winged helix/forkhead proteins. J. Biol. Chem. (2006) 281:17400–17409.

P-54

Novel crystal structure of Helicobacter pylori
neutrophil-activating protein (HP-NAP)
Osamu Tsuruta, Naoya Akao, Hideshi Yokoyama, Satoshi Fujii
University of Shizuoka , 52-1 Yada, Suruga-ku, Shizuoka-shi, Shizuoka-ken, 422-8526,
Japan (d09205@mail.u-shizuoka-ken.ac.jp)

Background Helicobacter pylori is a pathogen associated with gastric diseases, including
gastric ulcers and stomach cancers. Helicobacter pylori neutrophil-activating protein(HP-NAP) is a major 17 kDa antigen of H. pylori. This protein activates neutrophils and- 134 -

AsCA’09

Posterproduces reactive oxygen species. Thus, it is thought that HP-NAP is a cause of gastric cancer.
HP-NAP is a ferritin-like iron storage protein. Crystal structure of HP-NAP was solved in
2002 at 2.5 Å resolution (Giuseppe Zanotti et al.)1. According to the study, HP-NAP forms ahollow spherical dodecamer and contains 12 ferric ion binding sites in the dodecamer. In
order to understand the mechanism of iron uptake and elimination, we have determined thenovel crystal structure of HP-NAP. We obtained the metal-free crystal with different
amino-acid sequence. Moreover, because a new crystal is high symmetry and a highresolution, several structural bases of the accumulation of the metal will be able to beelucidated by the comparison with Zanotti's structure.
Method HP-NAP was expressed as a His-tag fused protein and crystallized using thehanging drop vapor diffusion method at 20 °C. To prevent the protein from aggregation, 0.1
M L-arginine was used during the purification and crystallization. Crystals were grown
against 500 μl of a reservoir solution containing 25% ethylene glycol. Crystallization drops
were prepared by mixing 2 μl of 8.3 mg ml-1 of protein solution in 50 mM Tris-HCl (pH 8.8)
and equal amount of the reservoir solution. A crystal (0.1 x 0.2 x 0.5 mm) was flash-frozen at-178 °C under a nitrogen-gas stream with the cryoprotectant solution containing 50% ethylene
glycol. X-ray diffraction data were collected at beam-line BL5A of the Photon Factory inJapan. Diffraction data integration, scaling, and merging were performed using HKL2000.
Structure determination and refinement were performed by the molecular replacement method
using MOLREP and REFMAC in the CCP4 package. Zanotti's structure was used as a searchmodel. Modeling was carried out with COOT.
Results and Discussion We determined the structure of HP-NAP at 2.2 Å resolution higher
than that of the Zanotti's one. The space group of our crystal was F432 and that of Zanotti's
one is P21. Thus, we have obtained the crystal that has higher symmetry and gives higher
resolution data. Additionally, our crystal has a high water content of 65.9% and does notcontain iron atom. By the comparison with Zanotti's structure, several new evidences
including the big structural changes of three amino-acid residues by the metal coordination
were obtained (His37, Asp52 and Glu56). There were two different pores formed at 3-foldrotational axes and metal ions may pass through each of them. To understand the iron uptake
and elimination mechanisms, more structural information such as mobility and charge
distribution will be elucidated. Due to its high water content, the new crystal is also suitable
for soaking experiment.

Structure of the HP-NAP dodecamer. It forms a sphere of
90 Å in diameter and has a large hollow space of 50 Å indiameter. Its inner surface is negatively charged and thus
HP-NAP is reported to accommodate up to 500 iron atoms
per dodecamer. To show the hollow structure, top andfront subunits are removed. One subunit is shown as aribbon diagram and the others are shown as a surface
representation view.

Reference
Giuseppe Zanotti, Elena Papinutto, William G. Dundon et al., Structure of the Neutrophil-activating Protein- 135 -

AsCA’09

Posterfrom Helicobacter pylori, J. Mol. Biol., 323, 125-130 (2002).

P-55

Structural and function researches on humanglutathione transferase kappa
Bing Wang, Yingjie Peng, Jianping Ding
Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences,
Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China(wangbing@sibs.ac.cn)

Glutathione transferases (GST) are a family of multifunctional proteins involved in thecellular detoxification of cytotoxic and genotoxic compound. The function of GST is toversatile and catalyze the nucleophilic addition of the thiol of reduced glutathione to a wide
variety of hydrophobic electrophiles. GST kappa is a unique class of this family for its
cellular localization and structure, which plays roles not only in detoxification but also indiabetes demonstrated recently.
We solved the structure of human GST kappa in apo form and the complex structure ofhGSTk and its inhibitor S-Hexylglutathione (GTX) at high resolution. The complex structureof hGSTk and its inhibitor may imply some hints for anti-cancer drug design. Compared withthe complex structure of hGSTk and GSF, the loop consisted of 52-62 residues changed its
conformation and formed an α-helix to interact with GSH directly. This result could be
confirmed by steady state kinetics parameters for hGSTk.
References
1.
2.
3.
4.

Morel, F., Rauch, C., Petit, E., Piton, A., Theret, N., Coles, B., and Guillouzo, A. (2004) Gene andprotein characterization of the human glutathione S-transferase kappa and evidence for a peroxisomal
localization. J Biol Chem. 279(16):16246-53.
Jane E. Ladner, James F. Parsons, Chris L. Rife, Gary L. Gilliland, and Richard N. Armstrong. (2004)
Parallel Evolutionary Pathways for Glutathione Transferases: Structure and Mechanism of the
Mitochondrial Class Kappa Enzyme rGSTK1-1. Biochemistry. 43 (2): 352-361
Li, J., Xia, Z., and Ding, J. (2005) Thioredoxin-like domain of human k class glutathione transferase
reveals sequence homology and structure similarity to the y class enzyme. Protein Science.
14:2361–2369
Liu, M., Zhou, L., Xu, A., Lam, K.S., Wetzel, M.D., Xiang, R., Zhang, J., Xin, X., Dong, LQ., and Liu,
F. (2008) A disulfide-bond A oxidoreductase-like protein (DsbA-L) regulates adiponectin
multimerization. Proc Natl Acad Sci U S A. 105(47):18302-7.

P-56

HCV Membrane Protein Purification, Characterization
and Crystallization
Liping Wang, Randy Bledsoe, William Burkhart, Annie Hassell, Robert Reid, Derek
Parks, Warren Rocque, Michael Thomson, Shawn Williams
GlaxoSmithKline, 5 Moore Drive, RTP, NC 27709, USA (liping.8.wang@gsk.com)

Although almost half of drug discovery targets are membrane proteins, crystallography
support on these projects is rare. Historically, the difficulty expressing, purifying active
protein, and obtaining structures required a long time span that was incompatible with drug
discovery. Because of the increasing number of membrane protein structures, including some- 136 -

AsCA’09

Posterat high resolution, we started to explore the crystallization of a HCV membrane protein at
GSK. The protein purification, biochemical and biophysical characterization and protein
crystallization efforts will be described and discussed.

An Intramolecular Self-Activation Mechanism of
Human Caspase-6

P-57

Xiao-Jun Wang1, Xiang Liu1, Kai-Tuo Wang1, Wei Mi1, Yan Zhang2, Lan-Fen Li1,
Andrea C. LeBlanc3, Xiao-Dong Su 1,41National Laboratory of Protein Engineering and Plant Genetic Engineering and2
College of Life Science, Peking University, Beijing 100871, People’s Republic of China
3
Department of Neurology and Neurosurgery, McGill University, Lady Davis Institutefor Medical Research, 3755 Ch. Côte Ste-Catherine, Montreal, Quebec, Canada
4
Peking University Shenzhen Graduate School, Shenzhen 518055, People’s Republic of
China

Caspases represent a family of cysteinyl proteases involved in inflammation and apoptosis.
The short pro-domain effector Caspase-6 (Casp6) is activated early in cognitive impairment
and in Alzheimer disease (AD), and is associated with neurodegeneration and axonal pruning.
To understand the mechanism of Casp6 activation, we have determined the crystal structuresof catalytically inactive Casp6 lacking its pro-domain (∆pro-Casp6C163A) and
Ac-VEID-CHO inhibited active Casp6.
The ∆pro-Casp6C163A structure shows
unexpectedly that the intersubunit linker cleavage site 190TEVD193 fits well into the active site
as a β strand, and the D193 is positioned readily to be attacked by the nucleophile C163. We
have confirmed biochemically that this intra-molecule-cleavage is a prerequisite condition for
casp6 self activation and further demonstrated that this unique intramolecular cleavage isdependent on the length of the L2 loop since deletion of only 4 amino acid residues from thelinker or substitution of the Casp6 linker by the shorter Casp3 linker is sufficient to abolishself-cleavage. These results show that unlike other effector caspases, which are activatedthrough exo-caspase proteolytic processing, Casp6 can activate by intramolecular
self-cleavage.

Redesign of a non-specific endonuclease to yield
better DNA-binding activity and altered DNA
sequence cleavage preference

P-58

Yi-Ting Wang1,2,3, Jon D. Wright4, Lyudmila G. Doudeva1, Hua-Ci Jhang1, Carmay
Lim4 and Hanna S. Yuan1,2
1
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan
2 Institute of Chemical Biology and Molecular Biophysics, Taiwan International
Graduate Program, Academia Sinica
3 Institute of Bioinformatics and Structural Biology, National Tsing Hua University
4 Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan

It is of crucial importance to elucidate the underlying principles that govern the binding
affinity and selectivity between proteins and DNA. Here we use the nuclease domain of
Colicin E7 (nColE7) as a model system to generate redesigned nucleases with improved
DNA-binding affinities and altered sequence cleavage preferences. ColE7 is an Escherichia- 137 -

AsCA’09

Postercoli toxin, bearing a nonspecific endonuclease domain with a preference for hydrolyzing
DNA phosphodiester bonds at the 3’ O-side after thymine.
Using systematic computational screening, six nColE7 mutants were predicted to fold andbind DNA. Fluorescence kinetic assays confirmed that all of the six designed mutants were
well-folded active enzymes, and three of the six mutants, D493N, D493Q and K497R, had 3
to 5-fold higher DNA binding affinity than wild-type nColE7. Footprint assays further showedthat D493N and D493Q digested DNA with an increased preference for guanine at -1 and +3
sites, as compared to the wild-type enzyme. To elucidate the observed higher DNA-binding
affinity and altered sequence preference in cleavage, the crystal structure of the nColE7
mutant, D493Q, in complex with an 18-bp DNA was determined, and free energy
decomposition calculations were performed. In summary, these results show that a
combination of crystal structural analysis and computational screening is a useful means forgenerating redesigned nucleases with higher DNA-binding affinities and altered sequence
preferences in DNA cleavage.

P-59

Trapping of Silica Nanoparticles at the Air-Water
Interface by Proteins
Joo Chuan Ang, Jhih-Min Lin, Peter N. Yaron and John W. White*
Research School of Chemistry, Australian National University, Canberra 0200,
Australia

We have observed the formation of protein-nanoparticle complexes at the air-water interface
from three different methods of presenting the nanoparticles to proteins. The structures
formed resemble the “protein-nanoparticle corona” proposed by Lynch et al.1,2 in relation to apossible route for nanoparticle entry into living cells. To do this the methods of X-ray andneutron reflectivity (with isotopic contrast variation between the protein and nanoparticles)
have been used to study the structures formed at the air-water interface of β casein presented
to silica nanoparticle dispersions. Whilst the silica dispersions showed no observablereflectivity, strong signals appear in the reflectivity when protein is present. Drop-wise
spreading of a small amount of protein at the air-silica sol interface and presentation of thesilica sol to an isolated monomolecular protein film (made by the “flow-trough”3 method)
give an immediate signal. Mixing the components in solution only produces a slow response
but in all cases a similar structure is formed. The different responses are interpreted instructural and stoichiometric ways.
References
1.
2.
3.
4.

Lynch, I et al. The nanoparticle-protein complex as a biological entity: a complex fluids and surface
challenge for the 21st century. Adv in Colloid and Interface Science 2007, 134-135, 167-174
Adam W. Perriman, Duncan J. McGillivray and John W. White. Reactions of Isolated Mono-MolecularProtein Films. Soft Matter, 2008, 4, 2192 - 2198
John. W. White*, Adam. W. Perriman, Duncan. J. McGillivray and Jin-Minh Lin -Protein Interfacial
Structure and Nanotoxicology, Nuclear Instruments and Methods in Physics Research A600 (2009)263-265ntegrated Research into the nanoparticle- protein corona: a new focus for safe, sustainable andequitable development of nanomedicines T.A.Faunce, J.W.White and K. Matthaei , Nanomedicine(2008), 3(6) 859-866- 138 -

AsCA’09
5.

PosterPerriman, A. W., Henderson, M. J., Holt, S. A., White, J. W. – Effect of the Air–Water Interface on the
Stability of beta–Lactoglobulin. The Journal of Physical Chemistry. B (2007), 111(48): pp. 13527–37.

Crystal structure of Helicobacter pylori urease
accessory protein ureF

P-60

Yu Hang Fong1, Yu Wai Chen2, Kam Bo Wong1
1
Department of Biochemistry, The Chinese University of Hong Kong, Shatin, HongKong.(kbwong@cuhk.edu.hk)
2
Randall Division of Cell and Molecular Biophysics, King's College London, London
WC2R 2LS, United Kingdom. (yu-wai.chen@kcl.ac.uk)

Urease is a nickel containing metalloenzyme that catalyses the conversion of urea into
ammonia and carbon dioxide. Its activity is thought to be essential for the survival of
Helicobacter pylori in the acidic environment in the stomach of the human host. UreF is oneof the molecular chaperons involved in metallocenter assembly and activation of urease.
Various roles have been proposed for ureF in the urease activation process. However, theexact function of ureF remained elusive. In our effort to elucidate the mechanism of urease
activation, we have determined the crystal structure of ureF in H. pylori. Crystals of ureF
were grown overnight in 24-28% PEG MME 5000 and 0.1M Bis-Tris pH 7.0. Diffraction data
were collected on beamline I-04 at the Diamond Light Source. Crystal structure was phasedwith MAD and solved using PHENIX AutoSol to 2.0?. It was then followed by iterative
cycles of model building and refinement with PHENIX.refine. The final crystal structure has a
Rfree of 0.232 and Rwork of 0.191. Analysis of the crystal structure revealed that it belongs to
C2 space group, with 3 asymmetric units per unit cell and cell dimenions of a = 135.16, b =89.04, c =65.99. Our model of ureF consists of residue 25 to 233, forming a total of 9 alphahelices. UreF exists as a dimer in the crystal structure with a buried surface area of ~1600A,
which corresponds to roughly 15% of the total surface area. Based on the structure, potentialfunctional implications of ureF were discussed.

Structural and function researches on two
α-isopropylmalate synthases from Leptospira biflexa,
key enzymes in leucine biosynthesis

P-61

Jian Wu1, Zilong Zhang2, Wei Lin2, Jun Ma2, Peng Zhang1, Guoping Zhao2,
Jianping Ding1
1
Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences,
Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China(wujian@sibs.ac.cn)
2Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences,
Chinese Academy of Sciences, 300 Feng-Lin Road, Shanghai 200032, China

Leptospirosis, a spirochetal zoonosis and mainly caused by Leptospira interrogans, is a
globally re-emerging infectious disease that has disseminated from its habitual rural base to
become the cause of urban epidemics in poor communities of industrialized and developing
nations. Leptospirosis has been recognized as a notifiable infectious disease in China since1955. The trend of this disease has been steady for recent years but outbreaks occasionallyoccurred, especially in several southern provinces of China and potential risk factors may- 139 -

AsCA’09

Posterexist in these areas. Similar with other micro-organisms, Leptospira biflexa, highly
homologous to pathogenic L. interrogans, employs an IPM pathway to synthesize leucine and
LbIPMSs (L. biflexa α-isopropylmalate synthases) catalyze the pivotal reaction of thispathway, which converts α-kiv (α-ketoisovalerate) and acetyl-CoA into α-ipm(α-isopropylmalate), thus making it an attractive target for the development of antibacterial
agents. Two IPMS genes are expressed in Leptospira, one product is IPMS1 composed of
catalytic-, sub1-, sub2-, and regulatory domains, and the other is IPMS2 containing the three
former domains. We report here the crystal structure of the catalytic domain of IPMS2 and thecomplex structures of full-length IPMS2 with bound Zn2+ and α-kiv or α-ipm. The catalytic
domain consists of an (α/β)8 TIM barrel flanked by sub1 domain, and the sub2 domain are
mainly composed of three α-helixes. IPMS2 forms a homodimer and the active site is locatedat the centre of the TIM barrel near the C-terminal ends of the β-strands. Sequence alignments
and biochemical data indicate that IPMS1 and IPMS2 share high similarity with each otherand both prefer acetyl-CoA substrate, however, the kinetic and mutagenesis studies show that
IPMS2 possesses relative low enzymatic activity but high specificity on α-kiv substrate, while
IPMS1 have the opposite features, consistent with the results from the structural comparisonsand analyses.
References
1.
2.
3.
4.
5.

Vinetz, J. M. (2001) Leptospirosis. Curr. Opin. Infect. Dis. 14, 527–538
Bharti, A. R., Nally, J. E., Ricaldi, J. N., Matthias, M. A., Diaz, M. M., Lovett, M. A., Levett, P. N.,
Gilman, R. H., Willig, M. R., Gotuzzo, E. et al. (2003) Leptospirosis: a zoonotic disease of global
importance. Lancet Infect. Dis. 3, 757–771
Koon, N., Squire, C. J. and Baker, E. N. (2004) Crystal structure of LeuA from Mycobacterium
tuberculosis, a key enzyme in leucine biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 101, 8295–8300
Ma, J., Zhang, P., Zhang, Z., Zha, M., Xu, H., Zhao, G. and Ding, J. (2008) Molecular basis of thesubstrate specificity and the catalytic mechanism of citramalate synthase from Leptospira interrogans.
Biochem. J. 414, 45–56
Zhang, P., Ma, J., Zhang, Z., Zha, M., Xu, H., Zhao, G. and Ding, J. (2009) Molecular basis of theinhibitor selectivity and insights into the feedback inhibition mechanism of citramalate synthase from
Leptospira interrogans. Biochem. J. 421, 133–143

Structural basis for a Reciprocating Mechanism ofNegative Cooperativity in Dimeric Phosphagen
kinase Activity

P-62

Xiaoai Wu1, Sheng Ye2, Shuyuan Guo3, Wupeng Yan1, Mark Bartlam4 and Zihe
Rao1,4,5
1
Laboratory of Structural Biology, School of Medicine,Tsinghua University, Beijing,
China (wuxa@xtal.tsinghua.edu.cn)
2
Department of Biochemistry and Molecular Biophysics, Columbia University, andHoward Hughes Medical Institute, New York, NY, USA
3
School of Life Science & Technology, Beijing Institute of Technology, Beijing, China
4
College of Life Sciences & Tianjin Key Laboratory of Protein Science, Nankai
University, Tianjin, China
5
National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of
Sciences, Beijing, China (raozh@nankai.edu.cn)

Phosphagen kinase (PK) family members catalyze the reversible phosphoryl transfer between
phosphagen and ADP to reserve or release energy in cell energy metabolism. The structures of- 140 -

AsCA’09

Posterclassic quaternary complexes of dimeric creatine kinase (CK) revealed asymmetric ligand
binding states of two protomers, but the significance and mechanism remain unclear. In orderto further understand this negative cooperativity, we determined the first structure of dimericarginine kinase (dAK), another PK family member, at 1.75 Å, as well as the structure of its
ternary complex with AMPPNP and arginine. Further structural analysis shows that theligand-free protomer in a ligand-bound dimer is opened more widely than the protomers in aligand-free dimer, leading to three different states of a dAK protomer. The unexpected
allostery of the ligand-free protomer in a ligand-bound dimer should be relayed from theligand-binding-induced allostery of its adjacent protomer. Mutations that weaken theinter-protomer connections dramatically reduced the catalytic activities of dAK, indicating theimportance of the allosteric propagation mediated by the homodimer interface. These results
suggest a reciprocating mechanism of dimeric PK, which is shared by other ATP related
oligomeric enzymes, e.g. ATP synthase.
Keywords: crystal structure, arginine kinase, creatine kinase, energy metabolism

Structural and Kinetic Analysis of Raucaffricine
Glucosidase (RG) from the Medicinal Plant Rauvolfia

P-63

Liqun Xia1,2*, Martin Ruppert2, Meitian Wang2, Santosh Panjikar4, Joachim
Stöckigt1,2*
1
Institute of Materia Medica, College of Pharmaceutical Sciences, Zhejiang University,
388 Yu Hang Tang Road, Hangzhou, Zhejiang Province, 310058, P.R. China(joesto2000@yahoo.com)
2
Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes
Gutenberg-University Mainz, Staudinger Weg 5, D-55099 Mainz, Germany
3
Swiss Light Source PX III, Paul Scherrer Institute, CH-5232 Villigen, Switzerland
4
European Molecular Biology Laboratory, Hamburg Outstation Deutsches
Elektronen-Synchrotron, Notkestrasse 85, D-22603 Hamburg, Germany

Raucaffricine-O-β-D-glucosidase (RG) is an enzyme that takes part in the biosynthesis ofmonoterpenoid indole alkaloids from the medical plant Rauvolfia serpentina (L.) Benth. Ex
Kurz. Based on initial sequence alignment studies, RG belongs unequivocally to the glycosylhydrolase (GH) family 1. The sequence identity was up to 55% compared to strictosidine
glucosidase (SG) which represents the gateway to the biosynthesis of the mentioned indole
alkaloid family.The family consists of about 2000 members. The best substrate forrecombinant RG was raucaffricine (KM 0.85 mM, Vmax 20.37 μM/min).The glucosides
secologanin and strictosidine at the beginning of ajmaline biosynthesis pathway were alsohydrolyzed in contrast to SG, which accepts exclusively its natural substrate strictosidine.
Site-directed mutagenesis of RG’s functional residue Glu-186 to a Gln residue resultsin >99% loss of enzyme activity. Crystals of RG and its complexes of inactive mutant
Glu186Gln (with secologanin and strictosidine, respectively) were obtained and survived
X-ray measurements at room temperature. Complete data sets were collected to less than
2.5Å.Detailed three-dimensional information describing both, native RG and complexes ofinactive mutant of RG, thus providing additional structural characterization andidentification of the amino acids that occupy the active site surface of the enzyme. Structural
analysis and site-directed mutagenesis experiments demonstrate the essential role of Glu-186- 141 -

AsCA’09

Posterin catalysis. The data presented here will contribute to deciphering the structure-related
substrate specificity and might allow a future structure-based rational re-engineering of
substrate acceptance of the enzyme.

Structure and Functional Implications of the Human
Rad9-Hus1-Rad1 Cell Cycle Checkpoint Complex

P-64

Min Xu, Lin Bai, Yong Gong, Wei Xie, Haiying Hang, Tao Jiang
Institute of Biophysics, Chinese, 15 Datun Road, Chaoyang District, Beijing, 100101,
China (tjiang@ibp.ac.cn)

Cellular DNA lesions are efficiently countered by DNA repair in conjunction with delays incell-cycle progression. Previous studies have demonstrated that Rad9, Hus1, and Rad1 canform a heterotrimeric complex (the 9-1-1 complex) that plays dual roles in cell cycle
checkpoint activation and DNA repair in eukaryotic cells. Although the 9-1-1 complex has
been proposed to form a toroidal structure similar to proliferating cell nuclear antigen(PCNA), which plays essential roles in DNA replication and repair, the structural basis bywhich it performs different functions has not been elucidated. Here we report the crystal
structure of the human 9-1-1 complex at 3.2Å resolution. The crystal structure, together withbiochemical assays, reveals that the interdomain connecting (IDC) loops of hRad9, hHus1,
and hRad1 are largely divergent, and further cocrystallization study indicates that a PIP-box
containing peptide derived from hFen1 binds tightly to the IDC loop of hRad1, providing themolecular basis for the damage-repair-specific activity of the 9-1-1 complex in contrast to
PCNA. Furthermore, structural comparison with PCNA reveals other unique structuralfeatures of the 9-1-1 complex that are proposed to contribute to DNA damage recognition.
Here we propose a damage sensing model. In this model, the clamp loader Rad17-RFC2-5
forms an ATP-dependent complex with the 9-1-1 sliding clamp in which Rad17 interacts with
Rad1, and loads the 9-1-1 complex onto DNA via opening the Rad1-Rad9 interface. Slidingof the clamp/clamp loader along DNA will stop when certain types of DNA lesions aredetected by some key residues inside the clamp. The detection of DNA lesions then leads toconformational changes that facilitate the ring closure and ATP hydrolysis, consequently
stimulate the dissociation of Rad17-RFC2-5 clamp loader from the 9-1-1 clamp, andultimately trigger further DNA repair. Collectively, our studies provide new insights into DNA
damage sensing and repair, which provides a starting point for further investigations anddevelopment of new anticancer agents.
βⅡ4
βⅡ3
βⅡ2
βⅡ6
βⅡ5
(not in hHus1)
βⅡ1
βⅡ7
βⅡ8
βⅡ9
βⅠ4
βⅠ3
βⅠ2
βⅠ6

NTD

CTD

αⅡ1

C

αⅡ2
αⅠ1
αⅠ2

βⅠ5
βⅠ1 N
βⅠ7
βⅠ8
βⅠ9
α3
(only in hHus1)

hHus1

CTD

NTD

hRad1

hRad9

NTD

CTD

Figure1. Overall structure of the 9-1-1 complex and DNA damage sensing model.
- 142 -

AsCA’09

Poster

References
1.
2.
3.
4.
5.
6.

Xu, M., Bai, L., Gong, Y., Xie, W., Hang, H., and Jiang, T. (2009) J. Biol. Chem. 284, 20457-20461
Sancar, A., Lindsey-Boltz, L. A., Unsal-Kacmaz, K., and Linn, S. (2004) Annu. Rev. Biochem. 73,
39-85
Lukas, J., Lukas, C., and Bartek, J. (2004) DNA Repair (Amst) 3, 997-1007
Bermudez, V. P., Lindsey-Boltz, L. A., Cesare, A. J., Maniwa, Y., Griffith, J. D., Hurwitz, J., andSancar, A. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 1633-1638
Zou, L., Cortez, D., and Elledge, S. J. (2002) Genes Dev. 16, 198-208
Rauen, M., Burtelow, M. A., Dufault, V. M., and Karnitz, L. M. (2000) J. Biol. Chem. 275,
29767-29771

In situ proteolysis doubles the success rate in protein
crystallization and structure determination

P-65

Xiaohui Xu¹·³, Aiping Dong², Hong Cui¹·³, Tatiana Skarina¹·³, Elena Evdokimova¹·³,
Aled Edwards¹ ² ³, Andrzej Joachimiak³, Alexei Savchenko¹·³
1.Ontario Center for Structure Proteomics, UHN, University of Toronto, 112 College
St. RM24, Toronto, Ontario, M5G 1L6 Canada (xxu@uhnres.utoronto.ca,
Alexei.savchenko@utoronto.ca)
2. The Structural Genomics Consortium (SGC), University of Toronto, 101 College St,
Suite 700.
Toronto, Ontario, M5G 1L7
Canada,(aled.edwards@utoronto.ca,
a.dong@utoronto.ca)
3.Midwest Center for Structural Genomic (MCSG), Argonne National Laboratory,9700
South Case Ave, Chicago, IL U.S.A (andrzejj@anl.gov)

Obtaining well-diffracting crystals remains the main bottle-neck in protein crystallography.
Analysis of large-scale structural genomics projects (http://targetdb.pdb.org) reports 13.5%
success rate in obtaining the structure quality crystals from a given set of purified proteins.
Thus vast majority of proteins submitted to conventional crystallization trials either do not
crystallize or form poor quality crystals, which can not be used for structure determination.
We present here a general rescue technique, named in situ proteolysis, allowing 15~20%
increase in successful crystallization.
Our method is based on observation that trace amounts of protease present in the protein
sample may lead to formation of hydrolyzed protein fragment prompt to crystallization. To
test if addition of protease can be used as general crystallization technique we selected 55
bacterial protein samples from the pool of Midwest Centre for Structural Genomics targets.
Of the 55 proteins, 20 had previously failed to crystallize and 35 had formed crystals thatwere unsuitable for structure determination. Addition of chymotrypsin protease to eachprotein sample prior crystallization trials (in 1:100 ratio) resulted in obtaining structure
quality crystals for eight proteins. The Trypsin and subtilisin protease addition to theremaining protein samples allowed obtaining three additional structures.
The analysis of eleven solved structures demonstrated that in every case the polypeptide chain
forming the crystal lattice was partially degraded by protease. The relative simplicity andsignificant increase in successful crystallization makes this method a prominent rescue
technique in protein crystallization. Apply this technique to large scale crystal screening thatcan dramatically improve the quality of crystal and double the success rate in structure
determination.
- 143 -

AsCA’09

Poster

A functional Assembly of a Tripartite acrolide-specificEfflux Pump

P-66

Yongbin Xu1, †, Hong-Man Kim2, Kangseok Lee2 and Nam-Chul Ha1.
1
College of Pharmacy and Research Institute for Drug Development, Pusan National
University, Busan 609-735, Korea (hnc@pusan.ac.kr)
2
Department of Life Science, Chung-Ang University, Seoul 156-756, Korea(kangseok@cau.ac.kr)

In Gram-negative bacteria, type I protein secretion systems and tripartite drug efflux pumps
have a periplasmic membrane fusion protein (MFP) as an essential component. MFPs bridge
the outer membrane factor and an inner membrane transporter, although the oligomeric stateof MFPs remains unclear. The most characterized MFP AcrA connects the outer membranefactor TolC and the resistance–nodulation–division-type efflux transporter AcrB, which is amajor multidrug efflux pump in Escherichia coli. MacA is the periplasmic MFP in the
MacAB–TolC pump, where MacB was characterized as a macrolide-specificATP-binding-cassette-type efflux transporter. Here, we report the crystal structure of E. coli
MacA and the experimentally phased map of Actinobacillus actinomycetemcomitans MacA,
which reveal a domain orientation of MacA different from that of AcrA. Notably, a hexamericassembly of MacA was found in both crystals, exhibiting a funnel-like structure with a central
channel and a conical mouth. The hexameric MacA assembly was further confirmed byelectron microscopy and functional studies in vitro and in vivo. The hexameric structure of
MacA provides insight into the oligomeric state in the functional complex of the drug efflux
pump and type I secretion system.

P-67

Homology Modeling of apo-CDK5 and Insights into
Structure-Based Inhibitor Design
Kosaraju Vamsi Krishna, Seow Yi Lim, Feng Xue
Department of Chemistry, National University of Singapore 3 Science Drive 3,
Singapore 117543 (chmxf@nus.edu.sg)

Cyclins and cyclin-dependent kinases (CDKs) play important roles in cell cycle regulation.
CDKs are a class of evolutionarily conserved serine/threonine protein kinases, each CDK
associates with a corresponding cyclin regulatory subunit to activate its phosphorylation
activity [1]. Unlike most human CDKs that involved in cell division, the post-mitotic CDK5
is a crucial regulator of neuronal migration during the development of the central nervous
system [2, 3]. Recent evidence indicates that deregulation of CDK5 is involved in thepathology of neurodegenerative diseases such as Parkinson’s disease or Alzheimer’s disease(AD), the leading cause of dementia and a increasing accelerated stochastically driven aging
process.
The crystal structure of CDK5-p25 complex unveiled a number of key facts related to theactivation and ligand binding [4]. However, CDK5 activation mechanism, which significantly
differs from typical CDK activation, is still unclear due to lack of the structure of inactive
CDK5 (apo-CDK5). We built a 3D model of apo-CDK5 based on the crystal structure of- 144 -

AsCA’09

Poster

apo-CDK2 (PDB: 1PW2) using homology modeling by spatial restraints implemented in
MODELLER. The model was refined by molecular mechanics and the stereochemical quality
was assessed by PROCHECK, ProsaII and Profiles-3D. Further molecular dynamic
simulation was applied to ensure the stability of the model. Molecular docking studies were
performed with known inhibitors to prove the suitability of the model for structure-based drug
design. Inactive kinases have been recognized to be another possible avenue to achieve
selectivity among kinase targets. Imatinib, a selective tyrosine kinase inhibitor, was docked
into the binding site of apo-CDK5 to evaluate the possibility of novel inhibitors.
Interestingly, the results showed that the inhibitor is capable of reaching the back floor of
apo-CDK5 binding site, as well as reveals additional hydrophobic pocket created by T-loop.

Targetinginactive kinase

References
1.
2.
3.
4.

Morgan, D.O., Cyclin-dependent kinases: engines, clocks, and microprocessors. Annu Rev Cell Dev
Biol, 1997. 13: p. 261-91.
Bibb, J.A., Role of Cdk5 in neuronal signaling, plasticity, and drug abuse. Neurosignals, 2003.
12(4-5): p. 191-9.
Paglini, G. and A. Caceres, The role of the Cdk5--p35 kinase in neuronal development. Eur J
Biochem, 2001. 268(6): p. 1528-33.
Tarricone, C., et al., Structure and regulation of the CDK5-p25(nck5a) complex. Mol Cell, 2001. 8(3):p. 657-69.

P-68

Xanthomonas campestris PqqD in the
Pyrroloquinoline Quinone Biosynthesis Operon
Adopts a Novel Saddle-Like Fold That Possibly
Serves as a PQQ Carrier
Chao-Yu Yang1, Tung-Yi Tsai1, Andrew H.-J. Wang2 & Shan-Ho Chou1, 31Institute of Biochemistry, National Chung-Hsing University, Taichung, 40227, Taiwan
2
Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan
3
National Chung Hsing University Biotechnology Center, Taichung, 40227, Taiwan,(shchou@nchu.edu.tw)

Pyrroloquinoline quinone (4,5-dihydro-4,5-dioxo-1H-pyrrolo-[2,3-f]quinoline- 2,7,9tricarboxylic acid, PQQ) is a novel heat-stable, water soluble redox cofactor present in avariety of bacterial alcohol and aldose dehydrogenases. It belongs to the third family ofortho-quinone cofactor following the well-known pyridine nucleotide- (such as NAD) andflavin-dependent (such as FAD) cofactors. Discovery of PQQ has elicited considerable
interests due to its role as a growth-promoting factor both in animals and plants. Although the- 145 -

AsCA’09

Posterstructures and functions of many enzymes using PQQ as a cofactor has been elucidated,
relatively little is known about the pathway leading to the biosynthesis of this intriguing
cofactor. Recently six genes belonging to the pqqABCDEF operon were found to be essential
for the biosynthesis of PQQ, and the biosynthesis of PQQ were found to involve many uniquesynthesis steps. Structural studies of these genes are necessary to elucidate the synthesis
mechanism. However, until now, only the structures of PqqB and PqqC have been determined.
We now report the tertiary structure of PqqD from a plant pathogen Xanthomonas campestris(Xc) determined to a resolution of 1.66 Å using X-ray crystallography. The crystal structure of
XcPqqD was found to adopt a dimer of novel saddle-like fold that revealed considerable
differences to the structure predicted de novo and carried out in the absence of suitable
template. In addition, a phosphate ligand was found to be situated very well in the highly
positively-charged central channel. Docking study of PqqD with PQQ located PQQ at thesimilar phosphate binding site as well, indicating that PqqD can possibly bind PQQ and serve
as a PQQ carrier.
Reference
Tsai T-Y, Yang C-Y, Shih H-L, Wang AH-J, Chou S-H. Xanthomonas campestris PqqD in the
Pyrroloquinoline Quinone Biosynthesis Operon Adopts a Novel Saddle-Like Fold That Possibly Serves asa PQQ Carrier. Proteins: Structure, Function and Bioinformatics 2009; in press.

Dual functions of an exosome component protein
Rrp46/CRN-5 in RNA degradation and DNA
fragmentation

P-69

Che-Chuan Yang1,2, Yi-Ting Wang2,3,4, Yu-Yuan Hsiao2,4, Lyudmila G. Doudeva2,and Hanna S. Yuan1,2,3*
1
Graduate Institute of Biochemistry and Molecular Biology, National Taiwan University
Taiwan2 Institute of Molecular Biology, Academia Sinica
3 Institute of Chemical Biology and Molecular Biophysics, Taiwan International
Graduate Program, Academia Sinica
4 Institute of Bioinformatics and Structural Biology, National Tsing Hua University,
Hsinchu, Taiwan.
(hanna@sinica.edu.tw)

Rrp46 is one of the RNase PH family proteins, first identified as a component protein of the
eukaryotic exosome, a protein complex involved in RNA turnover, surveillance andprocessing. The Rrp46 homolog, CRN-5, was subsequently characterized as a cell
death-related nuclease, participating in DNA fragmentation during apoptosis in C. elegans.
Here, we compare the biochemical and structural properties of CRN-5 to its human homolog,
hRrp46, and its rice homolog, oRrp46. The crystal structures of CRN-5 and oRrp46 were also
determined at a resolution of 3.9 Å and 2.0 Å, respectively. We found that the recombinantand endogenous Rrp46/CRN-5 formed homodimers, and the dimeric oRrp46 had both
phosphorolytic RNase and hydrolytic DNase activities, whereas hRrp46 and CRN-5 onlybound to DNA with neither RNase nor DNase activity. Crystal structures of CRN-5 showedthat the homo-dimeric assembly was similar to that of archaeal Rrp41-Rrp42. Site-directedmutagenesis of several residues in oRrp46 abolished its DNase and DNA/RNA binding- 146 -

AsCA’09

Posteractivities, confirming the critical importance of these residues in catalysis and substratebinding. CRN-5, although without any detectable DNase activity itself, interacted with the
apoptotic nuclease CRN-4, and enhanced the DNase activity of CRN-4. Together, all theseresults strongly suggest that Rrp46 plays dual roles, functioning as an exosome component
protein in RNA turnover in a healthy cell, and switching its role to participate in DNA
fragmentation in apoptosis.

Preliminary X-ray analysis of human Frk kinasedomain

P-70

Xiaoyan Yang1, Takayoshi Kinoshita1, Nao Miyano1, Tetsuko Nakaniwa1, Koichi
Yokota2, Masaki Gouda2, Toshiji Tada1
1Department of Biological Science, Graduate School of Science, Osaka Prefecture
University, Gakuen-cho 1-1, Sakai, Osaka 599-8531, Japan.
2Carna Bioscinences Inc. , KIBC 511, 5-2-2, Minatojima-Minatomachi ,Chuo-ku, Kobe
650-0047, Hyogo, Japan.

Frk is a member of Src family kinases and expressed especially in epithelial tissue.
Developmental expression patterns and functional over-expression suggested that Frk had a
crucial role in growth suppression and differentiation. Excess Frk activity is involved in type I
diabetes via beta-cell destruction and numerous human cancers. We aimed to perform X-ray
crystallography on Frk to elucidate the precise active-site structure for structure-based drug
design. The C-terminal His-tagged Frk kinase domain was expressed by E. coli. Purificationby the Ni-NTA affinity and anion-exchange chromatograms yielded three major peaks. The
fractionized samples were characterized as Frk at the differential phosphorylation states by
the SDS-PAGE, western blotting and activity measurement experiments. The
unphosphorylated and mono-phosphorylated (in the activation loop) proteins were
crystallized using the commercially available screening kits. Optimization of crystallization
condition is currently in progress.

Crystal structures of human BTG2 and mouse TIS21
involved in suppression of CAF1 deadenylase activity

P-71

Xiuna Yang1,2, Masahiro Morita3, Hui Wang1,2, Toru Suzuki3, Wen Yang1,4, Yunhai
Luo1, Cong Zhao4, Yue Yu5, Mark Bartlam4, Tadashi Yamamoto3,* and Zihe Rao1,2,4
1
Laboratory of Structural Biology, Tsinghua University, Beijing 100084,(yangxn@xtal.tsinghua.edu.cn)
2
National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of
Sciences, Beijing 100101, China,(raozh@xtal.tsinghua.edu.cn)
3
Division of Oncology, Institute of Medical Science, University of Tokyo, Minato-ku,
Tokyo 108-8639, Japan,(tyamamot@ims.u-tokyo.ac.jp)
4
College of Life Sciences & Tianjin State Laboratory of Protein Sciences, Nankai
University, Tianjin 300071(bartlam@nankai.edu.cn)

BTG2 is the prototypical member of the TOB family and is known to be involved in cell
growth, differentiation, and DNA repair. As a transcriptional co-regulator, BTG2 interacts
with CCR4-associated factor 1 (CAF1) and POP2 (CALIF), which are key components of thegeneral CCR4/NOT multi-subunit transcription complex, and which are reported to play
- 147 -

AsCA’09

Posterdistinct roles as nucleases involved in mRNA deadenylation. Here we report the crystal
structures of human BTG2 and mouse TIS21 to 2.3 Å and 2.2 Å resolution, respectively. The
structures reveal the putative CAF1 binding site. CAF1 deadenylase assays were performed
with wild-type BTG2 and mutants that disrupt the interaction with CAF1. The results reveal
the suppressive role of BTG2 in the regulation of CAF1 deadenylase activity. Our study
provides insights into the formation of the BTG2-CAF1 complex and the potential role of
BTG2 in the regulation of CAF1.
Keywords: BTG2; TOB family; CAF1 binding; deadenylase activity; crystal structure

Crystal Structure of YqeH, a Circularly Permuted
GTPaseP-72

Ji Young Yoon1, Hye-Jin Yoon1, Hyoun Sook Kim1, Kyoung Hoon Kim1, Do Jin
Kim1, Sang Jae Lee1, Jun Young Jang1, and Se Won Suh1,2
1
Department of Chemistry, College of Natural Sciences, Seoul National University,
151-747, Seoul, Korea (sewonsuh@snu.ac.kr)
2
Department of Biophysics and Chemical Biology, College of Natural Sciences, Seoul
National University, 151-747, Seoul, Korea

Proteins containing circularly permutated G-domains are prevalent in bacteria (YlqF, YqeH,
YjeQ, YawG, MJ1464), yeast, plants, and even humans (LSG1). YqeH is essential for theviability of Bacillus subtilis. YqeH participates in the biogenesis of the 30S ribosome subunit
and assists in 50S ribosome assembly. The YqeH C-terminal domain contains some conserved
residues that have been shown to be important for RNA binding by TRAP. YqeH probably
acts as a G-protein that regulates nucleic acid recognition. To gain insight into the YqeH
function at the molecular level, we have overexpressed and crystallized YqeH from
Thermotoga maritima in complex with GDP. X-ray diffraction data were collected to 2.8 Åusing synchrotron X-rays. The native crystal belongs to the tetragonal space group P41, withunit cell parameters of a = 81.62 Å, b = 81.62 Å, c = 146.00 Å, and α = β = γ = 90°. The
asymmetric unit contains two monomers, giving a crystal volume per protein mass (Vm) of
2.89 Å3 Da-1 and a solvent content of 57%. The structure was determined using themulti-wavelength anomalous diffraction data from a crystal of the SeMet-substituted protein.
The model has been refined to crystallograpic Rwork and Rfree values of 20.3% and 29.2%,
respectively.

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AsCA’09

P-73

Poster

Structure and function study of the DUF55 domain ofhuman thymocyte nuclear protein 1 and structure
determination method study of twinning crystals
Feng Yu1, Aixin Song2, Chunyan Xu1, Lihua Sun1, Jian Li1, Lin Tang1, Hongyu Hu2,
Jianhua He1*
1
Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai, China(hejh@sinap.ac.cn)
2
The Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences,
Shanghai, China

Human thymocyte nuclear protein 1 (hTHYN1), which is related with apoptosis, contains aunique DUF55 domain of 167 residues (55 - 221), but its cellular function is unclear.
The recombinant full-length hTHYN1 protein is unstable at high concentration and istherefore not well suited for structural analysis. DUF55 domain is a stable domain ofhTHYN1 and suited for structural analysis. Crystals of DUF55 belong to the trigonal spacegroup P31, and cell dimension is a = b = 51.26, c = 122.40 Å. Datasets to 2.3 Å resolution
were collected. The intensity statistical analysis confirmed that the crystals of DUF55 domain
were partially twinned by tetartohedry, and twin fractions were 0.424, 0.300, 0.134 and 0.142.
The structure determination of DUF55 domain was very difficult and couldn't be achieved bypreviously reported approach, so an improved approach was developed and applied to it. Afterthe structure was determined, only one twofold axis of rotational pseudosymmetry was foundin the crystal structure, which was different from other tetartohedral twinning cases.
Using the DALI program, a YTH domain, which is a potential RNA binding domain fromhuman YTH domain-containing protein 2, was identified to have the most similar
three-dimensional fold to DUF55. It is implied that DUF55 might be a potential RNA-related
domain.

P-74

Structure of Catalytic Domain of Matriptase inComplex with SFTI-1
Cai Yuan1, Longguang Jiang1, Liqing Chen2, Mingdong Huang1
1
Fujian Institute of Research on the Structure of Matter, The Chinese Academy of
Sciences, Fuzhou, Fujian 350002, China (yuancai@fjirsm.ac.cn)
2University of Alabama in Huntsville, Huntsville, AL 35899, USA (chenlq@uah.edu)

Matriptase is a type II transmembane serine protease. It was demonstrated to be able toactivate pro-uPA and pro-HGF/SF to their active forms [1], and thus play an important role intumor invasion and metastasis. Here we report the structure of catalytic domain of matriptase
in complex with sunflower trypsin inhibitor (SFTI-1), a potent inhibitor of matriptase with a
Ki of 0.92 nM [2,3]. Our crystal structure at 2.0 Å shows that SFTI-1 binds in the active siteof matriptase. Arg2, Thr4, Lys5, Ile7, and Phe12 of SFTI-1 play important roles in matriptase
binding through hydrogen bonds and van der Waals interactions with the residues located in
the active site of matriptase. Although the scissile bond between Lys5 and Ser6 of matriptase
is oriented properly for nucleophilic attack, the electron density confirms the scissile bond isuncleaved within the ``average'' structure observed in the crystal, probably because that the
distance between SFTI-1 Lys5 C and matriptase Ser195 Oγ is too long for effective chemical- 149 -

AsCA’09

Posterreaction. This study provide insight to matriptase structure and may assist with design ofspecific inhibitors to matriptase.
References
1.
2.
3.

Uhland K. Matriptase and its putative role in cancer. Cell Mol Life Sci 2006;63 (24):2968-78.
Long YQ, Lee SL, Lin CY, Enyedy IJ, Wang S, Li P, Dickson RB, Roller PP. Synthesis and evaluationof the sunflower derived trypsin inhibitor as a potent inhibitor of the type II transmembrane serine
protease, matriptase. Bioorg Med Chem Lett 2001;11 (18):2515-9.
Korsinczky ML, Schirra HJ, Craik DJ. Sunflower trypsin inhibitor-1. Curr Protein Pept Sci 2004;5(5):351-64.

P-75

Crystallization and preliminary X-ray crystallographic
analysis of Escherichia coli CusB
Bo-Young Yun, Yongbin Xu and Nam-Chul Ha
A College of Pharmacy and Research Institute for Drug Development, Pusan National
University, Jangjeon-dong, Geumjeong-gu, Busan 609-735, Republic of Korea,

Periplasmic membrane-fusion proteins (MFPs) are an essential component of multidrug andmetal-efflux pumps in Gram-negative bacteria. However, the functional structure of MFPs
remains unclear. CusCFBA, the CuI and AgI efflux system in Escherichia coli, consists of the
MFP CusB, the OMF CusC and the RND-type transporter CusA. The MFP CusB bridges theinner membrane RND-type efflux transporter CusA and the outer membrane factor CusC andexhibits substrate-linked conformational changes which distinguish it from other MFP-family
members. CusB from E. coli was overexpressed and the recombinant protein was purified
using Ni–NTA affinity, Q anion-exchange and gel-filtration chromatography. The purified
CusB protein was crystallized using the vapour-diffusion method. A diffraction data set wascollected to a resolution of 3.1 A ˚ at 100 K. The crystal belonged to space group C222.

Crystallization and preliminary crystallographic
analysis of a ribokinase from Staphylococcus aureus

P-76

Lin Wang1,2, Haipeng Wang1, Jianbin Ruan1, Changlin Tian1,2, Baolin Sun1,2 andJianye Zang1
1
School of Life Sciences, University of Science and Technology of China, 96 JinzhaiRoad, Hefei, Anhui 230027, People’s Republic of China (zangjy@ustc.edu.cn)
2
Hefei National Laboratory for Physical Sciences at Microscale, University of Scienceand Technology of China, 96 Jinzhai Road, Hefei, Anhui 230027, People’s Republic of
China

Ribokinase belongs to the PfkB carbohydrate kinase family and is found in both prokaryotes
and eukaryotes (Bork et al., 1993). Ribokinase, which catalyzes the reaction of D-ribose andATP to produce ADP and ribose-5-phosphate, plays a key role in the recycling of sugars
produced from the metabolism of nucleotides (Anderson & Cooper, 1969; Lopilato et al.,1984). The catalytic activity of ribokinase is nearly completely dependent on the presence ofpentavalent ions (PIV) such as phosphate (Maj & Gupta, 2001). Although there is a phosphate- 150 -

AsCA’09

Posterion present near the active site in the structure of E. coli ribokinase in complex with ribose
and ADP (Sigrell et al., 1998), the exact role that PIV plays in activating ribokinase still
remains elusive. In order to address this question, a ribokinase from Staphylococcus aureus
named Sa239 was cloned, expressed, purified. And it was crystallized at 295 K under thecondition consisting of 23% (w/v) PEG 3000, 0.1 M sodium citrate pH 5.6. A complete data
set to 2.89 Å resolution was collected at 100 K on beamline 3W1A at BSRF and processedusing HKL-2000 (Otwinowski & Minor, 1997). The Rmerges of the dataset are 10.2% and40.6% for overall data and highest shell, respectively. And the crystal belongs to thehexagonal space group P6122 or P6522 with unit cell parameters a = b = 91.8Å, c = 160.7Å,
α=β= 90º, γ= 120º. The calculated Matthews coefficient (VM) of 3.01Å3 Da-1, with a solvent
content of 59.2%, indicates the presence of one molecule in the asymmetric unit (Matthews,
1968). On the other hand, microcrystals of Sa239 in complex with phosphate were obtained
too. The crystals of Sa239 and its complex with phosphate ions provide the basis of theirstructures solving and their structures will help in elucidating the mechanism by which
phosphate ions activate ribokinase.
References
1.
2.
3.
4.
5.
6.
7.

Anderson, A. & Cooper, R. A. (1969). Biochim. Biophys. Acta, 177, 163–165.
Bork, O., Sander, C. & Valencia, A. (1993). Protein Sci. 2, 31–40.
Lopilato, J. E., Garwin, J. L., Emr, S. D., Silhavy, T. J. & Beckwith, J. R. (1984). J. Bacteriol. 158,
665–673.
Maj, M. C. & Gupta, R. S. (2001). J. Protein Chem. 20, 139–144.
Matthews, B. W. (1968). J. Mol. Biol. 33, 491–497.
Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307–326.
Sigrell, J. A., Cameron, A. D., Jones, T. A. & Mowbray, S. L. (1998). Structure, 6, 183–193.

Nucleoside Monophosphate Complex Structures of
the Endonuclease Domain from the Influenza
Polymerase PA Subunit Reveal the Substrate Binding
Site inside the Catalytic Center

P-77

Cong Zhao1,$, Zhiyong Lou1,$, Yu Guo2, Ming Ma3, Yutao Chen3, Shuaiyi Liang1,
Liang Zhang2, Shoudeng Chen3, Xuemei Li3, Yingfang Liu3,*, Mark Bartlam2 andZihe Rao1,2,3,*
1
Structural Biology Laboratory, Tsinghua University, Beijing, 100084, China,(raozh@xtal.tsinghua.edu.cn).
2
College of Life Sciences and Tianjin State Laboratory of Protein Science, Nankai
University, Tianjin 300071, China
3
National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of
Science, Beijing, 100101, China. ( liuy@sun5.ibp.ac.cn)

Highly pathogenic influenza strains currently in circulation pose the significant risk of a
global pandemic. Following the reported crystal structure of the endonuclease domain fromthe avian influenza virus polymerase PA subunit, here we report the results of a systematic
X-ray crystallographic analysis of its complex with adenosine, uridine and thymidine
monophosphates (NMPs). Electron density corresponding to the monophosphate moiety ofeach nucleotide was apparent in each NMP complex and bound to the catalytic metal. A
hydrophobic site was found to contribute to nucleoside binding. The NMPs complex- 151 -

AsCA’09

Posterstructures should represent the conformation of the bound product after nuclease cleavage.
Moreover, one solvent molecule was found to occupy an equivalent position to the second
reported Mn2+ ion where it mediates the interaction between bound NMPs and PAN in thepresence of Mg2+ ion. The results presented here indicate a possible cleavage mechanism andidentify a distinct nucleotide binding pocket. The identification of this binding pocket opens a
new avenue for anti-influenza drug discovery targeting the cap-dependent endonuclease, in
response to the world-wide threat of influenza.

P-78

From peptidic inhibitor leads to non-peptidic drugs:
Making use of the reversible binding of peptide
aldehydes to cysteine proteases in Dynamic Ligation
Screening
Lili Zhu,1 Jinzhi Tan,1 Marco F. Schmidt,2,3 Jörg Rademann2,3 & Rolf Hilgenfeld1
1
Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck
(zhu@biochem.uni-luebeck.de)2
Institute for Chemistry and Biochemistry, Free University Berlin, Takustr. 3, 14195
Berlin3
Leibniz Institute for Molecular Pharmacology (FMP), Robert-Rössle-Str. 10, 13125
BerlinIn contrast to chloromethyl ketones, aldehydes bind reversibly to the active-site sulfhydryl ofcysteine proteases [1]. We have developed a novel procedure that makes use of this property
in the search for non-peptidic competitive inhibitors of these proteases. This procedure iscalled“Dynamic Ligation Screening” (DLS). We used the SARS coronavirus main proteinase(SARS-CoV Mpro) as an example to test the DLS concept [2]. First, a peptidic aldehyde
inhibitor was reacted with the protease. This led to the formation of a covalent adductbetween the active-site Cys145 and the inhibitor. Then, we screened a small library (234compounds) of non-peptidic amines and other nucleophiles for compounds that would reactwith the protease-bound aldehyde and replace the active-site cysteine. The resulting imine
was assumed to occupy subsites P5 to P2’. Subsequently, the compound discovered had its
amine replaced by an aldehyde warhead. It was reacted with the native protease and formed acovalent adduct. The same library of nucleophiles was then screened for another non-peptidic
compound that would replace Cys145 from the aldehyde. The ligation product discovered
inhibited the enzyme with a Ki of 2.9 μM. Remarkably, this non-peptidic, competitive
inhibitor was ligated from two halves each of which had no inhibitory activity on its own.
These reactions will only work in the presence of the target enzyme. Thus, the reversibility of
the covalent adduct formation between aldehydes and cysteine proteases can be used to
discover non-peptidic inhibitors that block the target by non-covalent interaction. Recently,
we determined three crystal structures of SARS-CoV Mpro in complex with peptide aldehydes(Ac-ESTLQ-H, Ac-NSFSQ, and Ac-NSTSQ-H), explaining the mechanism of aldehyde
inhibitor binding to SARS-CoV Mpro. Co-crystallization experiments with the ligation imine
product are underway and performing the reaction in the crystals is also being tested..
References
1.

S.I. Al-Gharabli, S.T. Shah, S. Weik, M.F. Schmidt, J.R. Mesters, D. Kuhn, G. Klebe, R. Hilgenfeld, J.
- 152 -

AsCA’09

2.

PosterRademann, Chembiochem 7, 1048-1055 (2006).
M.F. Schmidt, A. Isidro-Llobet, M. Lisurek, A. El-Dahshan, J. Tan, R. Hilgenfeld, J. Rademann,
Angew Chem Int Ed Engl 47, 3275-3278 (2008).

- 153 -

AsCA’09

P-79

PosterCo-crystallization of Valproic acid by Co-grinding
and Structure Determination from Powder Diffraction
Data
Masahide Aoki1, Hidehiro Uekusa1, Hiroyuki Kurobe2, Etsuo Yonemochi2,
Katsuhide Terada2
1
Tokyo Institute of Technology, 2-12-1 Ookayama, Meguro-ku, Tokyo, 152-8551,
JAPAN (aoki.m.ab@m.titech.ac.jp)
2Toho University, 2-2-1 Miyama, Funabashi-shi, Chiba, 274-8510, JAPANCo-crystallization of pharmaceuticals with low molecular weight compounds is very effective
to improve physical properties such as stability, solubility, and bioavailability. Valproic acid(oily liquid) is known as antiepileptic agent, and used as sodium valproate form (white
crystalline powder) which is highly hygroscopic and deliquescent. In this study, valproic acidco-crylstals were explored to improve its hygroscopicity and the crystal structure wasanalyzed from PXRD.
As a result of vigorous screening, valproic acid and L-arginine
co-crystal was obtained only by co-grinding at 1:1 molar ratio(Fig.1). L-arginine is an amino acid with relatively strong basicity,and known to form organic salts with acids in co-crystals. The
hygroscopicity is greatly improved by co-crystallization, so theco-crystal is stable up to R.H. 70%. In contrast, sodium valproatetransforms to hydrate form at R.H. 35% and deliquesces at R.H.
45%.
When valproic acid and L-arginine were crystallized from water solution, only amorphousmaterials were obtained, so it was difficult to prepare single crystals for X-ray structure
analysis. Thus, the crystal structure was determined directly from powder diffraction data.
The powder diffraction dataset was measured in SPring-8 (BL19B2) using large IP
Debye-Scherrer camera. The structure solution was carried out by direct space method using azwitter-ion form of L-arginine, and organic salt form of the complex as the model structure.
The best solution was refined by Rietveld method using restraints (Fig.2).
Carboxylic anion group of valproic acid forms four O…H-N hydrogen bonds with L-arginine.
In addition, L-arginine forms N-H…O hydrogen bond with another L-arginine. In the
crystal, there are layers of valproic acid and L-arginine (Fig.3). Hydrophobic alkyl chains ofvalproic acid are inside of the valproic acid layer, on the other hand, hydrophilic carboxylgroups are exposed to the L-arginine layer and forming hydrogen bonds with L-arginine.

- 154 -

AsCA’09

Poster

The Design of New Bicyclo[3.3.0]octane Lattice
Inclusion Hosts and Cocrystal Partner Molecules

P-80

Roger Bishop1, Mohan M. Bhadbhade2, Isa Y. H. Chan1
1
School of Chemistry, University of New South Wales, UNSW Sydney NSW 2052,
Australia (r.bishop@unsw.edu.au)2
Analytical Centre, University of New South Wales, UNSW Sydney NSW 2052,
Australia,( m.bhadbhade@unsw.edu.au)

Vossen, working in Schroeter’s laboratory, unexpectedly discovered a beautiful red salt ofcomposition (C16H15O10Na).(CH3OH)2 in 1910 [1]. A considerable amount of chemical
detective work was necessary before the general structure of Schroeter and Vossen’s red salt, abicyclo[3.3.0]octane derivative, was reported by Yates and Bhat in 1954 [2]. However, detailsof the stereochemistry, metal co-ordination, and the role of the methanol guest molecules,
remained unknown until we reported the crystal structure of (1).(CH3OH)2 in 2002 [3].
Reduction of the red salt with sodium amalgam yields a tetraester,
shown by us to have the structure 2 [4]. Although compound 2 wasa non-host molecule, our X-ray structure determination revealed
that this simple V-shaped substance packed rather inefficiently byitself in the solid state.

MeO
O

1

C

_

OMe
O

C

O

Na

+

O
H
H
MeO2C H CO2Me

CO Me
MeO C
This characteristic is known to be one that often results in guest
H
inclusion in order to achieve a denser and lower energy crystal
H-O
O-H
structure. Therefore we were encouraged to prepare other
H
CO Me
MeO C
bicycle [3.3.0]octane derivatives and explore their inclusion
2
behaviour. It turns out that several very simple dialcoholH
derivatives of this ring system are excellent new host molecules.
O-H
H-O
The properties of these compounds are being investigatedH
systematically as part of a current Ph.D. project. The achiral3
dialcohol 3 is one example of these new alicyclic host molecules.
Examples of lattice inclusion and cocrystal structures formed by 3 will be described in crystal
engineering terms.

References[1] G. Vossen, Inauguraldissertation, University of Bonn, Germany, 1910.
[2] P. Yates and G. Bhat, Chem. Ind. (London), 1954, 1237.
[3] D. Djaidi, R. Bishop, D. C. Craig and M. L. Scudder, New J. Chem., 2002, 26, 614.
[4] D. Djaidi, Ph. D. thesis, The University of New South Wales, 2006.

- 155 -

2

2

2

2

AsCA’09

PosterZintl Phase Compounds Yb1-xCaxCd2Sb2 With Tunable
Thermoelectric Properties Induced by Cation
Substitution

P-81

Qigao Cao1,2, Hui Zhang1, Meibo Tang1, Haohong Chen1, Xinxin Yang1, Xiangxin
Guo1, Jingtai Zhao*1, Grin Yuri*3
1
Shanghai Institute of Ceramics Chinese Academy of Sciences, Chinese, 1295 Dingxi
Road, Changning District, Shanghai, 200050, China (caoqigao@mail.sic.ac.cn)
2Graduate School of Chinese Academy of Sciences, Beijing, China
3
Max-Planck-Institut für Chemische Physik fester Stoffe, Nöthnitzer Str. 40, 01187
Dresden, Germany

It has been shown previously that the thermoelectric properties of the Zintl phase compoundYbCd2Sb2 can be finely tuned via Zn substitution at
the Cd-site in the anionic (Cd2Sb2)2− framework. Here
we report the results of the investigation of
isoelectronic substitution of Yb by Ca. The p-type
Yb1-xCaxCd2Sb2 (0.2≤x≤0.8) samples have beensynthesized via a solid-state reaction followed bysuitable cooling, annealing, grounding, and spark
plasma sintering (SPS) densification processes. In
samples with x=0.2, 0.4, 0.5, 0.6, 0.8, the electricalconductivity, Seebeck coefficient, and thermal
conductivity measurements have been performed as a function of temperature from 300 to
650 K. It is found that the Ca substitution effectively lowers the thermal conductivity for all
samples at high temperature, while it significantly increases the Seebeck coefficient. As aresult, the best dimensionless figure of merit ZT of 0.96 has been attained at 650 K for x=0.4.

Molecular self-assembly – tweezers, forks, and boxes

P-82

Christine Cardin, Yu Gan, Zhixue Zhu and Howard Colquhoun
Department of Chemistry, university of Reading, Whiteknights, Reading, RG6 6AD, UK(c.j.cardin@rdg.ac.uk)

Intense current interest in the design of multi-component, nanoscale molecular assemblies has
led to the exploitation of many types of intermolecular interaction, including π-stacking
between aromatic donor and acceptor sites. This type of interaction has recently enabled thefabrication of nanoscale devices including light- and redox-driven switches and molecular
logic-gates. In view of the relatively labile nature of the N-benzylpyridinium linkage on whichmuch research into π-stacked molecular assemblies has so far depended, Professor
Colquhoun has recently developed a new class of supramolecular materials based onaromatic poly (imide-sulfone) chemistry. Linear and macrocyclic materials of this typedisplay extreme thermochemical stability and readily form π-stacked donor-acceptor
complexes with polycyclic hydrocarbons such as pyrene.
Most importantly, sequence-selective complexation of the imide residues in aromaticco-polyimides by a pyrene-based molecular tweezer enables monomer-sequence information
to be read by the tweezer and reported through sequence-dependent 1H NMR complexation- 156 -

AsCA’09

Postershifts. These very significant discoveries in molecular information-processing have been
crucially dependent on single-crystal X-ray analyses of tweezer-complexes with linear andcyclic oligo-imides (e.g. 2 and 3 above: hydrogens omitted for clarity). Tweezer-chain binding
has thus been shown to arise not only from π-π stacking interactions but also from N-H...O
and C-H...O hydrogen bonding, and from polymer chain-folding. Crystallographic data of thistype are of the utmost importance for predictive computational modelling of tweezer-polymer
interactions.
Recently we have refined in-house data on the elegant doubly-boundoligomer-tweezer ('zigzag') complex shown here. The crystal structure shown atright provides the first unequivocal model for chain-folding and small-moleculebinding in any synthetic polymer system. Moreover, the supramoleculargeometry found in the solid state is remarkably consistent with extensive NMR
studies of tweezer-binding in solution. The crystal contains very large solvent
cavities and both model building and structure-refinement required very highquality diffraction data. Using the in-house data from our Oxford Diffraction
Enhance-Ultra source, with a data collection time of three days, a model has in fact now been
built, with a current R factor of 13.2 %.
These and related examples of molecular self-assembly will be reported in this poster.

Metal Organic Frameworks from 3,3’-Biphenic Acid

P-83

Chun-Lung Choi1, Herman H-Y. Sung1, M. Gerry J. Lesley2, Ian D. Williams1
1
Department of Chemistry, Hong Kong University of Science and Technology, Clear
Water Bay, Kowloon, Hong Kong, China (chwill@ust.hk)
2
Department of Chemistry, Southern Connecticut State University, New Haven, U.S.A..

Biphenyl based carboxylates appear to have excellent characteristics for formation of open yet
stable, crystalline metal-organic framework polymers (MOFs). Whilst 4,4’- and 2,2’-biphenic
acids are commercially available and have been studied in depth, the 3,3’ analogue is not andits potential for MOF formation virtually unexplored. The ligand was prepared by coupling ofan arylbromide with phenylboronic acid by Miyaura-Suzuki catalyzed coupling. The
coordination polymers of 3,3’-biphenic acid with variety of transition metals and lanthanides
have been explored and about 10 new phase types are reported. Using 4,4’-bipyridine as aN-donor spacer ligand highly open frameworks [M(3,3’-biphenate)(4,4’-bipy)0.5] can beformed containing paddle-wheel tetracarboxylate metal dimers. These network structures
triply interpenetrate. From hydrothermal synthesis conditions at high pH several novel
open-framework hybrid solids containing 3,3’-biphenate and hydroxide can be formed, e.g.
[Zn5(OH)8(3,3’-biphenate)] and [Ln3(OH)6(3,3’-biphenate)(OAc)]. The structural stabilities
and sorption properties of these novel MOF materials are under investigation- 157 -

AsCA’09

Poster

Acknowledgements: We are grateful to the Research Grant Council HK (603306) andHKUST for funding of this work and Connecticut State University for granting sabbaticalleave for Prof. Lesley.

P-84

On the quality of data necessary for performing 2nd &4th moment method of evaluating crystallite size &
dislocation density
Prabal Dasgupta1 & Bholanath Mondal2
1,2
Department of central Scientific services, Indian Association for the Cultivation of
Science, Kolkata-700032,India (prabaldasgupta@hotmail.com)

With the advent of epoch-making paper by Borbely et al1 ,renaissance of 2nd & 4th moment
method of evaluating crystallite size has taken place. They reported that they have made useof high resolution XRD data.Present work aims to explores what quality of XRD data isessential to carry out such analysis.Background & instrumental broadening corrected,
111&200 profiles of XRD data of commercial grade metallic Cu & Ni ( in step-scan mode),
those were stripped of Kα2 contribution( using Bruecker software), were subjected to suchanalysis.M2 & M4/q2 plots suggest that peak broadening in these materials are mainly
crystallite size-related broadening .Different step widths(ranging from .005 to .03deg) andscan speeds (0.2,0.5& 2.50sec per stepwidth)were chosen so as to ascertain the quality of datathat yields more or less same crystallite size( within 3%) from the 2nd & 4th moment plot.It
was revealed that stepwidth of 0.01deg or less with scan speed of at least 2.0 sec step -1 yields
satisfactory converegence.
Reference
I.A.Borbely,A. Revesz & I.Groma ,Zeit Krist. Suppl 23 (2006) 87-92

Crystal structure of organic compound ethyl-2amino-5-bromothiazole-4-carboxylate

P-85

K.V.Arjuna Gowda1, Ramakrishna Gowda2 and I.A.Khazi3
1
Department of Physics, Government First Grade College, K.R.Pura, Bangalore, INDIA
2
Department of Physics, Government College for women, Kolar, INDIA
3
Department of Chemistry, Karnataka University, Dharwad, INDIA(arjunagowda@indiainfo.com)

The 2-amino-5-bromothiazole-4-carboxylate was required for the proposed synthesis of
ethyl-2-amino-5-arylthiothiazole-4-carboxylates and ethyl-2-amino-5-arenesulfonyl thiazole4- 158 -AsCA’09

Postercarboxylates by affecting SN2 reaction between suitably substituted thiophenoxide ions and2-amino-5-bromothiazole-4-carboxylate, which are reported to have anti-bacterial,anti-tubercular, Chemotherapeutic and schistosomicidal activities.
The title compound grown by slow evaporation from aqueous ethanol pale yellow needle
crystals obtained. The compound crystallizes as monoclinic system and cell parameters
a=8.665(6)Å,b=9.903(7)Å,c=11.381(7)Å,α=96.777(11)°β=93.596(11)°andγ=109.321(10)°.
The structure has been solved by direct methods using SHELXS-97 and refined by afull-matrix least-square method using SHELXL-97 program. The final R-value is 0.0403. The
title compound is under progress for publication.

Local Structure Analysis of an Automobile Catalyst
La1.02Fe0.95Pd0.05O3 by Pd K-edge XAFS

P-86

Shoshi Higuchi1, Daiju Matsumura2, Yasuo Nishihata2, Jun’iciro Mizuki2, Hikaru
Terauchi1, Isao Takahashi1, Masashi Taniguchi3, Mari Uenishi3, Hirohisa Tanaka3,
Kimiyoshi Kaneko4
1
Kwansei-Gakuin University, 2-1 Gakuen, Sanda Hyogo 669-1337, Japan,(czn29980@kwansei.ac.jp)
2
Synchrotron Radiation Research Center, Japan Atomic Energy Agency, Sayo, Hyogo
679-5148, Japan
3
Daihatsu Motor Co., Ltd., Gamo, Shiga 520-2593, Japan
4
Hokko Chemical Industry Co., Ltd., Fine Chemical Reserch Laboratories, 2165, Toda,
Atsugi-shi, Kanagawa 243-0023, JapanA La1.02Fe0.95Pd0.05O3(LFPO) catalyst has special feature which maintains high catalytic
property even in long time use, while an alumina catalyst employs a sufficient excess of
precious metals to ensure the activity. The reason of the long life catalyst is that the Pd
particle goes in and out of the perovskite structure of the LFPO during oxidation andreduction processes in the exhaust gas. Because of this mechanism, the Pd particle size
maintains effectively small. [1][2]In this study, samples were prepared by the alkoxide method and coprecipitation method for
the LFPO. We observed the local structural difference of these two samples by x-ray
absorption fine structure (XAFS) at 15 K with transmission mode at BL14B1, SPring-8. The
information by XAFS technique is different from long range structural information by x-ray
diffraction technique. XAFS technique shows elementary selective local structure. Therefore,
XAFS technique is very suitable to observe the local structure round Pd as a trace additive toarbitrary select.
Figure 1 shows extended x-ray absorption fine structure (EXAFS) function of the two
samples. It is found that main oscillations from Pd-O bond for the each sample are similar.
However some slight differences were found as shown in Fig.2 which shows an extended
figure for the square in Fig.1. These differences are derived from short wavelength component.
From the result of analysis, it is found that high coordination structure raises these differences.
At conclusion, it is revealed that first coordination from Pd-O bond is similar between two
samples, which were prepared by alkoxide method and coprecipitaton method, and minute- 159 -

AsCA’09

Posterstructure in higher coordination is different between them.
8

20
Alkoxide method
Coprecipitation method

16
12

4
-3

k χ(k) (Å )

0

2
0
-2

3

3

-3

k χ(k) (Å )

4
-4
-8
-12

-4
-6

-16
-20

Alkoxide method
Coprecipitation method

6

8

5

10

-8

15
-1

Fig.1 EXAFS function k3χ(k) measured at 15 K

3.6

4.0

4.4

4.8

5.2

5.6

6.0

-1

wave number (Å )wave number (Å )Fig.2 Close up of the EXAFS function in fig.1

References[1] Y. Nishihata et al., Nature, 418, 164 (2002)[2] H. Tanaka et al., Angew. Chem. Int. Ed, 5998, 45 (2006)

P-87

Regulation of Anthracene Arrangement andPhotoluminescence Properties by Using Organic
Salts
Tomoaki Hinoue, Norimitsu Tohnai, Ichiro Hisaki, Mikiji Miyata
Osaka University, 2-1, Yamadaoka, Suita-City, Osaka, 565-0871 Japan(koriki@molrec.mls.eng.osaka-u.ac.jp)

Solid-state photoluminescent properties depend strongly on molecular arrangement as well as
molecular structure of the constituent molecules. However, it is difficult to regulate thearrangements and therefore the relationships with solid-state photoluminescent properties
have not been elucidated exactly. In this context, we have regulated the arrangement offluorophores by employing organic salts composed of sulfonic acid bearing the fluorophores
and aliphatic amines. This method afforded convenient regulation of packing manner of thefluorophores depending on the substituents of aliphatic amines. Here, we present theregulation of anthracene arrangement and concomitant solid-state photoluminescence byusing ammonium anthracene disulfonate. Although unmodified anthracene molecule
aggregate in only 2-dimensional herringbone arrangement, ammonium anthracene disulfonate
afforded 1-dimentional and discrete monomer-like arrangement of anthracene moieties as wellas herringbone arrangement. Discrete arrangement showed strong fluorescence due to the
suppression of nonradiative deactivation, while 1-dimentional arrangement did weak but
red-shifted fluorescence.

Figure 1. Organic salts composed of anthracene disulfonic acid and aliphatic amine (top), and moleculararrangement of anthracene moieties obtained by X-ray crystal structure analyses (bottom).

References
1. Mizobe, Y., Tohnai, N., Miyata, M., Hasegawa, Y., Chem. Commun. 2005, 1839–1841.
2. Mizobe, Y., Hinoue, T., Yamamoto, A., Hisaki, I., Miyata, M., Hasegawa, Y., Tohnai, N., Chem. Eur. J.,- 160 -

AsCA’09

Posterin press.

P-88

X-ray structural study of intercalation compounds
BixTiS2
Sho Ikeda , Takuro Kawasaki and Ken-ichi Ohshima
Institute of Materials Science ,University of Tsukuba, Tsukuba 305-8573,Japan

Intercalated compounds titanium disulfides MxTiS2 have various structures and peculiar
physical properties depending on the kind or composition of M. Recently, Li et al. havereported that the resistivity and thermopower decreased as intercalated Bi content
increased[1,2]. However, there are no systematic reports on the crystal structure analysis of
BixTiS2.
Single crystals of BixTiS2 were grown in evacuated silica tubes by chemical vapor transport
method using iodine as a transport gas.Fig.1 shows the SEM image of BixTiS2. Structures
were investigated by single crystal X-ray diffraction method, where the data were collectedusing Imaging Plate (RAPID, Rigaku) at room temperature. The crystal structure was solved
by charge flipping methods and refined by the program JANA2006. The space groups andlattice parameters of BixTiS2 change with increasing intercalated Bi.

Fig.1

SEM image of BixTiS2References[1] D. Li, X.Y. Qin, Y.J. Gu (2006). Materials Research Bulletin 41, 282–290.
[2] D. Li, X.Y. Qin, J. Liu, H.S. Yang (2004). Phys. Lett. A 328, 493–499.

Crystal Structure of Tetracaine Hydrochloride
Polymorphs

P-89

Sayaka Ina1, Hidehiro Uekusa1, Naoko Itoda2, Etsuo Yonemochi2, Katsuhide
Terada2
1
Tokyo Institute of Technology, Japanese, 2-12-1 Ookayama, Meguro-ku, Tokyo,152-8551, Japan (ina.s.aa@m.titech.ac.jp)
2Toho University, 2-2-1 Miyama, Funabashi-shi, Chiba, 274-8510, JAPAN

Tetracaine hydrochloride (Fig. 1) is widely used local anesthetic drug. From thermal analysis,
it has ten (pseudo-) polymorphic forms, i.e. six anhydrous, three hydrates (hemi-, mono-, andtetra-hydrates), and one amorphous form, in different temperature and R.H. range, however,
only one crystal structure (Form 1) is known. Such pharmaceutical polymorphs should show
different physical properties like bioavailability or solubility depending on their crystal- 161 -

AsCA’09

Posterstructures. In this study, the crystal structures of the polymorphic crystals including thehydrates are analyzed, and their characteristic properties are examined.
Stable crystals of hemihydrate were recrystallized from 9:1 mixture of ethanol and water. On
the other hand, tetrahydrate crystals were obtained from anhydrous form (Form 1) at the highhumidity conditions (> R.H. 85%) or in slurry, which were relatively unstable andtransformed into mono- and then hemihydrates at ambient conditions. Crystal structure ofhemihydrate crystal was determined by single crystal X-ray structure analysis. The
crystallographic data are monoclinic, space group P21 with a=10.845(3), b=6.263(2),c=24.944(7)Å, β=94.695(6)°, and V=1688.5(9)å3.
In the crystal structure, two tetracaine hydrochloride molecules and one water molecule wereindependent. As for these two independent molecules, the torsion angle of –(CH2)2NMe2groups are different. It has a layer structure along c-axis in the crystal, in which the molecules
are packed as herringbone manner. The layers are connected by Cl– and water molecule via
NH+…Cl– and OH…Cl– charge assisted hydrogen bondings, and also by carbonyl O…HN
hydrogen bonding (Fig. 2). On the other hand, anhydrate form (Form1) has one independent
molecule, and it has flatter layer structure, which is considerably different from hemihydrate,
for example, each molecule has the same orientation in the same layer. The layers are also
connected by NH+…Cl– hydrogen bonds similar to the hemihydrate.
The difference of these crystal structures may influence characteristic such as solubility andstability.

Fig 1. Tetracaine hydrochloride

P-90

Fig 2. Crystal structure of hemihydrate viewed along b-axis

High Resolution X-ray Diffraction Analysis on(Lu2.1,Bi0.9)Fe5O12 Layers Grown on Gd3Ga5O12
Substrate
Hong Ji *, Huaiwu Zhang , Qiye Wen
State Key Laboratory of Electronic Thin Films and Integrated Devices, University ofElectronic Science and Technology of China, Chengdu 610054, China(jihong@uestc.edu.cn)

Epilayer composition, homogenous strain and surface morphology, which depend on processparameters, such as different doping, layer thickness, growth rate, etc. are of significant
importance for the device applications of the rare earth iron garnets films. High resolution
X-ray diffraction (HRXRD）is the most important non-destructive tool to obtain information
about physical properties, including crystal structure, defect levels, composition and thicknessof an epilayer and orientation relationship between the epilayer and its substrate. This paper
introduces HRXRD analysis (measuring X-ray instrument: Bede D1 Four-circle- 162 -

AsCA’09

Poster

Diffractometer ) on cubic (Lu2.1,Bi0.9)Fe5O12 thick films (~8um) grown on (111)
Gd3Ga5O12(GGG) single-crystal substrates (diameter size of 50 mm) by liquid phase epitaxy(LPE) method (growth rate of 0.39 nm/min), including observations of microstructural
heterogeneity on the epilayers using a rocking curve measurement (or ω scan), including
measurements of lattice constant on the epilayers using a ω/2θ scan. In the case of using acrystal analyzer , the (444) peak of (Lu2.1,Bi0.9)Fe5O12 is observed at the high-angle side of the
Gd3Ga5O12 (111) peak. The full width at half maximum intensity (FWHM) of rocking curve ofthe (Lu2.1,Bi0.9)Fe5O12 (444) peak is 14.16 arcsec. The calculated lattice constant of(Lu2.1,Bi0.9)Fe5O12 is 12.3732Å.
The purpose of this paper is to investigate the lattice constant of (Lu2.1,Bi0.9)Fe5O12 film layer.
In general, the lattice constant of (Lu2.1,Bi0.9)Fe5O12 changes systematically with the Lu or Bi
composition. In addition, it is understand that the crystal orientation direction of the(Lu2.1,Bi0.9)Fe5O12 epilayer is tilted with respect to the Gd3Ga5O12 substrate because its
mosaic structure, which will affect the measurement results. Therefore, a method for
eliminating the effect of epilayer tilt is needed to obtain reliable the (Lu2.1,Bi0.9)Fe5O12 lattice
constant. The derivative analysis technique for carefully corrected Bragg angle of the(Lu2.1,Bi0.9)Fe5O12 diffraction peak has been described in the paper. In some cases, we only
need to measure the average angular difference (peak separation) ᇞθB to eliminate the effectof epilayer tilt ( in an actual analysis, its ᇞθB value depends on lattice mismatch and thepresence or absence of lattice relaxation). In the case for symmetric diffraction, from the ᇞθBbetween the 444 sub and 444 film reflections, we can calculate the lattice constant of the film (αfilm) if the lattice constant of the substrate (αsub) is known [in this example, Gd3Ga5O12
substrate, αsub= 12.3800 Å (cubic)]. In here, based on the θ epi =θBsub +ᇞθB and the α film=[ sin(θBsub) / sin(θepi)] • αsub simple formulas, the lattice constant of (Lu2.1,Bi0.9)Fe5O12 canevaluated using a high-resolution out-of-plane measurement.

Study on Synthesis and Luminescence Properties of
LuBO3:Ce3+

P-91

Teng-Teng Jin1, 2, Jing-Tai Zhao1 , Hao-Hong Chen1, Xin-Xin Yang1
1
Key Laboratory of Transparent and Opto-Functional Inorganic Materials of Chinese
Academy of Sciences, Shanghai Institute of Ceramics, Shanghai 200050, P.R.
China( jtzhao@mail.sic.ac.cn)
2Graduate School of Chinese Academy of Science, Beijing, 100039, P.R. China

Both calcite and vaterite phases of LuBO3:Ce3+ have been prepared through solid state
reactions. Their X-ray and UV excited luminescence properties were investigated at room
temperature. The as-obtained phosphor samples exhibit a strong and rapid near UV-blueemission, originating from the typical of the 5d→4f transitions of Ce3+. The light yield of
LuBO3:Ce3+ is much higher than that of the well-known BGO under the same conditions. The
ultra fine powder of vaterite LuBO3:Ce3+ has been synthesized by hydrothermal and sol-gel－
method. However, due to the existence of the residual OH , the luminescence properties ofthese samples are not as good as that of solid state reactions. From the standpoints ofluminescence efficiency and high density, LuBO3:Ce3+ is an attractive candidate of
scintillating material. The single crystal growth of LuBO3:Ce3+ is under further investigation.
- 163 -

AsCA’09

Poster

Fig.1.XRD patterns of LuBO3:Ce3+ samples.

Fig.2. Excitation spectra and emission spectra of
LuBO3:Ce3+ compared to BGO. calcite
structure (λex=362nm, λem=337nm) , vaterite
structure (λex=393nm, λem=366nm) .

References[1] C.Mansuy, E.Tomasella, R.Mahiou, L.Gengembre, J.Grimblot, J.M.Nedelec, Thin Solid Films 2006,
515, 666.
[2] Yanping Li, Jiahua Zhang, Xia Zhang, Yongshi Luo, Shaozhe Lu, Xinguang Ren, Xiaojun Wang,
Lingdong Sun, and Chunhua Yan, Chem. Matter. 2009, 21, 468.

P-92

Structure refinement and electron density
distribution of trehalose dihydrate and anhydarate
Kunimitsu Kataoka, Shota Hasegawa, Takumi Tajima, Takuro Kawasaki and
Ken-ichi Ohshima
Univ. of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, Japan

Trehalose dihydrate has been recently recognized to be an interesting sugar as substitutes for apart of function of water in the body of living things; an intracellular protectant or
co-protectant against harsh conditoions, permitting to survive dehydration of freezing.
Biopreservation of trehalose has been widely studied and the trehalose is much used in thehandling of proteins, because of the stabilization it provides. However, there are few reportson the crystallographic investigation for the trehalose dihydrate[1,2] and anhydrate[3]. We have,therefore, determined the crystal structure and the electron density distributions (EDD) oftrehalose diydrate and anhydrate using the single-crystal X-ray data for understanding of thestructural characteristics.
The crystal structure of trehalose dihydrate was refined with the use of single-crystal X-ray
and neutron diffraction data at room temperature and is shown in Fig. 1. Furthermore, in orderto reduce an influence of atomic displacement parameters on the structure refinement, X-ray
diffraction intensity has been measured at low temperature. The crystal structure of trehaloseanhydrate was refined with the use of single-crystal X-ray diffraction data at room
temperature and is shown in Fig. 2. All the refinement and MEM analysis were performed
for obtaining the EDDs. From these results, the covalent bonding was confirmed to exist
between the trehalose molecules and the internal water molecules about trehalose dihydrate
and trehalose molecule and trehalose molecule about trehalose anhydrate. The EDDs, thus
- 164 -

AsCA’09

Posterobtained, was compared with that calculated using peseudopotentials and a planewave basiswith the program ABINIT. Furthermore, the bond overlap population was calculated using acluster model by the DV-Xα molecular orbital calculations model clusters

Fig. 1 Crystal structure of trehalose dihydaretFig. 2 Crystal structure of trehalose anhydrate

References[1] G. M. Brown, D. C. Rohrer, B. Berking, C. A. Beevers, R. O. Gould and R. Simpson, Acta Crystallogr.
Sect. B, 28, 3145 (1972).
[2] T. Taga, M. Senma, and K. Osaki, Acta Crystallogr. Sect. B, 28, 3258 (1972). [3] G. A. Jeffrey and R.
Nanni, Carbohydrate Research, 137, 21 (1985).

A single-crystal study of hollandite-type BaxTi8O16
and hexagonal BaTiO3-x

P-93

Kunimitsu Kataoka1,2,3, Norihito Kijima1, Hiroshi Hayakawa1, Junji Akimoto1 and
Ken-ichi Ohshima2
1
AIST, 1-1-1 Higashi, Tsukuba, Ibaraki, Japan2
Univ. of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, Japan
3
Research Fellow of the Japan Society for the Promotion of Science

The reduced titanium oxides form a class of compounds that can exhibit interesting electronic
and magnetic properties such as an oxide superconductor in LiTi2O4 and asemiconductor-metal transition in Ti2O3, as well as their intriguing structure features. In the
Ba-Ti-O system, several compounds including Ti3+ are reported in the literature until now.
Hollandite-type BaxTi8O16 (x = 0.8-1.3)[1,2] are reported in three crystallographic symmetries;i) tetragonal system, ii) monoclinic system, and iii) a superstructure. On the other hand,
reduced hexagonal BaTiO3-x are reported in a compositional range of 0 < x < 0.12.[3] In thepresent study, we successfully synthesized single-crystal samples of hollandite-type BaxTi8O16
and hexagonal BaTiO3-x, and determined the crystal structures and electron density
distributions of these compounds using the single-crystal X-ray diffraction data.
BaxTi8O16 samples were synthesized at 1373 K using Fe crucibles. BaTiO3-x samples weresynthesized at 1473 K using Ti tubes. The crystal structures of BaxTi8O16 and BaTiO3-x wererefined using single-crystal X-ray diffraction data. Space group of BaxTi8O16 is determined as
I4/m with the lattice parameters of a=10.145 Å, and c=2.968 Å, whose is shown Fig. 1. Space
group of BaTiO3-x is determined as P63/mmc with the lattice parameters of a = 5.731 Å, and c= 13.989 Å, whose is shown Fig. 2.

- 165 -

AsCA’09

PosterFig. 1 Crystal structure of BaxTi8O16

Fig. 2 Crystal structure of BaTiO3-x

Acknowledgements: This research was supported by the Research Fellowship of the Japan
Society for the promotion of Science for Young Scientists (21･1415).
References[1] R. W. Cheary, Acta Crystallogr. Sect. B, 46, 599 (1990).
[2] T. Höche, P. Olhe, R. Keding, C. Rüssel, P. A. van Aken, R. Schneider, H.-J. Kleebe, X. Wang, A.
Jacobson and S. Stemmer, Philosoph. Mag., 83, 165 (2003).
[3] K. Kolodiazhnyi, A. A. Belik, S. C. Wimbush and H. Haneda, Phys. Rev., B, 77, 075103 (2008).

P-94

Ordered Arrangements of Nb Atoms in Layered
Compounds NbxTiS2
Takuro Kawasaki, Yuki Azuma, Ken-ichi Ohshima
Institute of Materials Science, University of Tsukuba, Tsukua 305-8573, Japan(Kawasaki@jb.bk.tsukuba.ac.jp)

It is well known that the transition metal disulfides MS2 have a two dimensional layered
structure, in which in-plane atoms have strong covalent bondings and that various atoms or
molecules can be intercalated between the layers due to inter-layer weak van der Waals
interaction. These intercalation compounds are of interest because of the low-dimensional
properties and because of the application as high energy density batteries and thermoelectricmaterials.
Ordered arrangements of intercalated Ti atoms in self-intercalation compounds Ti1+xS2 arereported by Moret.[1] Because of long-range and short-range ordered arrangements ofintercalated Ti atoms in the van der Waals gap layers of the compounds, superlattice reflection
and diffuse scattering different according to x were appeared in the X-ray diffraction patterns.
In the present study, the layered compounds NbxTiS2 with the nominal compositions x=0.20,
0.40, 0.60, 0.80 and 1.0 were prepared by chemical vapor transport technique using iodine asa transport gas. Electron diffraction patterns perpendicular to the c* axis were obtained for thefive specimens with the use of transmission electron microscope (JEOL JEM-2010). In
x=0.20, honeycomb-like hexagonal diffuse scattering is appeared. In x=0.40, superlatticereflections are appeared at 1/3,1/3,0, 2/3,2/3,0 and their equivalent positions. In x=0.60,
separated hexagonal diffuse scattering is appeared. In x=0.80, superlattice reflections at
1/2,1/2,0, 1/2,0,0, 0,1/2,0 and their equivalent positions are appeared. On the other hand, in
x=1.0, superlattice reflection and diffuse scattering did not appear in the diffraction pattern.
These revealed that the in-plane arrangements of intercalated Nb atoms are different
according to the composition x in the compounds. The diffraction pattern of x=0.20 and the- 166 -

AsCA’09

Posterschematic drawing are shown below. Further, from the result of X-ray diffraction
measurements it is expected that stacking sequences of TiS2 layer in the compounds aredifferent from the sequence of pure 1T-type TiS2.
010

000

100

Electron diffraction pattern of Nb0.20TiS2

Reference
R. Moret, M. Huber, and R. Comes: Journal De Physique. 38 (1977) C7-202.

P-95

Structure Analysis of CaMoO4 using Energy-filtered
Precession Electron Diffraction
Jin-Gyu Kim, Sung-Woo Lee, Kyung Song, Youn-Joong Kim
Korea Basic Science Institute, 52 Eoeun-dong, Yuseong-gu, Daejeon, 305-333, Korea(jjintta@kbsi.re.kr)

Although X-ray crystallography is very useful for the structure analysis of large single orpowder crystals (> 1 micron), there are several limitations for application to nano-crystalline
materials. Electron diffraction is a more adequate method for structure determination in cases
where X-ray diffraction is not applicable, such as multi-phase or nanometer-sized powders
because of its higher interaction between electron and specimen. The dynamical effect ofelectron interaction, however, is the most serious problem for structure solving by electron
diffraction. As a solution for this problem, the electron precession technique, first developed
by Vincent and Midgley, is very useful to get intensities of electron diffraction reflections
closer to kinematical characters [1].
Our electron precession unit, ‘SPINNING STAR’, was installed in Carl-Zeiss EM912 Ω(120kV, Ω Energy-Filter). To apply the precession technique for determining the crystal
structure of CaMoO4, we have calibrated and evaluated several parameters, such as precession
semi-angle (φ), Rov (usable diffraction radius), specimen thickness. First, precession
semi-angle depends on the maximum beam tilt angle and objective lens type of electron
microscope. In case of our precession system, we can use the precession angle up to ~ 2.9
degree. Second, Rov is related to the wavelength of source and cell parameters of specimen.
The lattice length of specimen should be smaller than 16 Å in our TEM (Transmission
Electron Microscope). We experienced that it is possible to obtain quasi-kinematical
diffraction data for thicker sample of a about 100 nm using precession technique.
We have performed the structure analysis of CaMoO4 by using conventional SAED (Selected
Area Electron Diffraction), PED (Precession Electron Diffraction), and EF-PED- 167 -

AsCA’09

Poster(Energy-Filtered Precession Electron Diffraction). All PED patterns were acquired at
precession angle of 2.7 degree and EF-PED patterns were obtained with 15 eV and 30 eV ofslit widths for zero-loss and plasmon-loss filtering, respectively. As a result, EF-PED method
turned out to be advantages for determining crystal structures and accurate cell parameters of
CaMoO4 crystal structure due to resolution enhancement, shaper peak shape as well as
reducing inelastic scattering effect.

Fig. 1. Four different electron diffraction patterns for [110] zone axis of CaMoO4 crystal: a) SAED pattern,b) PED pattern, c) Zero-loss filtered PED pattern, d) Plasmon-loss filtered PED pattern.

Reference
R. Vincent, P.A. Midgley, Ultramicroscopy 53 (1994) 271-282

Intermolecular interactions in two halogenated
Imidazo [2,1-b] [1,3,4] thiadiazole derivatives

P-96

M K Kokila1, G N AnilKumar2, Puttaraja1, S. S. Karki,3 R. Vinayakumar,3 S.
Kumar3,
1
Department of Physics, Bangalore University, Bangalore-560056, India(drmkkokila@hotmail.com)
2
Department of Physics, M S Ramaiah Institute of Technology, MSRIT Post,
Bangalore-560054, India, (anilkumargn@gmail.com)
3
Department of Pharmaceutical Chemistry and Pharmacology, KLES College of
Pharmacy, 2nd Block, Rajajinagar, Bangalore 560 010, India.
( subhasskarki@gmail.com)

Imidazo[2,1-b][1,3,4]thiadiazole with aryl substituted derivatives have been of interest to the
medicinal chemists for many years because of their anticancer, antitubercular, antibacterial,
antifungal, anticonvulsant, analgesic and antisecretary activities. Because theimidazo[2,1-b][1,3,4]thiadiazoles system is bioisosteric with imidazo[2,1-b]thiazole ringpresent in the well known immunomodulator. Recently in crystal engineering the study ofinteractions involving halogens, particularly fluorine is of major interest. Conventionalhydrogen bonding is the significant interaction in many crystal structures but weakinteractions involving halogens are of great importance. In the present study, we haveanalyzed the crystal and molecular structures of two Imidazo[2,1-b][1,3,4]thiadiazole
derivatives with pharmacophoric substituents involving halogens such as bromine andfluorine with an intention of understanding the role of these halogens in stabilizing crystal
structures.
Crystal structures of two compounds 2-benzyl-5-bromo-6-(4-fluorophenyl) imidazo [2,1-b][1,3,4] thiadiazole(I), and2-benzyl-5-bromo-6-(4-methylphenyl)imidazo[2,1-b] [1,3,4]- 168 -

AsCA’09

Posterthiadiazole(II) were determined. It has been found that compound (I) crystallizes under
Orthorhombic system, Pbca space group where as (II) crystallized under Monoclinic P21/c
spacegroup. In crystal packing of (I) is stabilized only by a number of C – H … pi interactions.
A weak C – H … F interaction is also observed between the molecules. In (II) in addition to C
– H …pi interaction there is also a rare C – Br …pi interaction that stabilized the molecular
structure. A detailed discussion of packing & experimental results will be presented.

Crystal and molecular structure of 2-amino-N(2-furylmethyl) -5,6-dihydro-4H-cyclopenta[b]thiophene-3-carboxamide’P-97

M K Kokila1, K. Chandra Kumar2, Puttaraja1, S. Mohan3 and J. Saravanan3
1
Department of Physics, Bangalore University, Bangalore-560056, India(drmkkokila@gmail.com)
2
Department of Engineering Physics, HKBK College of Engineering, Nagawara, Arabic
College Post, Bangalore, Karnataka, 560045, India (chandru_mhk@rediffmail.com)
3
PES College of Pharmacy, Hanumanthanagar, Bangalore, Karnataka, 560050, India.

Thiophenes and their related derivatives containing amino and carboxyl functions have beenfound to exhibit broad spectrum of biological activities such as antiviral, antiinflammatory
and antimicrobial activities. Specifically, 2-aminothiophene -3-carboxylates andcarboxamides were recognized as allosteric enhancers for A1 adenosine receptors. In view of
the
above
crystalstructureof‘2-amino-N-(2-furylmethyl)-5,6-dihydro-4Hcyclopenta[b]thiophene-3-carboxamide’ has been presented.
The compound C13H14N2O2S, crystallizes under Monoclinic system, C2/c, space group, a= 21.6939(24) Å, b = 9.8547(11)Å, c = 15.1162(16) Å, β = 131.661(2)º, V = 2414.33(58) Å3,
Z = 8, D = 1.44 Mg m−3. The data of the compound were corrected for LP factors and used forthe structure solution. The structure was solved by direct methods using SIR92 program andrefined using full matrix least squares on F2 to an R value of 0.043 using SHELXL-97
program. The crystal is stabilized by intermolecular N – H … O and C – H … O hydrogenbonds.

Structures of bioactive compounds: substituted,3,2–benzoxazaphosphinine derivatives

P-98

Krishnaiah . M¹ , Surendra Babu .V.H.H¹and Vedavathi G.Puranik²¹ Department of Physics,Sri venkateswara University, Tirupati, 517502 India(profkrishnaiah.m@gmail.com)² Centre for Material Characterization,National Chemical Laboratory,Pune, 411008
India (vg.puranik@ncl.res.in)

The phosphorus heterocycles have recently attracted considerable attention owing to theirunique physicochemical and potential biological properties. The oxazaphosphorine ringsystem bearing PO and PN units such as cyclophosmaide and its derivatives are known to be
antitumor agents.
The

molecular

structuresof

6-Bromo-3-(4-chlorophenyl)-2-(4-methoxyphenyl)-3,4- 169 -AsCA’09

Posterdihydro-1,3,2-benzoxazaphosphinine
2-sulfide[1],3-(3-Chloro-4-fluorophenyl)-2(2-chlorophenoxy)-3,4-dihydro-2H-1,3,2-benzoxazaphosphorine
2-oxide[2]and2-4(-nitrophenoxy)-3,4-dihydro-6-bromo-3(1-phenylethyl)-2H-[1,3,2] benzoxazaphosphorine 2 –oxide[3] have been determined to study the effect of the substituents on heterocyclic moiety
and their biological activity.
The six membered oxazaphosphinine ring exhibits a boat conformation with S atom in axial
position in [1], a screw boat with phosphoryl O atom in axial position in [2] and a twist boatwith phosphoryl O atom in equatorial position

[1]

[2]

[3]

All the compounds show significant antimicrobial and insecticidalactivity. It has been seenthat the phosphoninine group is responsible for this biological activity. The changes inconformation of the phosphoninine moiety and its effect on the activity will be discussed.

P-99

Critical evolution of surface morphology of Quartz(001) surface on alpha-incommensurate-beta
structural phase transitions
Tsuyoshi Kumagai, Chibon Hyon, Yoshiki Ueno, Hikaru Terauchi and Isao
Takahashi
Faculty of Science and Technology, Kwansei Gakuin University, Sanda 6691337, Japan(avl22854@kwansei.ac.jp)

SiO2 is a ubiquitous material in the lithosphere and known to exhibit isomorphism under hightemperature and pressure. Especially, structural phase transition between alpha quartz andbeta quartz has attracted great attention for the decades owing to its reversibility and peculiar
triangular domain structure (Dauphine twins) forming in alpha phase on cooling fromhexagonal beta phase. Group theoretical considerations had predicted an incommensurate (IC)phase as an additional intermediate phase, subsequently confirmed. It is not surprising not tobe reported till then, if relatively high transition temperature (Tc = 846 K) and narrowtemperature range of the IC phase (ca. 1.3 K) are recalled. Although there are a lot of
dielectric materials showing the Normal - IC – Commensurate (N-IC-C) phase successive
phase transitions, we must regard quartz as a unique substance in which instability of acoustic
phonon slightly away from the Gamma point in reciprocal space constructed by hexagonal
symmetry plays an crucial role in developing the IC structure and responsible for the
Dauphine twins formation. In spite of the understandings and amount of our knowledge onbulk structure on N-IC-C phase transitions, we must admit that less is known for surface
structure and surface morphology when it undergoes the successive phase transitions. In the- 170 -

AsCA’09

Posterpresent study, we investigated the surface structure of quartz with surface-sensitive-X-ray
diffractions so as to give a novel insight into this phase transitions.
Sample was a (001) plane of synthesized quartz polished at room temperature with dimensionof 20 mm x 20 mm x 1.5 mm. It was placed into a heater with a PID temperature controller
mounted on an X-ray diffractometer (SmartLab, Rigaku). Sample temperature was controlled
between room temperature and 950 K with a stability of 0.5 K where the sample was kept inair. Surface-sensitive X-ray diffractions we exploited were crystal truncation rod (CTR)
scattering emanating from the 003 Bragg point and X-ray reflectivity (XR). Rocking curves(qx scan) and longitudinal curves (qz scan) of XR in 2theta range between 0 and 5-8 degrees
were collected at each temperature.
In the alpha phase, a noticeable increase in width of specular XR (qx scan) beyond the totalreflection regime is reproducibly observed as the sample temperature T approaches Tc.
Furthermore, specular XR in total reflection regime also shows an anomalous decrease inintensity. Both anomalies can well be fitted by C/(Tc – T), indicating that the variation of
surface morphology in alpha phase does accompany some critical features.

Synchrotron radiation X-ray characterization of
epitaxial magnetic multilayers of yttrium irongarnet/gadolinium gallium garnet

P-100

Chih-Hao Lee1,2, K.S. Laing2, and M.Y. Chern3
1. Department of Engineering and System Science, National Tsing Hua University,
Hsinchu, Taiwan. (chlee@mx.nthu.edu.tw)
2. National Synchrotron Radiation Research Center, Hsinchu, Taiwan(kslaing@nsrrc.org.tw)
3. Department Physics, National Taiwan University, Taipei, Taiwan.
(mychern@phys.ntu.edu.tw)

Epitaxial magnetic multilayers of yttrium iron garnet/gadolinium gallium garnet(YIG(111)/GGG(111)) on GGG single crystal substrates using the laser ablation deposition
method. In this work, X-ray reflectivity, in-plane and plane normal diffraction and truncation
rod measurements were carried out to characterize in detail the epitaxial relations of themultilayer, noting that both YIG and GGG have the same cubic structure with a nearly
identical lattice constant (0.03% difference). The perfection of the epitaxy can be best
revealed in the observation of the in-plane forbidden (1-10) peak and truncation rod
measurement. The reflectivity curves show the surface roughness is small than 1 nm. The
longitudinal diffuse scattering curve as functions of two theta angle show the same pattern ofoscillation as specular reflection, which indicates the thin film is in good conformation
relation on each layer for the sample of YIG/GGG multilayer. The measurable intensity of
the forbidden in-plane peak, YIG or GGG, indicates that the structure of the YIG/GGG
epitaxial film was slightly deformed. The truncation rod profile of (YIG(1)/GGG(1))12 showsa diffraction intensity of the superperiod of the sample which reveals a good in-plane solid on
solid epitaxial relation.

- 171 -

AsCA’09

PosterStudy on Simulation and Preparation of Spherical
Diamond Film

P-101

Duosheng Li1, Xianliang Zhou1, Dunwen Zuo2 , Xiaozhen Hua1
1
College of Material Science and Engineering , Nanchang Hangkong University,
Nanchang 330034, China (ldsnuaa@nuaa.edu.cn)
2College of Mechanical and Electrical Engineering , Nanjing University of Aeronautics
and Astronautics, Nanjing 210016, China

Spherical diamond film has some excellent properties and is a good candidate for some
applications[1-3]. FEM is a good method to simulate the fluid and temperature field of film.
Velocity, pressure and temperature fields of reaction chamber were simulated by FLUENT.
Spherical diamond film was prepared on convex Mo substrate by DCPCVD, Internal quality
and surface morphology were investigated by scanning electron microscopy (SEM), Raman
spectroscopy. The total pressure was 46 Torr, and CH4 concentration was about 1.6%, andsubstrate temperature was about 1150K.The velocity, pressure and temperature fields ofsimulation are shown in Fig.1, Fig.2 and Fig.3 respectively.

Fig.1 Velocity field of DC plasma

Fig.2 Pressure field of DC plasma

Fig.3 Temperature field of DC plasma

Fig.1 shows that plasma velocity field from the exit of anode nozzle was uniform. But thevelocity field of near convex Mo substrate was not uniform, and it was much lower in centernear substrate than that of the edge of substrate. Fig.2 shows that plasma velocity field
fluctuates above spherical substrate, in center of plasma, the pressure is the biggest, and it
tends to decrease with increasing of radius of the plasma，which is harmful to prepare highquality spherical diamond film. Fig.3 shows that there is a uniform temperature field on thesubstrate. It is necessary to successfully prepare spherical diamond film.
SEM micrographs of diamond films are shown in Fig.4 (a), (b) respectively.

40 60 802θ/degrees

100

Intensity/a.u.

Intensity/a.u.

21
m
0c
0/
6r
1e
b
0m
0u
2n
1e
v
0a
0W
8
0
0
0
0
1

20

(311)

0
0
0
0
2

(220)

0
0
0
0
3

(b)

0
0
0
0
4

(a)

(111)

2500
2000
1500
1000
500
0

Fig.4. SEM of diamond film: (a) surface, (b) cross-section Fig.5. XRD of diamond film Fig.6. Raman of diamond film

Fig.4 (a) shows that the grain of spherical diamond film is uniform, compact. There were notnon-diamond inclusions, and there are also not remarkable bigger gains in the film. Fig.4 (b)indicated that the columnar structure grains keep their columnar growth direction from thesubstrate surface to the growth surface. An average size of diamond crystal was about
15μm.Diamond (111), (220) and (311) peaks were found in Fig.5 by XRD, thus, diamond film
is polycrystalline and (111) faces of diamond film are dominant. Fig.6. shows there is a sharp- 172 -

AsCA’09

Posterdiamond characteristic peak at 1332.0 cm-1 with FWHM, and characteristic peaks ofpolycrystalline graphite and amorphous graphite were not obviously observed. Thus, highquality spherical diamond film was prepared.
References[1] Paul W. May, MATERIALS SCIENCE: The New Diamond Age, Science. 2008, 319(14), 1490
[2] D.S. Li, D.W. Zuo, R.F. Chen, Solid State Ionics, 179(2008), 1263
[3] I. Vlasov, O. I. Lebedev, V. G. Ralchenko, Advanced Materials, 2007, 19(22), 4058

The Topological Analysis of Minerals

P-102

Li Jia-Ju1 Li Hui2
1
Institute of Geology and Geophysics Chinese Academy of Sciences Beijing 100029
1
Shimadzu International Trading(Shanghai) Co. Limited Beijing Branch 100022(lijiaju_1@yahoo.com.cn) (bsljj@shimadzu.com.cn)
2
Beijing University of Technology, Beijing 100124 (huilicn@yahoo.com)

The electron density distribution of Pyrite and Pyrrhotite were reconstructed with powder
X-ray diffraction data in this research work. Meanwhile, the gradient of charge density and its
Laplacian were also supplied. With these results, it shows obviously that the characters ofbond critical points of Fe-S bond in these two minerals are different. This difference
represented the bond type of Fe-S in Pyrite and Pyrrhotite and its characters of physics andchemistry.

Fig. 1 The electron density of Pyrite (1-10) plane (Left) and Pyrrhotite (110) plane (Right). The charge
density grids range from 0.2e/Å3 to 3.0e/Å 3 intervals 0.05e/Å 3. The charge densities in bond critical points(Arrow) of Pyrite and Pyrrhotite are 0.335e/Å 3 and 0.25e/Å 3 respectively.

Fig. 2 The gradient of electron density of Pyrite (1-10) plane (Left) and Pyrrhotite (110) plane (Right). The
grids range from 0.0e/Å4 to 5.0e/Å4 intervals 0.2e/Å4. The gradient of electron density in bond criticalpoints (Arrow) of Pyrite and Pyrrhotite equals to 0.0e/Å4.
- 173 -

AsCA’09

PosterFig. 3 The Laplacian of Pyrite (1-10) plane (Left) and Pyrrhotite (110) plane (Right). The grids range from
-2.0e/Å3 to 6.0e/Å5 intervals 0.2e/Å5. The Laplacian in bond critical points (Arrow) of Pyrite and Pyrrhotite
are 5.4e/Å5 and 2.0e/Å5 respectively.

The electron density, gradient electron density and Laplacian distribution of Pyrite (1-10)
plane and Pyrrhotite (110) plane show that the electron density values in BCP(bond criticalpoint) are ρ(rc)ED = 0.335, 0.25e/A3, ▽ρ(rc)GRD = 0.0, 0.0e/A4 and ▽ 2ρ(rc)Lap = 5.4,
2.0e/A5 respectively. The values of ρ(rc)ED for pyrite are higher than pyrrhotite. This means
the bond strength of pyrite is higher and more stable than pyrrhotite. The bond length of Fe-S
in pyrite and pyrrhotite are 2.259Å and 2.451Å respectively. It is well known, the pyrite isharder, more difficult to be oxidized and semi-conductance as germanium and diamond, while
pyrrhotite having good conductibility, magnetism, easier to be oxidized and its hardness islower.
References
1. G..V. Gibbs, R.T. Downs, D.F. Cox, et al., Z. Kristallogr., 2008, 223, 1-40.
2. K. Momma, F, Izumi, J. Appl. Cryst.., 2008, 41, 653.

P-103

XC6012 from Xanthomonas campestris Adopts a
Novel Tetrameric PilZ Domain Structure Stabilized bya Central Parallel Four-Stranded Coiled-Coil
Tso-Ning Li1, Ko-Hsin Chin1, Andrew H.-J. Wang2 & Shan-Ho Chou1, 31Institute of Biochemistry, National Chung-Hsing University, Taichung, 40227, Taiwan
2
Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan
3
National Chung Hsing University Biotechnology Center, Taichung, 40227, Taiwan,(shchou@nchu.edu.tw)

Cyclic di-GMP (c-di-GMP) has emerged as an important secondary messenger, controlling avariety of cellular processes, mainly in biogenesis of extracellular components, flagella andpili, and exopolysaccharide synthesis in diverse bacteria. It is proposed to be a key regulator
in bacterial evolution, during its transition from a single-cellular and motile entity to a
multicellular and sessile entity. PilZ domain is found to be one of the key receptors for thisimportant second messenger. Currently, many such PilZ domain-containing proteins havebeen identified, and several tertiary structures of PilZ domains capable of binding c-di-GMP
with strong affinity have been determined. These include the receptor protein PA4608 from
Pseudomonas aeruoginosa (1YWU) that was determined by NMR method, and the receptor
proteins VCA0042 from Vibrio cholerae O1 (1YLN) and PP4397 from Pseudomonas putida- 174 -

AsCA’09

Poster

KT2440 (2GJG) that were determined by X-ray crystallography. A co-crystal structure of the
PilZ/c-di-GMP complex from Vibrio cholerae has also been reported (2RDE), providing morestructural insights into the allosteric conformational changes triggered by the c-di-GMP
binding. However, not every one of them can bind c-di-GMP tightly. PA2960 from
Pseudomonas aeruginosa is one of such sequences, and is a protein required for type IV
pilus-mediated twitching motility. However, it lacks a c-di-GMP switch loop, and theessential residues in the D/NxSxxG signature sequence required for c-di-GMP binding. It has
therefore been suggested that PA2960 may represent an inactive form of the PilZ domain, or
needs accessory protein domains such as PilZNR or PilZN to stabilize the bound c-di-GMP.
There are thus more studies necessary to fully understand how these different PilZ domains
interact with their receptors.
Xanthomonas campestris pv. Campestris genome was found to contain four PilZ
domain-containing proteins (Xc0965, Xc2249, Xc2317, and Xc3221). Mutations of Xc2249
were found to lead to a significant reduction in the virulence of Chinese radish, a reduction in
mobility, and the extracellular enzyme production. To better understand the pathogenic effectof Xc2249, we have used X-ray crystallography to determine the crystal structure of the
Xc2249 homolog, XC6012 from Xanthomonas campestris. The final results indicate that it
adopts a novel tetrameric PilZ-domain structure stabilized by a central parallel four-stranded
coiled-coil, with the four PilZ domains pointing outward. Interestingly, the c-di-GMP
signature motif for XC6012 is again only partially fulfilled, indicating it may need othercofactors to perform its functions.
References
Mccarthy Y, Ryan RP, O'donovan K, He Y-Q, Jiang B-L, Feng J-X, Tang J-L, Dow J. M. The role of PilZ
domain proteins in the virulence of Xanthomonas campestris pv. campestris. Molecular Plant Pathology
2008;9:819-824.

New palladium-containing skutterudites
BaPd4SnxSb12-x

P-104

Ying Liang1, 2, Horst Borrmann1, Walter Schnelle1, Jing-Tai Zhao2 and Yuri Grin1
1
Max-Planck-Institut für Chemische Physik fester Stoffe, Nöthnitzerstr. 40, 01187
Dresden, Germany(yliang@cpfs.mpg.de)2
State Key Lab of High Performance Ceramics and Superfine Microstructures,
Shanghai Institute of Ceramics, Chinese Academic of Sciences, Dingxi Road 1295,
Shanghai 200050, P.R.China(jtzhao@mail.sic.ac.cn)

A new skutterudite BaPd4SnxSb12-x has been synthesized and characterized. The lattice
parameter refinement and the WDX analyses revealed a wide range of homogeneity for 2 ≤x ≤ 7. It is evident by the single crystal X-ray diffraction that the Sn and Sb atoms in
random distribution share the framework site with different coordinate parameters caused by
the difference in atomic size. The thermal electrical properties vary evidently with thetin-to-antimony ration.

- 175 -

AsCA’09

PosterFigure 1. The crystal structure of BaPd4Sn7.3Sb4.9.
The palladium atoms (dark gray ball) are octahedrally
coordinated by Sn/Sb atoms (light gray balls). The
barium atoms (white ball) are icohedrally coordinatedby 8 Pd atoms and 12 Sn/Sb atoms.
Table 1. Composition and lattice parameters of BaPd4SnxSb12-x

P-105

Starting Composition
BaPd4Sn7.3Sb4.9(crystal refinement)
BaPd4Sn6.0Sb6.0
BaPd4Sn5.5Sb6.5
BaPd4Sn5.0Sb7.0
BaPd4Sn4.0Sb8.0

Lattice parameter (Å)

BaPd4Sn3.0Sb9.0

9.4500(8)BaPd4Sn2.0Sb10.0

9.4626(4)9.4139(2)9.4165(7)9.4202(2)9.4246(2)9.4395(8)Preparation and Characterization of Ammonium
Polyphosphate with Crystal Form-V
Xinchun Liu, Wenyan Chen, Gousheng Liu
Engineering Research Center of Resources Process Engineering, Ministry of Education.
East China University of Science and Technology, Shanghai 200237, China(gsliu@ecust.edu.cn)

As halogen-free and intumescent flame retardant, ammonium polyphosphate (APP) has been
extensively applied in the field of flame retardant materials in recent decades. In the six
different kinds of crystal forms from form-I to form-VI, more attentions have been paid toform-I and form-II at home and abroad. Except form-I and form-II, form-V APP has betterstability. Until now, less study has been found for APP with crystal form-V.
In this study, APP with crystal form-V has been prepared. Ammonium phosphate is the main
raw material, urea is the condensing agent. The two chemicals are mixed, heated and melted
at high temperature under a dry ammonia atmosphere. Some effects, such as chemical ratio,
heating temperature, time of heating and condensing, flow and pressure of dry ammonia
atmosphere are investigated. Structural characterization of prepared product is carried out
through XRD, SEM, and IR. Compared with the patterns of industrial-grade APP with crystal
form-I, form-II, form-V and cited from literature, it is identified that the prep ared product is
APP with crystal form-V. The optimal conditions are:n(ammonium phosphatesalt):n(CO(NH2)2 ）=1:1, thermal melting temperature 360~380℃, thermal melting time
50~60min, ammonia flow 1.2~1.5L/min, ammonia pressure 0.02~0.04Mpa and sustain 1h
under such atmosphere.
Keywords: Ammonium polyphosphate, XRD, Structural characterization, Different crystal
forms- 176 -

AsCA’09

Poster

XRD spectra of prepared product and cited in literature

References[1]Watanabe Makoto. Production of V type of Ammonium Polyphosphate[P]. JP 09235110，1997[2]C. Y. Shen, et al. Preparation and Characterization of crystalline of long chain Ammonium
Polyphosphates[J]. Am. Chem. Soc.1969, 91(1): 62~67

Acid-base approach to Valproic acid co-crystal andthe crystal structure analysis

P-106

Takashi Miyamoto1, Akiko Sekine1, Hidehiro Uekusa1, Etsuo Yonemochi2,
Katsuhide Terada2
1
Tokyo Institute of Technology, Japanese, 2-12-1, Oookayama, Meguro-ku, Tokyo,152-8551, JAPAN (miyamoto.t.aa@m.titech.ac.jp)
2Toho University, 2-2-1 Miyama, Funabashi-shi, Chiba, 274-8510, JAPAN

Valproic acid (2-n-Propylpentanoic acid, Fig.1) is used as an antiepilepsy drug. It is liquid in
the ambient temperature and also its sodium salt has strong higroscopicity. In order tocontrol the hygroscopic properties, organic salt co-crystal formation of valproic acid withorganic base molecule would be an effective strategy. In this study, this kind of acid-baseapproach was examined and the crystal structures of valproic acid and organic base co-crystal
were analyzed.
Through co-crystal screening experiments based on co-grinding method, co-crystal of
valproic acid with 2-amino-3-hydroxypyridine (Fig.1) was successfully formed. The single
crystal was obtained by recrystallization from methanol solution of equimolar amounts
mixture. The X-ray structure analysis showed that it crystallized in the monoclinic spacegroup P21/c with cell parameters a = 12.2783(2), b =12.6185(2), c = 18.3943(3) Å and β=92.711(1)°. The asymmetric unit contains two valproic acids and two 2-amino3-hydroxy-pyridine molecules. The major difference of two valproic acids is theconformation of propyl groups. Amino pyridine group and carboxylic group form a [R22(8)]heterosynthon via two N-H…O hydrogen bondings. Actually, charge interactions by the
proton transfer from carboxylic acid to pyridine were observed. Also, each carboxylic
oxygen atom forms hydrogen bond with the amino proton of a neighboring molecule. These
hydrogen bonds form zigzag chains of valproate and 2-amino-3-hydroxypyridium ions along
the a-direction (Fig.2). The chains are connected via hydroxyl OH…O hydrogen bonds toconstruct whole crystal structure.
- 177 -

AsCA’09

PosterHydrogen-bonded Network in Quaternary Ammonium
Salts Used as Charge Control Agents

P-107

Jin Mizuguchi1, Kazuya Uta1, Yohei Sato1, Osamu Yamate2
1
Graduate School of Engineering, Yokohama National University, 79-5 Tokiwadai,
Hodogaya-ku, 240-8501 Yokohama, Japan (mizu-j@ynu.ac.jp)
2
Orient Chemical Industries, Ltd., 541-0057 Osaka, Japan

We have previously investigated the origin of the unusual high thermal stability ofbenzyltributylammonium-4-hydroxynaphthalene-1-sulfonate used as a charge control agent(P-51: Orient Chemical Industries, Ltd.) from the standpoint of the X-ray structure analysis.
In anions of P-51, we found chains of OH…O intermolecular hydrogen-bonds between the OH
group of one anion and the sulfonate O atom of the neighboring one. The present
hydrogen-bond network is found to impart a polymer-like stability to P-51. In the present
investigation, we extended our studies to seven derivatives of P-51, in which the cation
remains the same while the anion part is modified. Among these, five derivatives are solid andpossess various OH…O hydrogen-bond networks in anions: dimer, or one-dimensional, or
two-dimensional network. These results lead us to conclude that the hydrogen-bond network
is responsible for the high thermal stability of P-51 derivatives. On the other hand, theremaining two derivatives are found to be liquid at room temperature, probably because of thelack of intermolecular hydrogen bonds.
SO3-

C4H9
C4H9

N

CH2

C4H9

OH

Structure of P-51

Molecular arrangement of P-51

- 178 -

AsCA’09

P-108

Poster

Suppression of Pseudo-polymorphs by High
Temperature Crystallization: Case Study of Oleanic
Acid
Thanh-ha Nguyen1, Alvin W-H. Siu1,Herman H-Y. Sung1, Henry H-Y. Tong2, Ian D.
Williams1
1
Department of Chemistry, Hong Kong University of Science and Technology, Clear
Water Bay, Kowloon, Hong Kong, China (chwill@ust.hk)
2
Macao Polytechnic Institute, Macau, China

Oleanic acid (C30H48O3) is a common chiral triterpenoid natural product found in certain
Traditional Chinese Medicinal sources and, together with its derivatives, is of growing
importance for treatment of a variety of ailments. It has low aqueous solubility, but can berecrystallized from many organic solvents. Commercial
sources of the parent compound give a powder
diffractogram consistent with a methanol solvate, which
may be prepared from hot MeOH. A non-solvated form
can be obtained from hot acetonitrile or acetone, whilst
various alcohols yield different pseudo-polymorphs,
containing the alcohol or water, several of which we havestructurally characterized by single crystal diffraction. Useof solvothermal conditions, in which crystallization occurs at higher temperatures can lead tosuppression of the various alcoholic pseudo-polymorphs and directly yield the non-solvatedphase. The driving force behind this phenomenon, which is important for pharmaceuticalprocessing, is the relative instability of pseudo-polymorphs at higher temperatures due to theincreasing loss of entropy due to the trapped solvate molecules.
Acknowledgements: We are grateful to RGCHK and HKUST (RPC07/08.SCI17) for financial
support.

Measurement using multiple diffraction with
four-circle diffractometer

P-109

Koji Okada1, Kiyoaki Tanaka1, Yasuyuki Takenaka2, Isao Kagomiya1
1
Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya, Japan( Tanaka.kiyoaki@nitech.ac.jp)
2
Hokkaidou University of Education, 1-2 Hachiman-cho Hakodata, Hokkaido, Japan,(bow@bussei.hak.hokkyodai.ac.jp)

Introduction Multiple diffraction (MD) is a phenomenon observed when two or more
reciprocal lattice points meet the diffraction requirement at the same time. We call thereflection being measured as the primary reflection(H1) and the remaining one as thesecondary reflection(H2). By rotating the crystal around the scattering vector (ψ-rotation) of
the primary reflection, the condition for MD to occur is surely fulfilled. In the present study afour-circle diffractometer equipped with the APD detector installed at PF14A was used. The
Ψ-angles for large multiple diffraction (weakly primary beam and strong secondary beam) are
observed for several primary reflections. Then the UB-matrix(1) were calculated by aleast-squares method minimizing the sum of the differences between observed and calculated- 179 -

AsCA’09

Posterpsi-angles. In the present presentation the basic relationships and experimental results will bepresented.
Calculate psi-angle H2 is rotated around H1 (Ψ-rotation) and is expressed as function of Ψ,
H2(Ψ). When H1 is on the reflection sphere with ω-2θ setting, which defines Ψ=0, thereciprocal point of H2(0) locates at P0 in Fig. 1. Then H2(0) is rotated around H1 by Ψ1 and Ψ2and cross the reflection sphere at P1 and P2, respectively. It also crosses the horizontal plane(x-y and x’-y’ plane) at P0’ after the rotation Ψ0. Since the absolute value of the Ψ-angles
from P0’ to P1 and P2 are equal to Ψ’, Ψ1 = Ψ0 + Ψ’ and Ψ2 = Ψ0 － Ψ’. By using therelation that P1 and P2 are on the reflection, Ψ’, H1 and H2 fulfill the following equation:cosΨ’ = tan(θ1)・（H21・H2）/ |H1×H2| , where H21=H1-H2, θ1 is the Bragg angle of H1. The
four angles for two reflections H1 and H2 to fulfill the diffraction condition simultaneously
are easily evaluated from eq. (1).
Experimental The four-angles (Ψ-angle) are measured experimentally about single crystalof Fe3O4 at PF14A and compared with those calculated by the above equation. Though thepeak width is very narrow, significant differences were found for 25 pairs indicating the
crystal orientation determined experimentally can be improved by utilizing the multiple
diffraction.

Fig.1. H2(Ψ) with Ψ-rotation makes a circular cone and crosses reflection sphere

References
William R. Busing and Henri A. Levy (1967). Acta Cryst. 22, 457.

P-110

Electronic spectra of the 1:1 rhodamine B base with
ethyl gallate in solution and in the solid state
Kazuyuki Sato, Hideki Shima, Jin Mizuguchi
Graduate School of Engineering, Yokohama National University, 79-5 Tokiwadai,
Hodogaya-ku, 240-8501, Yokohama, Japan (d07sd201@ynu.ac.jp)

The electronic spectra of the 1:1 rhodamine B base (RBB: leuco dye) with ethyl gallate (EG:developer) have been studied in solution and in the solid state (i.e. in spin-coated films and insingle crystals) on the basis of the crystal structure analysis. There are two crystalline phasesin the 1:1 “RBB/EG” colorant at low (93 K) and room temperatures. In solution, themaximum color intensity occurs with the 1:1 molar ratio of RBB with HCl, giving an- 180 -

AsCA’09

Posterabsorption band at about 556 nm. In the solid state of spin-coated RBB/EG layers, anabsorption band appears around 577 nm due to the ring opening caused by the hydrogen-bondformation between RBB and EG. However, the color intensity is found to be limited to about
80% of the maximum available value. This has been attributed to a residual fraction of RBB
molecules whose lactone-ring is still closed due to steric hindrance. In addition, the polarizedreflection spectra measured on single crystals of RBB/EG exhibit a drastically different
spectrum (i.e. absorption maximum: about 480 nm) from that of spin-coated films of theamorphous state. This suggests that strong excitonic interactions of the H-aggregate type areoperative in single crystals of RBB/EG that displace significantly the absorption band toward
shorter wavelengths.

Schematic illustration of the molecularconformation: (a) 93 K and (b) RT.
Polarized reflection spectra together withsolution spectrum measured on the (010) planeof RBB/EG single crystals.

Crystal Structures and Photochromism of Indandione
derivatives

P-111

Akiko Sekine1, Yuji Karakane1, Hidehiro Uekusa1, Masashi Yokoyama2, Yuki
Nakai2, Koichi Tanaka2
1
Department of Chemistry and Materials Science, Tokyo Institute of Technology, Tokyo,152-8551, Japan (asekine@chem.titech.ac.jp)
2
Department of Life Science and Biotechnology, Kansai University, Osaka, 564-8680,
Japan

It has been reported that trans-biindenylidenedione derivatives show photochromism in thesolid state as evidenced by color change, from yellow to red, upon irradiation with UV andvisible light [1].
The direct observation of the photoproduct and photoreactant by the single crystal X-ray
analysis revealed that the photochromic reaction was caused by a Norrish Type II
intra-molecular hydrogen transfer.
Recently, new indandione derivatives that have related skeleton to trans-biindenylidenedione
were synthesized and found to show photochromic reaction. In this paper, we investigated therelationship between crystal structure and photochromic mechanism.
- 181 -

AsCA’09

PosterFive indandione derivatives (Fig.1) have different sizes of cycloalkanes (five- (3,4), six- (1,2),
and seven- (5) membered ring) to modify the intra- and inter-molecular configuration.
Among them, crystals of 1, 2, and 5 showed photochromism (yellow to orange, colorless todark green, and colorless to green, respectively) by the photo-irradiation (>300nm) and the
ESR signals were observed.
On the other hand, for both 3 and 4, the photochromism and the ESR signals were notobserved. The crystal structure analysis shows that there are no strong intermolecularinteractions in crystals of 1-5. The observed ESR signals indicated the mechanism would bea hydrogen subtraction by carbonyl oxygen, so the nearest H…O distances were examined.
For 1, 2 and 5 crystals which show photochromism, the distances were 2.283(2)Å, 2.222(2)Å,and 2.221(2)Å. However, for 3 and 4 crystals which doesn’t show the photochromism, thedistance were between 2.601(2)Å and 2.9682(2)Å which are significantly longer than thephotochromic crystals. Therefore, it is considered that new photochromism of theindandione derivatives was also caused by the Norrish Type II intra-molecular hydrogentransfer reaction same as trans-biindenylidenediones.

1

2

3
Fig. 1 Indandione derivatives

4

5

Reference
Koichi Tanaka et al., CryslEngComm., 2004, 6(2), 1-4

Structural and Functional Analysis of Nup120
Suggests Ring Formation of the Nup84 Complex

P-112

Hyuk-Soo Seo, Yingli Ma, Erik W. Debler, Daniel Wacker, Stephan Kutik, Günter
Blobel, André Hoelz
Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller
University, 1230 York Ave, New York, NY 10065, USA (hseo@rockefeller.edu)

The Nup84 complex constitutes a key building block in the nuclear pore complex (NPC).
Here, we present the crystal structure of one of its seven components, Nup120, which reveals
a β-propeller and an α-helical domain representing anovel fold. We discovered a previously unidentified
interaction of Nup120 with Nup133 and confirmed thephysiological relevance in vivo. Since mapping of theindividual components in the Nup84 complex positions
Nup120 and Nup133 at opposite ends of the heptamer,
our findings indicate a head-to-tail arrangement ofelongated Nup84 complexes into a ring structure,
consistent with a fence-like coat for the nuclear poremembrane. The attachment site for Nup133 resides at- 182 -

AsCA’09

Posterthe very end of an extended unstructured region, which would allow for flexibility in the
diameter of the Nup84 complex ring. These results illuminate important roles of terminal
unstructured segments in nucleoporins for the architecture, function, and assembly of the
NPC.

Gas Pores Formation in Laser Induced Ti Melts for
Implant Prototyping

P-113

A. A. Shaikh1, S. Dudziak2, O. Meier2 and T. M. Gesing3
1
Department of Chemistry, University of Dhaka, Dhaka 1000, Bangladesh(aftab74@yahoo.com )2
Laser Zentrum Hannover e. V. Hollerithallee 8, 30419 Hannover, Germany(S.Dudziak@lzh.de )3
Department of Crystallography, Institute of Geosciences, University of Bremen,
Germany (gesing@uni-bremen.de)

Ti based materials have been extensively used as implants for artificial hard-tissue
replacement because of their excellent biocompatibility, superior corrosion resistance, highspecific strength and low density. Although the Young’s modulus of pure Ti (110 GPa) isrelatively low compared to other conventional implant materials (210 GPa for stainless steel),
there is a huge difference in elasticity between the Ti implant and its surrounding tissues.
However, critical problems arisen by the mismatch of Young’s modulus between implant andsurrounding tissues are still unsolved. An alternative to improve the mechanical property
mismatch is to reduce elastic modulus of pure Ti by introducing pores, thereby minimizing
stress shielding effect between implant and bone where inserting. A number of biocompatible
foaming agents have been developed by our research group which allows a laser induced Ti
foaming without leaving the toxic degradation products in the Ti matrix. The porous samples
were analysed regarding the total porosity, the allocation and the size and shape of pores bytaking optical and electron micrographs together with micro-CT imaging and analysis. The
porous Ti structure with maximum total porosity of 57.0% could be generated in this laser
induced foaming process. The porous Ti sample with this amount of porosity is predictable toreduce the stiffness of pure Ti material. Therefore, this porous material could have highpotentiality to use as implant material for hard-tissue replacement.

A Study of Tantalum Substituted Potassium Tungsten
BronzesP-114

Md. Mahbubur Rahman Shakil1, Altaf Hussain2
1
Department of Chemistry, Dhaka University of Engineering & Technology,
Gazipur-1700, Bangladesh, (mrshakildu@yahoo.com)
2
Department of Chemistry, University of Dhaka, Dhaka -1000, Bangladesh,(altaf@univdhaka.edu)

Tungsten bronzes are non-stoichiometric ternary metal oxides having general formula AxWO3
where A is electropositive element and 0 < x < 1. Because of their interesting physical andchemical properties, pure potassium tungsten bronzes have been studied extensively [1].
However, there are very few reports available on tantalum substituted potassium tungsten- 183 -

AsCA’09

Posterbronze [2]. Therefore, attempts were made to prepare a series of compounds in the system
KxTayW1-yO3 with x = 0.30, 0.00 ≤ y ≤ 0.30 and x = 0.55, 0.00 ≤ y ≤ 0.10 by conventional
solid state synthesis method.
The samples were characterized with XRD, SEM/EDX and optical spectroscopy. X-ray
powder patterns reveal that the samples with nominal compositions x = 0.30, y ≤ 0.30 show
hexagonal tungsten bronze (HTB) type pure phase and the samples with x = 0.55, 0.02 ≤ y ≤0.10 show a mixture of two phases (K-HTB and tetragonal potassium tungsten bronze,
K-TTB). Structure refinements of K-HTB samples using Rietveld fitting procedures reveal adecrease in a and an increase in c lattice parameters with increasing nominal Ta content. The
elemental compositions of the crystals determined by SEM/EDX analysis also show anincrease in Ta content with increasing y. Investigations of the optical reflectivity and theinfrared absorption spectra of powder K0.3TayW1-yO3 samples indicate a decreasing polaron
concentration with increasing Ta content.
References[1] Ph. Labbe, Key Engineering Materials 68 (1992) 293-339.
[2] A. Deschanvres, M. Frey, B. Raveau, J. C. Thorhazeau, Bull. Soc. Chim. Fr. 9 (1968) 3519.

P-115

Stability and tinctorial strength of black
leuco-colorants as viewed from the crystal structureof a phenolic developer
Hideki Shima, Kazuyuki Sato, and Jin Mizuguchi
Graduate School of Engineering, Yokohama National University; 79-5 Tokiwadai,
Hodogaya-ku, 240-8501 Yokohama, Japan (d09gd230@ynu.ac.jp)

2-[(4-Hydroxyphenyl)sulfonyl]-phenol (BPS) is a well-known developer for black leuco-dyes(for example, 6’-(diethylamino)-3’-methyl-2’-(phenylamino)-spiro[isobenzofuran-1(3H),9’[9H]-xanthen)-3-one]: ODB) in thermosensitive papers. Although BPS is a small molecule(molecular weight: about 250), it is thermally stable as characterized by a high melting pointof about 184 °C. Furthermore, BPS is also known to stabilize the 1:1 “ODB/BPS” system.
Because of this, structure analysis of BPS has been carried out in order to elucidate thestability of BPS itself as well as its “leuco/developer” system. Then, we found that one BPS
molecule is hydrogen-bonded to four different neighboring ones, forming an OH…O
two-dimensional hydrogen-bond network. This ensures a high thermal stability of BPS. On
the other hand, in the “ODB/BPS” system, only one of the four hydrogen bonds in BPS is
used for the formation of the 1:1 “ODB/BPS” colorant while the remaining three hydrogenbonds keep the network. As for the tinctorial strength in spin-coated ODB/BPS, the color
intensity is found to be limited to about 70 % of the maximum available value. This isbecause there is a fraction of ODB molecules whose lactone-ring is still closed due to thesteric hindrance.

- 184 -

AsCA’09

Poster

Molecular structure of BPS

P-116

Molecular structure of ODB

Crystallographic statistical studies of the
decavanadate anion: toward a prediction of the
non-covalent interactions
Anne Spasojević – de Biré1 , Nada Bosnjaković-Pavlović
1
Laboratoire “Structures Propriétés et Modélisation des Solides”, UMR 8580 du CNRS,
Ecole Centrale Paris, 92295 Châtenay-Malabry, France (anne.spasojevic@ecp.fr)
2
Faculty of Physical Chemistry, University of Belgrade, P.O.Box 47, 11001 Belgrade,
Serbia (nadab@ffh.bg.ac.rs)

More than 100 structures containing the [V10O28 Hx]6-x anion has already been published.
From a geometric point of view, the decavanadate anion [V10O28]6- appears very rigid withreally small variations in interatomic distances or bond angle values.
We have retrieved from the organic-organometallic database (CSD), the protein data base
(PDB) and an extensive bibliographic search 30 different crystalline structures, which imply
600 contacts for which the structure is of excellent crystalline quality. In a previous study, we
have experimentally determined the electron and electrostatic properties of two decavanadatebased compound Na3V10O28(C4N3OH5)3(C4N3OH6)3 ·10H2O and (NH4)6 [V10O28] . 6H2O.
From these results we have predicted the preferential non-covalent interactions (figure 1a)with the different oxygen atoms of the decavanadate anion. These predictions are confirmed,
in this statistical study. The non-covalent interactions are strongly different depending on theoxygen atom type. The Ob and Oc oxygen atoms, for which the electrostatic potential in thevicinity have the lowest value, are involved mainly in the strong O-H…O, N-H…O while Of
or Og are mainly involved in weakest hydrogen bonds such as C-H…O or cation interactions.
(figure 1b).
These results are important in the context of the various biological applications of the
decavanadate such as, for example, inhibition of the Ca2+ ATPase, myosin ATPase, and new
development in insulin mimetic.

- 185 -

AsCA’09

Poster

Ob

180

Oc

170
160
150
140
130

Of

120
110

Ob
Od

100
90
80
1,5

1,7

1,9

2,1

2,3

2,5

2,7

2,9

1,9

2,1

2,3

2,5

2,7

2,9

180
170
160
150

Oe

140

Oc

130
120

-1

e.Å

Og

OH匫
NH匫
CH匫

110
100
90
80
1,5

1,7

a
b
Figure 1. a ) Molecular surface of the decavanadate anion colored by the experimental electrostatic
potential values. b) Distribution of the hydrogen bonds observed between an OH, NH or CH moiety and an
oxygen of the decavanadate anion ; x axis : H…O distance (Å) ; y axis DH…O angle (°) ; top Ob, bottom
Og.

Non Photochemical Light Induced Nucleation. A tool
to crystallize polymorphs on demand ? Application tocarbamazepine.

P-117

David Miret1,2, Janice Aber2, Bruce Garetz2, Philippe Scouflaire3, Anne Spasojević– de Biré1
1
Laboratoire “Structures Propriétés et Modélisation des Solides”, UMR 8580 du CNRS,
Ecole Centrale Paris, 92295 Châtenay-Malabry, France (anne.spasojevic@ecp.fr)
2
Department of Chemistry, Polytechnic Institute of New York University, New York, USA(bgaretz@duke.poly.edu)
3
Laboratoire EM2C, UPR 288 du CNRS, Ecole Centrale Paris, 92295
Châtenay-Malabry Cedex, France (philippe.scouflaire@em2c.ecp.fr)

There is tremendous pressure on the pharmaceutical industry to understand the polymorphismof drugs in order to control and produce the most stable and effective polymorphs. There is a
growing awareness of the effects of polymorphism and pseudo-polymorphism on theproperties of drugs, such as their physical and chemical stability, solubility, dissolution rate,bio-availability, and mechanical properties, and their consequences on the manufacturing
process. We have developed a fundamental approach to study polymorphism, which
combines high-resolution X-ray diffraction and ab initio theoretical calculations. That would
enable us to study the consequences of drug polymorphism on the physical and chemical
properties of drugs. Ideally, the experimental study of polymorphism requires the possibility
to crystallize the desired polymorphic forms “at will” and to obtain new, yet uncharacterizedphases.
Garetz and Myerson have invented an original nucleation method, termed NPLIN,“Non-Photochemical Light-Induced Nucleation” that makes it possible to control the
nucleation process. We have already implemented this method at Ecole Centrale Paris andtested it successfully on glycine.
- 186 -

AsCA’09

PosterCarbamazepine is anti-epileptic drug, a highly polymorphic compound (4 true polymorphs,
more than 20 hydrates or solvates) generally studied as a model compound for studying
polymorphism. It represents a suitable compound for the demonstration of the feasibility of
the NPLIN method for drug compound.
The polymorphs obtained after crystallization under NPLIN method will be discussed
according to the hypothesis that the optical Kerr effect is involved in the NPLIN mechanism.
LP

CP

a
b
Figure 1. a) Schematic representation of the NPLIN method. b) Dimer of carbamazepine molecules
involved in the 4 thrue polymorphs.

Investigation of Lattice dynamics and Anharmonicityof Raman modes in BaWO4 crystal

P-118

J. Suda1, P. G. Zverev2, O. Kamishima3, J. Kawamura3 and T.Hattori4
1
Department of Electric Engineering, Kushiro National College of Technology,
Otanoshike-nish, kushiro, 084-0916, Japan, (suda@kushiro-ct.ac.jp)
2
A M Prokhorov General Physics Institute Russian Academy of Sciences, 38 Vavilov
Street, Moscow 119991, Russia,( pgz2000@yandex.ru)
3
Institute of Multidiscpilinary Research for Advanced Materials, Tohoku University,
Katahira, Aobaku, Sendai 980-8577, Japan
4
Department of Applied Physics, Faculty of Science, Tokyo University of Science, Tokyo
162-8601, Japan

The phonon-dispersion relations (Fig. 1) of BaWO4 crystal are calculated using the Latticedynamical calculations approach described earlier [1]. Spontaneous Raman spectra (Fig. 2) inthe BaWO4 were measured in the temperature range 10-295K for a body-centered tetragonalphase [2]. The temperature dependence of linewidth of the Eg (72 cm-1) and the SRS-active
Ag (926 cm-1) were analyzed using TDOS (Fig. 3) due to cubic term. The calculated results
well describe the observed ones in this temperature range in Fig. 4. Also, the variation oflinewidth of the 72cm-1 peak is also about 1.8 times greater than those for the 926cm-1 peak.
The scattering of a thermal phonon by observed phonons dominates phonon-phonon
interactions on the lower-frequency mode [the Eg (72 cm-1)]. Phonon-phonon interactions on
the higher mode [the Ag (926 cm-1)] are dominated by the decay of the observed phonons into
two phonons having lower energies. We found that this originates in a clearly large phononband gap (Fig. 1) in the PDOS (phonon density of states) that produces a difference inanharmonic effects on each peak’s channels. This result is similar to that in thehigh-temperature phase in the case of LaGaO3 [3].

- 187 -

AsCA’09

Poster1000

12

T=300K

X=Ba

500

0

Γ

X

P

N

Γ

Z

F

0

500

1000

0
0

-1

Fig.2

500
?
W ave number[cm ]

Fig.3

-1

scattering

Frequency (cm )

Fig.1

-1

72cm peakΓ [cm ]

D[arb.units]?

Frequency[cm ]

decay

1000

-1

926cm

1

0
0

100

200

300

T[K]

Fig.4

References[1] J. Suda and T. Sato, J. Phys. Soc. Japan. 66, 1707(1997).
[2] T. T. Basiev, A. A. Sobol, Yu. K. Voronko, P. G. Zverev, Optical Materials, 15, 205 (2000).
[3] J. Suda et al., J. Phys. Conf. Ser 92, 012148(2007).

P-119

Absolute Structure Determination of Organic
Compounds: an Update
Herman H-Y. Sung1, Thanh-ha Nguyen1, Zoltan Gal2, Ian D. Williams1
1
Department of Chemistry, Hong Kong University of Science and Technology, Clear
Water Bay, Kowloon, Hong Kong, China (hermans@ust.hk)
2
Oxford Diffraction Ltd., Abingdon, United Kingdom.

There has been a renaissance in the use of copper X-radiation for small molecule structures, inpart due to the advent of dual wavelength diffractometers. One advantage for pure light atomorganic molecules is the larger anomalous scattering terms for softer Cu-Kα radiation offers
realistic prospects for absolute structure determination. The classical method of carefulmeasurement of strongly differentiated Friedel pairs is not readily attempted with modern
CCD diffractometry. In this paper we report a summary of absolute structure determination
for a range of synthetic and natural product organics. Even with a data set of reasonable
quality the Flack x parameter is typically indeterminate since its esd is often 0.15-0.20.
Results are compared using a new approach using Bayesian statistics (the Hooft y parameter)
available in the PLATON program package. The new method appears slightly more robust
and has the advantage of quantifying the probability of chirality determination. Attempts tosolve organic absolute structures using Mo-Kα data are also reported, including use ofmulti-pole refinement.
Acknowledgements: The Research Grants Council of Hong Kong and HKUST are gratefully
acknowledged for funding of this work through grant RPC07/08.SCI17.

P-120

Crystal structure and phase transition of a lead-based
inorganic-organic perovskite (C5H10NH2) PbBr3
Kota Takano , Munehiko Nakatsuma , Miwako Takahashi and Ken-ichi Ohshima
Institute of Materials Science, Unviersity of Tsukuba, Japan(takano@jb.bk.tsukuba.ac.jp)

Organic-inorganic hybrid perovskites have been synthesized and widely studied. They are
low-dimensional compounds and exhibit unique physical properties like anisotropic- 188 -

AsCA’09

Posterconductivity and structural phase transitions due to a structural instability. Lead-halide
perovskites (C5H10NH2)PbX3 (X=I, Br, Cl) are one-dimensional semiconductors consisting of
one-dimensional chains of face-sharing lead-halide octahedra and barrier parts of C5H10NH2+
molecules. For (C5H10NH2)PbI3, structure and physical properties have been extensively
studied. It has a structure of orthorhombic C2221 (No.20) and undergoes temperature induced
successive phase transitions and a pressure-induced transition. For (C5H10NH2)PbBr3 on theother hand, there are very few studies[1] and its precise structure has not been determined yet.
In this research, we synthesized single crystals of (C5H10NH2)PbBr3 and investigated its
crystal structure using single crystal X-ray diffraction (XRD). The structure at room
temperature is determined to be monoclinic P21 space group (No.4). The phase transition in(C5H10NH2)PbBr3 was also studied using Differential Scanning Calorimetry (DSC) and XRD
for a temperature range of 100K ~ 420K. We found a phase transition occurs at around380K-410K and the structure transforms to orthorhombic C2221 in high temperature phase.

mcal/sec

-0.02
-0.04
-0.06
-0.08
-0.10

360 370 380 390 400 410 420
temperature (K)Fig.1. Crystal structure at room temperature and 420K.

Fig.2. The DSC curve of (C5H10NH2)PbBr3.

Reference
A. Bonamartini Corradi et al.: Inorganica Chimica Acta 254 (1997) 137-143.

Super accurate structure factor measurement ad
PF14A

P-121

Kiyoaki Tanaka1, Yasuyuki Takenaka2, Terutoshi Sakakura1, Shirou Fanahashi1,
Koji Okada1
1
Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya, Japan( Tanaka.kiyoaki@nitech.ac.jp)
2
Hokkaidou University of Education, 1-2 Hachiman-cho Hakodata, Hokkaido, Japan,(bow@bussei.hak.hokkyodai.ac.jp)

Introduction
We have been investigated the 4f-electron density distribution1) and realisethat the accuracy of the structure-factor measurement with the laboratory X-ray source anddiffractometer is very close to its limit and more accurate data should be collected. Thus, theresearch aiming to measure structure factors of all reflections with the accuracy of 0.1 % wasstarted.
Experimental Since more than 2.5x105 photon counts are necessary to reduce the statisticalcounting error less than 0.1% and since the multiple diffraction should be avoided with
ψ-scan, the four-circle diffractometer equipped with the APD detector installed at PF14A wasused. Since high order reflections of CeB6 (space group pm-3m, a=4.1407A) is still strong(the largest ratio of the structure factors is 9.8.), 5800 reflections in the full space were
- 189 -

AsCA’09

Postermeasured with the statistical counting error less than 0.1% in five days. When reflections
deviated more than 2% from the mean of the symmetry related reflections they were
measured again. The reference reflections which were measured to see the stability of theexperiment were not fluctuated more than 1% after the intensity normalization using themonitor counts measured by the ionic chamber (IC). This is due to the top-up operation
recently started at PF. The ψ-rotation was made possible for the diffractometer at BL14 andthe multiple diffraction were avoided though it can't be avoided for some reflections evenwith the parallel SR beams2). When the secondary reflection comes on the Ewald sphere after
the primary reflection, the intensity of which is measured, with the delay angle of 1.5 times ofthe sum of the FWHM's (full width at half maximum) of the two reflections, 1010 secondaryreflections were judged to be affected by the MD effect. FWHM of five reflections wasaveraged to be 0.0126°and used to evaluate MD.
Refinement
Starting from the final parameters of our previous refinement at room
3)
temperature , the scale factor, atomic parameters and type I extinction parameters wererefined. R factors without and with the reflections affected by MD are 0.00610 and 0.00606.
After the XO analysis R factor was reduced to 000433. This indicates the measurement with
the SR gave reliable results. The difference density after the spherical-atom refinement
clearly revealed peaks of 0.25eÅ-3 due to 4fj=5/2Γ8. After the XAO analysis4) these peaks weredeleted. However the differences between the observed and calculated structure factors of
low-order strong reflections are still large. They are more than 10 times of their statisticalcounting errors.
Discussion Judging from the very low R factors the measurement was successful. The
intensity of the incident beams was monitored with the IC. However it is easily influenced by
the Xe gas pressure passing the IC. Actually the monitor counts varied sometimes more than
5%. However the structure factors of the reference reflections which were normalized using
the monitor counts were stable indicating the correction by the monitors was successful. Thus
if more reliable monitor is used, the accuracy of the measurement will be enhanced. The large
differences between the observed and calculated structure factors remained in the low orderstrong reflections indicating the anisotropic extinction correction is not good enough.
References
1) R. Makita et al. (2007) Acta Cryst. B63, 683-692.
2) Y. Takenaka et al. (2008). Acta Ceryst. A64, C566.
3) K. Tanaka & Y. Onuki (2002). Acta Cryst. B58, 423-436.
4) K. Tanaka, et al (2008). Acta cryst. A64, 437-439.

Surface Morphology and Crystallinity ofPoly(hydroxybutyrate)/Poly(L-lactic acid) Blends

P-122

Akihisa Tokuda, Takashi Asano, Yusuke Oji, Yukihiro Ozaki, Hikaru Terauchi, andIsao Takahashi
Faculty of Science and Technology, Kwansei Gakuin University, Sanda 6691337, JAPAN(adl28058@kwansei.ac.jp)

For past decades, biodegradable polymers have attracted a lot of attention due to the- 190 -

AsCA’09

Posterworld-wide concern on environmental problem and preservation of fossil fuels. Polymers areoften used as films and fibers where surface properties become more and more important thanthose of bulk. Even for biodegradable polymer thin films and fibers, controlling surface
morphology and structure is a critical issue for practical usage in near future. Polymer blend(polymer alloy) is a widely-accepted effective technique for improving the physical propertiesof polymeric materials. However, we must admit that little is known for ultrathin films of
blended biodegradable polymers. In the present study, we study crystallization andmorphology of the biodegradable polymer blends with surface-sensitive X-ray diffraction
techniques.
Poly(hydroxybutyrate)[PHB] is a biodegradable crystalline polymer which is transparent,
good odor and indicates decent thermo-plasticity, biocompatibility and relatively high melting
point. All of such properties make PHB a promising biodegradable polymer. Therefore,
controlling the crystallinity in the surface region and thin films also affecting the surface
morphology becomes an essential technique for delicate fabrications in near future.
In the present study, we study thin films of PHB blended with another biodegradable polymer,
Poly(L-lactic acid) [PLLA] to investigate how PLLA affects the surface structure andmorphology of PHB film with thickness of several nm. The spin-coated polymer blends wereprepared on Si(100). X-ray reflectivity (XR) and grazing incident X-ray diffraction (GIXD)
were chosen as tools for investigation of surface morphology and crystallinity in the surface
region, respectively. Atomic force microscopy was also used to observe surface morphology.
From weight ratio dependence and molecular weight dependence of PLLA on crytallinity andmorphology, we found that a small amount of PLLA (ca. 10wt%) effectively retards the
crystallization of PHB and makes the surface sufficiently flat in PHB/PLLA films, which wenever have had corresponding results for bulk samples. We confirm that PLLA is anappropriate material which affects the surface morphology of ultrathin PHB without
deteriorating its biodegradability.

Status Report on Super High Resolution Powder
Diffractometer at J-PARC

P-123

Shuki Torii1, Takashi Kamiyama1, Takashi Muroya1, Setsuo Sato1, Hidenori
Sagehashi1, Ryoko Oishi1, Takahiro Morishima1, Teguh Panca Putra1, Junrong
Zhang1, Kenji Iwase2, Masao Yonemura2, Akinori Hoshikawa2, Toru Ishigaki2,
Susumu Ikeda1
1High Energy Accelerator Research Organization, KEK Tokai Campus, 2-4 Shirakata
Shirane, Tokai, Naka, Ibaraki 319-1195, Japan, (torii@post.kek.jp)
2
Ibaraki University, Ibaraki Quantum Beam Research Center, 162-1 Shirakata, Tokai,
Naka, Ibaraki 319-1106, Japan,

At the end of May in 2008, the first neutron was produced successfully from a spallation
neutron source in Japan Proton Accelerator Research Complex (J-PARC). High resolution
Bragg reflections were obtained using the Sirius diffractometer chamber at Super High
Resolution Powder Diffractometer (SuperHRPD) beam line at Materials and Life Science
Experimental Facility (MLF). We divide and consider the project of SuperHRPD in twophases. In the “Phase-I” of our project, we started up quickly by using the existing Sirius- 191 -

AsCA’09

Posterchamber. Simultaneously, we were carrying out basic study to design and construct a new
SuperHRPD chamber, and the Sirius chamber will be exchanged for new one in summer of2009. We have succeeded in achieving the best resolution among all the neutron powder
diffractometers in the world, a part of detector pixels of SuperHRPD has achieved ∆d/d =0.035 %. Currently, about 300 detectors have been installed in the backward detector bank (2θ= 150º ~ 175º), and several standard samples including Si (NIST SRM640c) have beenmeasured. As the result, a chi-square value of 2.08 was obtained from a refinement of the Si
powder data using a Z-Code developed by our group. In the “Phase-II”, we will install a newchamber to improve S/N, and achieve better resolution as well as intensity. In the design of a
new chamber, a detector solid angle is increased, d-range / Q-range is expanded, and also has
options of high-intensity mode and high-resolution mode with incident collimations.

Fig.1 The fitting result using a Z-Code

Crystal Structure Comparisons of
Tetrakis(4-hydroxyphenyl)alkane Inclusion Crystals

P-124

Kazuyuki Toyota1, Hidehiro Uekusa1, Natsuki Amanokura2, Masami Kaneko2, andHiroshi Suzuki2aDepartment of chemistry and materials science, Tokyo Institute of Technology, 2-12-1
Ookayama, Meguro-ku, Tokyo, JAPANb
Nippon Soda Co.Ltd, JAPAN

Inclusion crystals have unique characteristics such as controlled guest solubility or
temperature dependent guest releasing, which are relevant to the structure of host framework
enclosing guest molecules. Hence it is of great importance to investigate and develop hostframeworks to design new functional materials. 1,1,2,2-tetrakis (4-hydroxyphenyl)ethane,
TEP (Fig.1), has four phenyl groups in different directions to build various types of hydrogenbonding host frameworks corresponding to the types of guest molecules. In our previous
study, three kinds of host frameworks accommodating different kinds of guest molecules via
hydrogen bonds were analyzed to show TEP has well-qualified ability as an inclusion hostmolecule.
In this study, new host molecules are synthesized as the modification of TEP, and their
inclusion crystal structures are analyzed to compare the host frameworks. By making thecentral alkane chain longer, new host molecules, TBP and TPP, (Fig.1) were synthesized tomake inclusion crystals with small organic molecules. In contrast to practically rigid TEP
molecule, their longer alkane chains give more conformational flexibility so as to form new- 192 -

AsCA’09

Posterhost frameworks that are different from TEP inclusion crystals.
TBP-THF-H2O inclusion crystal is an example of new host frameworks (Fig.2). In thechannel structure of TBP host framework, THF molecules are aligned in 1-dimentionalmanner. Because new hosts should form larger channel in the framework by utilizing theirflexibility, larger organic molecule guests which could not be accommodated to the TEP
frameworks are employed as guests in order to demonstrate the inclusion ability of new hosts.

Fig.1 Molecular structures of hosts. n=0,2,3
corresponds to TEP, TBP, TPP, respectively.

P-125

Fig.2 The crystal structure of TBP-THF-H2O
projected from a-axis.

Pharmaceutical Polymorphs and their Phase
Transitions Investigated by Ab Initio Structure
Determination from Powder Diffraction Data
Hidehiro Uekusa1, Etsuo Yonemochi2, Katsuhide Terada2
1
Tokyo Institute of Technology, Ookayama 2, Meguro-ku, Tokyo 152-8551, JAPAN(uekusa@cms.titech.ac.jp)
2Toho University, 2-2-1 Miyama, Funabashi-shi, Chiba, 274-8510, JAPAN

Many pharmaceutical organic crystals show polymorphism including hydrate or solvate
crystals. As their physicochemical properties such as stability, solubility, and bioavailability
differ from each other depending on the crystal structures. Also by a mechanical treatment or
during storage, unexpected phase transition among (pseudo-) polymorphs is sometimes
observed. Thus, in order to utilize the pharmaceutical polymorphic crystals as API, structuralinvestigation of phase transition phenomena is essential. However, after the phase transition, asingle crystalline form usually tends to degrade and becomes powdery crystal. In such case,ab initio structure determination from powder diffraction data (SDPD) is efficient techniqueto analyze the crystal structure from PXRD.
In this study, crystal structures and phase transitions of pharmaceutical polymorphs areinvestigated by SDPD technique.
1. Thermal transformation of Tolbutamide polymorphic crystals
Tolbutamide (Fig. 1) is a hypoglycemic agent, and has four polymorphic forms. From theheat of solution measurement, it was found that the stability of Form III decreased above
303K due to the thermal phase transition to a new form. The crystal structure wasdetermined from high resolution PXRD using synchrotron radiation by SDPD technique.
In the new form of crystal, tolbutamide molecule shows a twist in the terminal chainorientation, and the molecular packing is almost similar [1].
- 193 -

AsCA’09

Poster

2. Two step dehydration process of Lisinopril dihydrate
Pharmaceutical hydrates are well used as API (Active Pharmaceutical Ingredients) and often
show dehydration phenomena. Lisinopril (Fig. 2) is used as an anti-hypertension drug inthe dihydrate form. A DSC-PXRD measurement indicated that water molecules werereleased at 373K and 383K to form monohydrate and anhydrous form, respectively. Bothcrystal structures were successfully analyzed from high resolution PXRD. The dehydration
mechanism is illustrated as the two step water molecule releasing from two different channel
structures in order. During the process, terminal phenylethyl group turns to close theempty channel and to stabilize the structure.
3. Pharmaceutical co-crystal formation by co-grinding
Co-grinding of pharmaceutical compound with co-crystal former sometimes gives a new
co-crystal having favorable properties. Co-crystal of valproic acid and L-arginine (Fig. 3)
was obtained only by this method to resolve the hygroscopicity of API. Because theground co-crystal was powdery crystal, the crystal structure was analyzed by SDPD
technique to reveal unique layer structure and very stable crystalline form even under high
R.H. conditions.

Fig.1 Tolbutamide

Fig.2 Lisinopril

Fig. 3 Valproic acid and L-arginine

Reference
H. Hasegawa et al., International Journal of Pharmaceutics, 369, 12-18(2009).

P-126

Molecular ordering and orientation in surface regionof natural cocoa butter and its constituent oils, POP,
SOS and POS revealed by X-ray Diffraction
Yoshihito Uozaki, Kimihiko Nozaki, Mai Uenaka, Hikaru Terauchi and Isao
Takahashi
Faculty of Science and Technology, Kwansei Gakuin University, Sanda 6691337, Japan(zm28987@kwansei.ac.jp)

Cocoa butter exhibits six polymorphisms characterized by the type of molecular stacking andorientation. Cocoa butter consists of various oils and fats, e.g., POP (sn-1,3-dipalmitoyl-2-oleoylglycerol), SOS (sn-1,3-dipalmitoyl-2-stearoyl-glycerol) and POS (1,3-rac-palmitoylstearoyl-2-oleoylglycerol). The properties of these oils and fats are similar to each other; POP,
SOS, POS and other fats has five (or six) similar polymorphisms and show successive
transformations from quasi-stable form to stable form like cocoa butter.
We recently studied surface-induced preferred orientation of natural cocoa butter ultrathin
films with surface-sensitive X-ray diffractions, and found a novel double-layer to single-layertransition reminiscent of transitions seen in smectic liquid crystals. [1] In the present study,
we expand the research on the surface structure of each principal constituent oils, POP, SOS
and POS, and their bulk structures. The techniques adopted here are X-ray reflectivity (XR)
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AsCA’09

Posterand Grazing incident X-ray diffraction (GIXD) with a supplementary use of AFM and optical
microscopy. Since the typical diffraction angles of XR correspond to that of small angle X-ray
scattering (SAXS), XR enables us to determine the surface morphology and distribution ofelectron density in a wide range of scale between sub microns to several nano meters. On theother hand, GIXD is quite sensitive to the molecular orientations in the surface region ofmaterials to a depth of several nanometers to microns. For POP, a quasi-stable pseudo-’
form revealed to be fairly stable in the double-layer of spin-coated thin films, which has neverbeen attained for the bulk structure. We consider that either confined effect or dimensionality
affects the configuration of local minima in energy landscape of this material.
Reference
Y. Hayashi et. al., Transactions of the Materials Research Society of Japan, Vol. 33[3] (2008) 641-644.

INTER MOLECULAR INTERACTIONS IN 2 AMINOAND SCHIFF BASES OF THIOPHENES

P-127

Vasu Sriranga a and Deepak Chopra baVivekananda Degree College, Bangalore-560055 , India(asusriranga@rediffmail.com)b
Solid State Structural Chemistry Unit, IISc., Bangalore560012, India(deepakcryst@gmail.com)

Probing intermolecular interactions in functionalized thiophenes has been carried out tounderstand the influence of various substituents on the bond parameters and the conformation.
The research work reported describes the crystal structure and onformation.
The research work reported describes the crystal structure and conformational studies of
2-amino thiophenes, and Schiff bases of thiophenes, which serve as starting materials fornumber of intermediate derivatives. These compounds are antibacterial, antitubercular,
antifungal, anti-inflammatory and antitoxic. The crystallographic studies throw light onmolecular structure which helps in understanding the activities of the biological molecules.
The X-ray structure determination of 17 compounds has been carried out in the above family.
The structural comparisons of all the thiophene compounds are as follows. There are certain
similar and dissimilar molecular and crystal packing features are described amont 2-amino
thiophene derivatives and Schiff bases of thiophne derivatives. The thiophene moiety is planar
in all the compounds. It is noticed that from the half-chair conformation with different
substituents. Strong intra-molecular interactions which locks the molecular conformation isobserved in all the compounds. In addition to this the presence of intermolecular interactions
within the crystal lattice is influencing the packing of the molecules which modifies theproperities. Interesting details will be presented at the time of conference.

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AsCA’09

PosterOrgano-chelated Borates as Anions for
Crystallization and Chiral Resolution

P-128

Lawrence W-Y. Wong, Jack W-H.Kan, Pokka K-C. Pang, Alex S-F. Au Yeung,Thanh-ha Nguyen, Herman H-Y. Sung, Ian D. Williams
Department of Chemistry, Hong Kong University of Science and Technology, Clear
Water Bay, Kowloon, Hong Kong, China (chwill@ust.hk)

Boron may be chelated by a variety of dianionic ligands such as diolates, catecholates,
salicylates and mixed alkoxy-carboxylates, such as tartrate, lactate and mandelate. The
resulting molecular species have one negative charge per tetrahedrally coordinated boron
centre. In this respect these species are analogs of tertrafluoroborate [BF4]- andtetraphenylborate [BPh4]- which have been extensively used as crystallizing counter-anions,with low coordinative ability. Herein we report the facile synthesis of several familes oforgano-chelated borates, along with some representative crystal chemistry. The use ofasymmetric chelates such as salicylate creates a stereogenic center at boron. The chiralborabis(salicylates) [BSal2] have been resolved using quninium or sparteinium cations.
Solution CD spectra indicate the chirality at boron has a half-life of an hour at RT. Suchcompounds may be useful crystallizing agents but are not helpful for chiral resolution. The
use of chiral chelating ligands, such as R- or S-mandelate, offer help in this repect. Use of
R-mandelic acid affords exclusively [BS(R-Man)2] ions in 15 solid state structures to-date andhas allowed successful chiral separation of Traditional Chinese Medicinal components fromracemic mixtures.

Acknowledgements: The Research Grants Council of Hong Kong is gratefully acknowledged
for funding of this work through grant 603307.

P-129

A Unique Approach to Precisely Dispense Chemicals
with Diverse Properties
Jian Xu and Matthew Lundy
Rigaku Automation Inc., 5999 Avenida Encinas, Suite 150, Carlsbad, CA 92008

A common challenge researchers are faced with in many different laboratory techniques is theconsistent handling of liquids that have varying physical properties, such as viscosity andvolatility. In order to address this need, Rigaku has created the AlchemistTM II, which employsa unique approach to liquid handling and stock management [1] and excels at precisely
dispensing volumes ranging from 1 microliter up to 10 milliliters. Using TapperTM technology,
viscosity dependent dispensing parameters, and three different sized positive displacement- 196 -

AsCA’09

Postersyringes, the Alchemist II dispenses a wide range of viscosities, ranging from low viscosity
solutions such as alcohols to high viscosity polymer solutions such as 30% polyethylene
glycol 20,000, with a high degree of precision, without requiring touch-off on the target plate.
We report herein the dispense precision achieved by the Alchemist II when dispensing several
diverse chemical stocks, measured using a quantitative volumetric dispense assay. The resultsof the study demonstrate the Alchemist II’s ability to dispense chemicals with differing
physical properties consistently over a wide range of volumes.
1. Alchemist II information available at http://www.rigaku.com/automation/alchemist.html

P-130

Reversible Transformation and Fluorescent
Properties in Polymorphic Crystals of
n-Butylammonium 2-Naphthalenesulfonate
Atsushi Yamamoto, Masaaki Matsumoto, Tomoaki Hinoue, Yuji Mizobe, Ichiro
Hisaki, Mikiji Miyata, Norimitsu Tohnai
Department of Material and Life Science, Graduate School of Engineering, Osaka
University, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan,( yamamoto@molrec.mls.eng.osaka-u.ac.jp)

Organic luminescent materials have been extensively researched. In particular, dynamic
tuning or switching system of solid-state luminescence has been much attention for theirpotential application to optoelectronic devices. For the purpose of construction of thesesystems, we have been modulated molecular arrangements by using organic salts.
Recently, we have reported organic salts composed of anthracene- 2,6-disulfonic acid withprimary amines exhibited a static change of crystal structures and fluorescence intensity in thesolid-state1-2). Here we report an organic salt of 2-naphthalenesulfonic acid and n-butylamine(Scheme 1) showed a dynamic change of crystal structures by mechanical stimuli and heating.
And these phenomena induced modulation of fluorescence colours.
Organic salt of n-butylammonium 2-naphthalenesulfonate yielded two polymorphic crystals:
the block-like Form A and the plate-like Form B. The former was obtained from polar
solvents such as 1-propanol, while the latter was obtained from non-polar solvents such as
m-xylene.
As a result of X-ray crystallographic studies, Form A has π-π interactions among naphthalenerings and hydrogen-bonding network involving two oxygen atoms of sulfonate group. So, thisform exhibited excimer luminescence. On the other hand, Form B has CH-π interactions andthe network involving three oxygen atoms. Luminescence from Form B which hasedge-to-edge interaction of naphthalene rings was monomeric.
Interestingly, Form A was transformed to From B by mechanical grinding. Moreover, Form A
was recovered by heat treatment at 120 ˚C (Figure 1). At the same time, luminescent
properties were changed between them because of drastic change of structures3).

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AsCA’09

PosterScheme 1

Figure 1. Reversible structure change between twopolymorphic crystals: Form A(a) and Form B(b)composedof 2-naphthalenesulfonic acid and n-butylamine.

References
1) Y. Mizobe, N. Tohnai, M. Miyata, and Y. Hasegawa, Chem. Commun., 2005, 1839-1841.
2) Y. Mizobe, H. Ito, I. Hisaki, M. Miyata, Y. Hasegawa, and N. Tohnai, Chem. Commun., 2006
2126-2128.
3) A. Yamamoto, M. Matsumoto, T. Hinoue, Y. Mizobe, I. Hisaki, M. Miyata and N. Tohnai, Synth. Met.,
2009, 905-909.

P-131

NaVO2(IO3)2(H2O): A New 1D Vanadyl Iodate With Very
Strong Second Harmonic Generation
Bing-Ping Yang, Jiang-Gao Mao*
State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the
Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002 (mjg@fjirsm.ac.cn)

The search of new second-order nonlinear optical (NLO) material is of current interest andgreat importance owing to their applications in photonic technologies.1 Metal iodates such as
α-LiIO3 which also contain a lone-pair cation I5+ in an asymmetric coordination geometry
have been reported to show wide transparency region, large second-harmonic generation(SHG) coefficients, high optical damage thresholds as well as good thermal stability.2
Vanadium(V) is apt to form a vanadyl moiety (cis-VO2+) in acidic aqueous media. When four
additional ligands bind the vanadyl moiety, the resultant VO6 octahedron strongly distorted
because of the bent nature of the O=V=O bond angle (≈107°). The combination of iodate with
distorted VO6 octahedron may result in new compounds with excellent SHG properties.
Guided by this idea, we have successfully obtained a new type of polar material,
NaVO2(IO3)2(H2O), with a very large SHG response of about 20 x KDP. Herein we report its
crystal structure, and NLO properties.
NaVO2(IO3)2(H2O) crystallizes in the acentric space group P21 (No.4). Its anionic structure
may be considered to be one-dimensional, composed of [VO2(IO3)2]1-∞ zig-zag chains, thesechains run down the b-axis, are separated by Na+ cations. These chains are constructed fromfive-coordinate V(V) atoms that are bound by two terminal oxo atoms to create a cis-VO2+
moiety and by one monodentate and two bridging iodate anions to create a distorted trigonal
bipyramidal geometry. I5+ cations are in asymmetric coordination environment attributed to
the SOJT effects. I5+ cations are in distorted trigonal-pyramidal environments, being
coordinated by three oxygen atoms. I-O bond distances range from 1.773(6) Å to 1.873(5) Å.
The polarizations of all of the IO3 anions are toward the -b direction. The Na+ cations is- 198 -

AsCA’09

Postersurrounded by six oxygen atoms from one aqua molecule and two IO3 groups in a unidentate
fashion and three vanadyl oxygen atoms with Na–O distances in the range of 2.385(7) 2.587(7) Å.
Optical diffuse reflectance spectrum indicates an optical band gap of 2.54 eV.
NaVO2(IO3)2(H2O) is stable up to 218 ºC. The SHG measurements on the sieved powder
samples (80-100 mesh), using 1064 nm radiation, revealed that NaVO2(IO3)2(H2O) exhibits avery large SHG response of about 20 x KDP (KH2PO4). Furthermore, the compound wasfound to be phase-matchable. The extremely large SHG efficiency can be attributed to thesynergic effect of the polarizations of the IO3- anions.
c

100

b

SHG Intensity (arb.)

a

80
60
40
20
0

V

0

I

50

100

150

200

250

300

Particle Size (μm)

O

Fig.1. 1D chain [VO2(IO3)2]1-∞ in NaVO2(IO3)2(H2O)

Fig.2.Phase-matching curve for NaVO2(IO3)2(H2O).

References
1. (a) Chen, C.; Liu, G. Annu. Rev. Mater. Sci. 1986, 16, 203. (b) Ok, K. M.; Halasyamani, P. S. Chem. Soc.
Rev. 2006, 35, 710. and references cited therein.
2. (a) Chang, H.-Y.; Kim, S.-H.; Halasyamani, P. S.; Ok, K. M. J. Am. Chem. Soc. 2009, 131, 2426. (b) C.-F.
Sun, C.-L. Hu, J.-B. Ling, T. Hu, F. Kong, X.-F. Long, J.-G. Mao, J. Am. Chem. Soc. 2009, In press.

Acknowledgments: We thank the Nation Natural Science Foundation of China (No. 20825104,
20731006) for the financial support.

P-132

Critical narrowing of glass transition in supported
ultrathin polystyrene films
Chunming Yang, Naoki Koyasu, Kohei Ishimoto, Hikaru Terauchi, Isao Takahashi
Faculty of Science and Technology, Kwansei Gakuin University, Gakuen 2-1,
Sanda 669-1337, Japan (yangchunming@126.com)

Most materials form the crystalline sate as a minimum free-energy state of given external
conditions, but not a few materials are known to favor noncrystalline states. The glass
forming materials are ubiquitous and even crucial in our civilization. In the past decades, a lotof studies have dedicated to the properties and peculiar dynamics of glass forming materials
placed in highly confined circumstances, such as a nano-pore structures and ultra thin films.
The dynamics in such a confined system will strongly be affected by boundary conditions.
The broadening phenomenon of glass transition would be one of the most representativeinterface effects, in which the glass transition ranging in the temperature increases withdecreasing the thickness.
In the present study, we perform precise measurements on X-ray reflectivity (XR) of thin
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Posterpolystyrene (PS) films under various heating rates. Atactic PS thin layers were prepared byspin-coating method with Si substrates. Before the XR measurements, samples were annealed
above bulk glass transition temperature Tg for 12 h. Film thickness investigated ranges from 4
nm and 70 nm, comparable to the radius of gyration. The broadening of transition temperature
is most distinctively observed under the fast heating condition (0.50 oC/min), which isconsistent with previous studies [1, 2]. Furthermore, a narrowing of transition temperature isalso found with the PS films with decreasing thickness under the slowest heating condition(0.01oC/min). Since the broadening in thin films reflects the heterogeneity and local dynamics
which depends on the distance from the free surface [3], the narrowing of transition might besome homogeneity of dynamics in ultrathin films developing with the time interval.
References[1] S. Kawana, R.A.L. Jones, Phys. Rev. E 63, 021501 (2001)[2] Zahra Fakhraai and James A. Forrest, Phys. Rev. Lett. 95, 025701 (2005)[3] James A. Forresta, Kari Dalnoki-Veressb, Advances in Colloid and Interface Science, 94,167(2001)

P-133

Zeolitic Imidazolate Framework (ZIF) Compounds
using Asymmetric Imidazoles
Fion T-Y. Yeong, Fanny L-Y. Shek, Herman H-Y. Sung, Ian D. Williams
Department of Chemistry, Hong Kong University of Science and Technology, Clear
Water Bay, Kowloon, Hong Kong, China (chwill@ust.hk)

Metal imidazolides of formula [MIm2] are a highly robust family of metal organic frameworkmaterials. Variable temperature pXRD studies show stabilities up to 400oC. Many of thesephases have been prepared from polar organic solvents such as dialkyl-formamides underbasic conditions. Metal dications, such as Zn, Co or Cd are tetrahedrally coordinated and theimidazolide anions act as bent bridging ligands, Thus topologically they are analogues of SiO2
and aluminosilicate zeolites. Since the organic imidazole and crystallization conditions canbe varied greatly, a diverse family of open frameworks are possible. One interesting aspect we
explore in this paper is the case of asymmetric imidazoles, such as 4-methyl-imidazole,
4-nitro-imidazole, 4-phenyl-imidazole and 2-ethyl-4-methyl-imidazole. These introduce anasymmetry into each Im bridge and could lead to three outcomes; amorphous phases,
crystalline phases with 4,5-positional disorder or fully ordered crystalline phases. In generallower temperatures give amorphous or poorly crystalline phases, whilst higher crystallization
temperatures (160oC) can lead to fully ordered systems. We are now exploring possible hightemperature solid-state phase transitions of the amorphous materials.
Acknowledgements: We are grateful to the Research Grant Council HK (603307) andHKUST for funding of this work.

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AsCA’09

PosterModulated structure feature in over-doped
manganese oxides

P-134

Xiuzhen Yu1, YasuhideTomioka2, Yoshio Kaneko3, Toru Asaka4, Koji Kimoto1,
Taka-hisa Arima5, Yoshinori Tokura3,6, and Yoshio Matsui1
1
Advanced Electron Microscopy Group, ANCC, National Institute for Materials
Science, Tsukuba, 305-0044, Japan (Yu.xiuzhen@nims.go.jp)
2.
Nanoelectronics Research Institute, National Institute of Advanced Industrial Scienceand Technology, Tsukuba 305-8562, Japan
3
Multiferroic Project, ERATO, Japan Science and Technology Agency, Tokyo 113-8656,
Japan
4Japan Fine Ceramics Center (JFCC), 2-4-1 Mutsuno, Atsuta-ku, Nagoya, 456-8587,
Japan
5
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University,
Sendai 980-8577, Japan
6
Department of Applied Physics, University of Tokyo, Tokyo 113-8656, Japan

In half-doped perovskite manganese oxide RE1-xCaxMnO3 (x = 0.5) (RE: rare earth elements),
the charge/orbital ordering (CO/OO), being responsible for the ordering of Mn3+/Mn4+ with
1/1 accompanied by the eg-orbital ordering, are associated with the modulated crystal
structure with modulation vector Q = (0, 1/2, 0) 1. Accordingly, the CO/OO structure feature
can be certainly defined by analyzing the modulated crystal structure2-3. Different to stable
CO/OO structure observed in RE0.5Ca0.5MnO3 with pseudo-cubic structure and small
quenched disorder, the CO/OO structure in over-doped RE1-xSrxMnO3 (x>0.5) and layered
perovskite RE1-xCa1+xMnO4 (x>0.5) should be complex due to unbalance of Mn3+/Mn4+ orlayered structure, and hence multi-phase competition4. It is therefore desirable to study themodulated structure of over-doped manganites in CO/OO state.
In this study, the modulated structures of Sm1-xSrxMnO3 (x>0.5) and layered perovskite
Pr1-xCa1+xMnO4 (x>0.5) have been systematically investigated by low-temperature transmission
electron microscopy (TEM). In Sm1-xSrxMnO3 (x>0.5) with relatively large quenched disorder, thecommensurate CO/OO structure with modulation vector Q = (0, 1/3, 0) was observed above theA-type antiferromagnetic transition temperature (TNA ~ 180 K) 4. This modulation structure changes toan incommensurate one below TNA. In layered perovskite Pr1-xCa1+xMnO4 with small quencheddisorder, the incommensurate CO/OO is independent on temperature, and the modulation

wavenumber linearly decreases with increasing x.
These results reveal that in Sm1-xSrxMnO3 (x>0.5) the commensurate CO/OO structure with Q= (0, 1/3, 0) is fluctuated as it competes with A-type 4 antiferromagnetic structure, while inlayered perovskite Pr1-xCa1+xMnO4, the stable incommensurate CO/OO is seen, being
analogous to that observed in RE1-xCaxMnO3 (x > 0.5) 5.
References
1. “Colossal Magnetoresistive Oxides” edited by Y. Tokura, Gorden and Breach Scirnce Publisher, (2000).
2. X. Z. Yu, R. Mathieu, T. Arima, Y. Kaneko, J. P. He, M. Uchida, T. Asaka, T. Nagai, K. Kimoto, Y. Matsui
and Y. Tokura, Phys. Rev. B 75, (2007) p. 174441.
3. X. Z. Yu, Y. Tomioka, T. Asaka, K. Kimoto, T. Arima, Y. Tokura and Y. Matsui, Appl. Phys. Lett. 94,
082509 (2009).
4. Y. Tomioka, X. Z. Yu, T. Ito, Y. Matsui and Y. Tokura, Phys. Rev. B, in press.
5. G. C. Milward, M. J. Calderon and P. B. Littlewood, Nature 433, 607 (2005).

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P-135

Poster

Structural Studies of Ba2LaIrO6 and La2ZnIrO6 – Two
Monoclinic Perovskites With Different Space Groups
Qingdi Zhou, Brendan J. Kennedy
School of Chemistry, The University of Sydney, Sydney, NSW 2006 Australia(q.zhou@chem.usyd.edu.au)

For well over half a century the structural chemistry, electronic and magnetic properties of
ABO3 perovskites including the A2BB’O6 double perovskites, in which two different ions are
regularly ordered at the octahedral B-site have been of interest. The enormous flexibility ofperovskites allows the possibility of forming materials with highly tailored compositions, andhence structures and ultimately properties. The solid-state chemistry of mixed-metal oxides
containing ruthenium or iridium has attracted a great deal of recent research reflecting thediverse range of structures and electronic properties displayed by such oxides. For example,
the perovskite SrRuO3 is ferromagnetic below 160 K [1] and the layered perovskite Sr2RuO4
is a superconductor below 1 K [2].
Despite the strong correlation between structure and properties in perovskites accurate andprecise structures of numerous well studied examples are not available. Ba2LaIrO6 is a caseat point. This oxide was apparently first prepared by Thumm et al [3] who concluded that itwas cubic with ordering of the La and Ir cations. Ramos et al [4] reported the material was
actually orthorhombic without ordering of the La and Ir cations. In 1999 Wakeshima et al [5]also reported ordering of the cations but suggested the true symmetry was monoclinic in P21/n.
Most recently Fu and IJdo [6] concluded the symmetry was actually rhombohedral in spacegroup R3 , this space group allowing ordering of the two B-site cations. Whist differences in
preparative methods occasionally result in different symmetries; it is more common that thehigh pseudo symmetry and weakness of selected diagnostic reflections leads to uncertainty inthe choice of space group. This is especially true when the structures are determined bypowder X-ray diffraction methods utilising un-monochromated Cu radiation on laboratory
based diffractometers as employed in the above four experimental studies. Xiang et al [7]concluded from density functional theory calculations that the most likely structure of
Ba2LaIrO6 was rhombohedral.
The continuing interest in Ba2LaIrO6 prompted us to re-examine the structure of this oxideusing both synchrotron X-ray and neutron powder diffraction. Accurate and precise structures
for the two oxides La2ZnIrO6 and Ba2LaIrO6 are presented. The structure of La2ZnIrO6 ismonoclinic in space group P21/n in which both in-phase and out-of-phase tilting co-exist withthe rock-salt like ordering of the Zn and Ir cations. Careful analysis of the synchrotron
diffraction profile of Ba2LaIrO6 suggests that, at room temperature, this exists as a mixture of
monoclinic I2/m and rhombohedral R3 phases, both of which are characterised byout-of-phase tilting of the cation ordered BO6 octahedra. The pure rhombohedral phase is
obtained by heating the sample to 375 K, with further heating resulting in the loss of thetilting of the octahedra, the structure being in Fm3m .

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Cooling the sample induces an

AsCA’09

Posteradditional phase transition to a triclinic structure in I1 .
References
1. J. M. Longo; P. M. Raccah; J. B. Goodenough, J. Appl. Phys. 39 (1968) 1327.
2. Y. Maeno; H. Hashimoto; K. Yoshida; S. Nishizaki; T. Fujita; J. G. Bednorz; F. Lichtenberg, Nature 372(1994) 532.
3. I. Thumm; U. Treiber; S. Kemmlersack, J. Solid State Chem. 35 (1980) 156.
4. E. M. Ramos; I. Alvarez; R. Saezpuche; M. L. Veiga; C. Pico, J. Alloys Compounds 225 (1995) 212.
5. M. Wakeshima; D. Harada; Y. Hinatsu, J. Alloys Compounds 287 (1999) 130.
6. W. T. Fu; D. J. W. Ijdo, J. Alloys Compounds 394 (2005) L5.
7. H. P. Xiang; X. J. Liu; X. F. Hao; J. Meng; Z. J. Wu, J. Alloys Compounds 457 (2008) 571.

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AsCA’09

Poster

SMART BREEZE - The affordable high-quality
solution for Chemical Crystallography

P-136

Eric Hovestreydt1, Michael Ruf2, Holger Ott1
1
Bruker AXS GmbH, Oestliche Rheinbrueckenstrasse 49, D 76181 Karlsruhe, Germany(info@bruker-axs.de)2
Bruker AXS Inc., E. Cheryl Parkway 5, MADISON, WI 53711-5373, United States ofAmerica (info@bruker-axs.com)

An exceptionally easy to operate solution for users in chemical crystallography has become
available. The SMART BREEZE offers automated molecular 3D structure analysis ataffordable costs.
The air-cooled BREEZE 4K CCD detector sets the SMART BREEZE apart from traditional
water-cooled CCD systems. Nevertheless, the BREEZE offers the same or even higher data
quality when compared to most conventional water-cooled CCD cameras due to the extremely
low electronic noise of its CCD chip. Examples will be shown.
Despite of the moderate price the highly versatile fixed-chi goniometer is accurate and precise
and built for durability.
APEX2 software offers a high level of automation, is extremely easy to use, and provides
feedback with modern graphics. The highly intuitive software opens the field of
crystallography to synthetic chemists and novice crystallographers, giving access to fast andreliable structure determination. Publication-ready reports which are generated automaticallyin various formats and HTML reports will be shown and discussed.

Ready, set, screen: X8 PROSPECTOR

P-137

Eric Hovestreydt1, Matt Benning2, Marianna Biadene1
1
Bruker AXS GmbH, Oestliche Rheinbrueckenstrasse 49, D 76181 Karlsruhe, Germany(info@bruker-axs.de)2
Bruker AXS Inc. E. Cheryl Parkway 5, MADISON, WI 53711-5373, United States ofAmerica(info@bruker-axs.com)

The key for success in solving a protein structure is finding the best crystal. When screening a
myriad of candidates, it is important to have a highly reliable no-nonsense system, one thatkeeps working day and night.
The only way to find out how well your crystal diffracts is to put it in the X-ray beam. Why- 204 -

AsCA’09

Posterwaste your valuable synchrotron time screening crystals? The X8 PROSPECTOR is a systemdesigned to serve the demand for efficient screening, economical and reliable. It tells you
everything about your crystals prior to going to the beamline With its compact design andsmall footprint, it can be placed in any laboratory. The source is completely air-cooled andtherefore requires no external plumbing. It also uses regular, single-phase power, so it requires
no special electrical wiring. A microfocus sealed tube delivers X-rays equivalent in intensity
to a traditional 300 micron rotating anode generator. Coupled with the QUAZAR optics, thissource delivers a highly stable beam.
The rock-solid, most sensitive, fourth generation APEX II CCD detector is coupled with thispowerful source.
The X8 PROSPECTOR not only speeds up your screening work, it also takes you by the handthrough the whole process. The PROTEUM2 software controls the hardware and analyzes theresults to give quick and reliable answers to your questions.
A couple of examples will be presented showing how easily the X8 PROSPECTOR finds thejewels from your crystallization plates. Furthermore, we will discuss examples of a complete
structural data collection on proteins, peptides and pharmaceutical compounds.

Focusing Effects in Parabolic Shaped Multi-Plate
Crystal Cavity for X-rays

P-138

Y.-Y. Chang1 , S.-Y. Chen1, M.-T. Tang2, Yu. Stetsko2, M. Yabashi3, S.-C. Weng1,
C.-H. Chu 1, B.-Y. Shew2, and S.-L. Chang1
1.
Department of Physics, National Tsing Hua University, Hsinchu,Taiwan,300(d947301@oz.nthu.edu.tw)2
National Synchrotron Radiation Research Center, Hsinchu, Taiwan, 300
3Spring-8/RIKEN Mikazuki, Hyogo, JapanThe Fabry-Perot type multi-plate crystal cavities consisting of compound refractive lenses(CRL) on silicon wafers are prepared by using micro-electronic lithographic techniques. Eachrefractive lens is a parabolic shaped concave lens. The crystal orientation of this X-ray opticaldevice is the same as that of the two-plate x-ray resonators reported (Phys. Rev. Lett. 94,
174801, 2005). Experimentally, the transmitted X-ray beam size of the (12 4 0) backdiffraction through these monolithic silicon crystal devices is measured with a fine knife-edge.
The measurements show enhanced focusing effect from the CRL due to X-ray backdiffraction. Also observed is the energy-dependent focusing. Detailed analysis on cavity- 205 -

AsCA’09

Posterinterference and beam focusing will be discussed.

P-139

Bringing the power of synchrotron crystallography tothe chemical community
William Clegg, Ross W Harrington, Luca Russo
School of Chemistry, Newcastle University, Newcastle upon Tyne NE1 7RU, UK(w.clegg@ncl.ac.uk)

Between 2001 and 2008 the synchrotron component of the U.K. National Crystallography
Service, run from Newcastle, made extensive and frequent use of station 9.8 at Daresbury’s
Synchrotron Radiation Source, successfully and efficiently generating a large collection of
structures from difficult samples submitted by groups engaged in a wide range of chemical
and materials research. Station 9.8 had been constructed in a Newcastle-led project during
1994–1997 and established a reputation as the most productive facility of this kind in theworld, with a major international impact including serving as a model for other facilities
developed subsequently. Following the closure of the SRS, the service has transferred tobeamline I19 at Diamond Light Source and we have been among the first users to be allocatedtime there, as part of the ongoing commissioning phase of the new facility.
Our in-depth experience with challenging samples at Daresbury has enabled us to contribute
substantially to the development of the equipment and software of I19, identifying features for
improvement. By the time of the AsCA Meeting we will have made 8 visits to collect data
(6 already by June), with significant improvements already noted and more expected eachtime; we have now reached what can almost be considered as normal productivity operation
rather than commissioning and development. A variety of new structures have been
determined, and we have addressed interesting problems including twinning, major disorder,
superstructures, and compounds of which the true chemical identity was quite unexpected.
We will give an account of some of the main features of the beamline from a users’ point ofview, describe some of our experiences, and present a selection of new results to demonstrate
what can be achieved with this facility, even in its early days. Funding for continuation of
the National Service is currently being sought. There are useful lessons here for otherfacilities.

Optimization of parameters for new rotation function

P-140

Wei Ding 1,FanJiang 2
1
Institute of Physics, Chinese Academy of Sciences, No.8 South Third Street
ZhongGuanCun, Haidian District, P.O.Box603, Beijing, 100190, China(wding@bio.iphy.ac.cn)
2Institute of Physics, Chinese Academy of Sciences, Beijing, 100190, China(fjiang@aphy.iphy.ac.cn)

A new rotation function calculated by matching the search model directly with the Patterson
vector map had been described by our recent works (Jiang, 2008). The results of that work
were encouraging but the parameters seemed to be dependent on the specific models and- 206 -

AsCA’09

Poster

crystal structures, so designing a way of optimizing or screening for a best set of parameters isnecessary. In this work, we consider that the correct solutions are the signal and the random
ones are the noise. We first demonstrate that the signal-to-noise ratio is a valid criterion inparameters choice. But when the correct solution is unknown, the value of signal can not becalculated. However, we further verify that the value of noise is a suitable criterion too.
According to the second criterion, we get the optimized parameters, and our final works showthat the satisfactory test results can be deduced by them.
Reference
Jiang, F. (2008). Acta Cryst. D64, 561-566.

The current status of versatile neutron diffractometer
iMATERIA at J-PARC

P-141

Toru Ishigaki1, Akinori Hoshikawa1, Masao Yonemura2, Kenji Iwase1, D. S.
Adipranoto1, Hidetoshi Oguro1, Takahiro Morishima3, Takashi Kamiyama3, Ryoko
Oishi3, Kazuhiro Mori4, Ryoji Kiyanagi5, Kazuya Aizawa6, Makoto Hayashi7
1
Frontier Research Center for Applied Nuclear Sciences, Ibaraki University, Tokai,
Naka, Ibaraki, 319-1106, JAPAN (toru.ishigaki@j-parc.jp)
2
Institute of Applied Beam Science, Ibaraki University, Hitachi, Ibaraki, JAPAN3
Neutron Science Laboratory, KEK, Tsukuba, Ibaraki, JAPAN
4
KUR, Kyoto University, Kumatori, Osaka, JAPAN5
IMRAM, Tohoku University, Sendai, Miyagi, JAPAN6
J-PARC Center, JAEA, Tokai, Naka, Ibaraki, JAPAN
7
Ibaraki prefecture, Mito, Ibaraki, JAPANIbaraki prefecture, the local government of the area where J-PARC sites in Japan, has decided
to build a versatile neutron diffractometer (IBARAKI Materials Design Diffractometer,
iMATERIA) to promote industrial applications for neutron beam in J-PARC. iMATERIA isplanned to be a high throughput diffractometer so that materials engineers and scientists canuse this diffractometer like the chemical analytical instruments in their materials development
process. It covers the d in range 0.18 < d (Å) < 5 with Δd/d = 0.16 % at high resolution bank,and 5 < d (Å) < 800 with the resolution changing gradually at three detector banks of 90
degree, low angle and small angle. It takes several minutes to obtain a ‘Rietveld-quality’ data
for the X-ray laboratory sized sample measured at 1MW. Currently, the beam power islimited for tuning the accelerator, so that the standard measuring time is about one to twohours. To promote industrial applications, a utilization system of this diffractometer isrequired. Since several tens to thousands experiments will be carried out in one year, we haveto prepare an automatically sample exchange system and special large numbers of sample
holders. The analysis software is also very important for powder diffraction data, so that we
prepare a software package consisting of combination of several powder-diffraction software,structural databases and visualization. The construction of iMATERIA was completed as oneof the day-one instruments at J-PARC and the beam-on commissioning was started since May
2008. The recent data of iMATERIA will be reported.

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AsCA’09

Poster

Fig.1 IBARAKI Materials Design Diffractometer, iMATERIA
without detector for each bank and instrument shieldings.
High-resolution bank, special environment bank (90 degreebank), low angle bank, can be seen from right to left. and small
angle detector bank, which are not shown in picture, aresituated in the low angle vacuum chamber (left hand of thepicture).

P-142

Study on membrane chain-chain packing by grazing
incident X-ray diffraction
Ming-Tao Lee
National Synchrotron Radiation Research Center, Taiwan (mtlee@nsrrc.org.tw)

Membrane structure is very important issue for cell. Membrane is not only the “wall” forprotecting cell but also the interface for exchanging signal, ions and molecules. Manyevidences show that membrane protein will fold to functional structure by associating withsuitable membrane structure. Lipid chain-chain packing is one of important structures andwill affect membrane thickness, lipid lateral diffusion and membrane domain formation. We
will use grazing incident X-ray diffraction to probe lipid chain-chain packing. The 12keV
X-ray light source in BL13A beam line of NSRRC and home-made humidity-temperature
controlled chamber will be applied in the measurements. The ion channel peptide Gramicidin
A and cholesterol will be used to interact with model membrane to study their effect on
chain-chain packing.

P-143

Imposition of multiple F constraints in the maximum
entropy method
Koichi Momma and Fujio Izumi
Quantum Beam Center, National Institute for Materials Science, 1-1 Namiki, Tsukuba,
Iaraki 305-0044, Japan (MOMMA.Koichi@nims.go.jp), (IZUMI.Fujio@nims.go.jp)

The maximum entropy method (MEM) is used for reconstruction of the least-biased
distribution of electron or nuclear densities from X-ray or neutron diffraction data by
maximizing the information entropy S under some constraints. Because the errors of observed
structure factors, Fo(hi), for reflec- tions hi should have Gaussian distribution ideally, theso-called F constraint is usually imposed on calculated structure factors F(hi):,(1)

where N is the total number of reflections, and σ(hi) is the standard uncertainty of |Fo(hi)|.
However, the above constraint has a serious disadvantage that the distribution of thenormalized residuals of the structure factors, ΔF(hi)/σ(hi) = [|Fo(hi)|−|F(hi)|]/σ(hi), tend todeviate from the expected Gaussian distribution. The Gaussian distribution of the errors is a
- 208 -

AsCA’09

Posterprerequisite for Eq. (1), which, however, does not always ensure the Gaussian distribution ofΔF(hi)/σ(hi).
In order to improve the histogram of ΔF(hi)/σ(hi), Palatinus and van Smaalen [1] proposed thegeneralized F constraint defined as,(2)

where mn is the even n-order central moment of the normalized Gaussian distribution. CF2
corresponds to constraint (1). Although CFn constraints with n = 4–8 provide us with better
histograms of ΔF(hi)/σ(hi) with less artifacts in reconstructed electron densities, none of theconstraints are sufficient to constrain the histogram to the Gaussian shape.
In this study, a new computer program has been written in C++ to impose a set of multiple F
constraints with different orders of n. The normalized electron density, ρk, with the maximum
S under the multiple constraints CFn (n = 2, 4, 6, ···) is given by,(3)

where the suffixes k and k′ denote positions in the unit cell, and λn is the Lagrangian multiplier.
Equation (3) cannot be solved analytically because both sides of Eq. (3) contain ρk. Our new
program adopts 0-th order single pixel approximation [2] to solve Eq. (3) by iterative
calculations with λn values dynamically adjusted in every cycle. Simultaneous imposition of
two or three Fn constraints with different n led to artifact suppression in the resulting electron
densities. The number of iterations required for the convergence of MEM analysis is also
reduced, even when convergence is hardly achieved by imposing the classical F constraint.
Some examples of applying the new methodology of MEM to single-crystal and powder
diffraction data will be presented.
References[1] Palatinus, L. & van Smaalen, S. (2002). Acta Cryst. A58, 559–567.
[2] Kumazawa, S., Takata, M. & Sakata, M. (1995). Acta Cryst. A51, 47–53.

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AsCA’09

PosterSynchrotron Radiation Beamline for Macromolecular
Assemblies Operated by the IPR at SPring-8(BL44XU)

P-144

Eiki Yamashita1, Masato Yoshimura1,2, Mamoru Suzuki1, Kazuya Hasegawa3,
Yukito Furukawa3, Toru Ohata3, Takashi Kumasaka3, Go Ueno4, Masaki
Yamamoto4, Shinya Yoshikawa5, Tomitake Tsukihara1,5, Atsushi Nakagawa1,*
1
Institute for Protein Reseach, Osaka University, 3-2 Yamadaoka, Suita, Osaka
565-0871, Japan (*atsushi@protein.osaka-u.ac.jp)
2
Taiwan NSRRC, Taiwan Beamline Office at SPring-8, 1-1-1 Kouto, Sayo-cho,
Sayo-gun, Hyogo 679-5148, Japan
2
JASRI/SPring-8, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan
3
RIKEN/SPring-8, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan
4
Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho,
Ako-gun, Hyogo 678-1297, Japan

Biological macromolecular assemblies play significant roles in many biological reaction
systems, such as energy transfer, protein synthesis, signal transduction, molecular motors andso on. Detailed understanding of the functions of the macromolecular assemblies requires
information derived from three-dimensional atomic structures. X-ray crystallography is one of
the most powerful techniques to determine the three-dimensional structures ofmacromolecular assemblies at atomic level.
It is usually be known that biological macromolecular assembles are difficult to be
crystallized or grown to larger size crystals. In addition, the unit cells of these crystals arequite large. Because of these features of the crystals of biological macromolecular assemblies,
it is usually very difficult to obtain good diffraction data. The difficulties of diffraction datacollection of biological macromolecular assembles are as follows; extremely weak diffraction
power, narrow space between diffraction sports, x-ray radiation sensitive etc. High brillianceand highly paralleled synchrotron radiation from the undulator is an extremely powerful toolfor diffraction data collection from macromolecular assembly crystals with large unite cell.
The Institute for Protein Research (IPR) of Osaka University is operating a beamline forcrystal structure analysis of biological macromolecular assemblies at SPring-8 (BL44XU).
This beamline is specially designed to collect high quality diffraction data from biologicalmacromolecule assembly crystals with large unit cells. The light source of this beamline is a
SPring-8 standard type in-vacuum undulator. Liquid nitrogen cooled double crystal
monochromator and horizontal focusing mirror areused as the optical components. A newly designed
high precision diffractometer combined with a
specially designed large image-plate detector,
DIP6020, is installed. Recently, BSS (Beamline
Scheduling Software), which is SPring-8 protein
crystallography beamline standard GUI, is installed
to unify user operation throughout protein
crystallography beamlines in the SPring-8.
Diffraction data from crystals of biological macromolecular assemblies with large unit cell(over 700 angstrom) has been collected higher than 3.5 Å resolution.
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AsCA’09

PosterPresent status and the future plan of the beamline will be discussed.

P-145

X-ray diffraction from crystals in crystallization
plates
Tadeusz Skarzynski
Oxford Diffraction Ltd., Oxford Industrial Park, Yarnton, Oxfordshire, OX5 1QU,
United Kingdom. (tadeusz.skarzynski@oxford-diffraction.com)

The PX Scanner is a unique instrument from Oxford Diffraction enabling the identificationand characterization of protein crystals with X-rays, in-situ, in the crystallization plate. The
PX Scanner addresses the bottleneck in high-throughput crystallization allowing aquantitative evaluation of the diffraction properties of crystals without having to manually
extract crystals from the crystallization plate. Combining an optical imaging system with apowerful, micro-focus Cu X-ray source, highly sensitive CCD detector and intuitive software
provides an essential laboratory resource for crystallographers involved in difficult structural
biology projects.
The PX Scanner is now further enhanced with new software named CrystalEyes which
expands the functionality of the instrument, utilizing new algorithms to improve theacquisition and quality of the optical and X-ray images. Furthermore, new database accesscapabilities allow the data to be easily output from the PX Scanner and integrated with a‘LIMS’ style lab data management system.
We will show how the PX Scanner can be used as a powerful tool providing valuable
information at all stages of macromolecule crystallization, including differentiating salt fromprotein crystals in initial screens, selecting the best crystals for synchrotron X-ray datacollection, optimizing harvesting, cryo-protecting and soaking conditions, and determining
crystal lattice parameters.

Electrostatic potential as an experimental or atheoretical tool for a better understanding of druginteractions

P-146

Anne Spasojević – de Biré1 and Nour Eddine Ghermani2
1
Laboratoire “Structures Propriétés et Modélisation des Solides”, UMR 8580 du CNRS,
Ecole Centrale Paris, 92295 Châtenay-Malabry, France (anne.spasojevic@ecp.fr)
2
Laboratoire Physico-chimie, Pharmacotechnie, Biopharmacie, UMR 8612 du CNRS,Paris-Sud, Faculté de pharmacie, 92296 Châtenay-Malabry, France(noureddine.ghermani@u-psud.fr)

High-resolution X-ray diffraction and theoretical calculations allow a fine characterization ofthese electronic and electrostatic properties in crystals, which is essential to the understanding
and prediction of the interaction of drugs with the biological targets (pharmacology) andexcipients (formulation). This fundamental approach can have important consequences forpractical applications in the areas of drug design or drug delivery.
Our collaborative work has enabled us to answer several questions posed by medicinal- 211 -

AsCA’09

Posterchemists or galenists, in particular relative to the following topics:- Electronic and electrostatic properties of racemic ibuprofen- Electronic and electrostatic properties of a complex of zinc aspirin- Understanding of the crystallization of busulfan, a pediatric cancer chemotherapeutic
drug, and development of a new formulation (encapsulation in a cyclodextrine derivate)- Experimental and theoretical electrostatic properties of styrylquinoline-based compounds
as new inhibitors in the integrase of the HIV-1 (figure 1a)- Understanding of the reactivity toward nucleophile agent: a putative intermediary productin the total synthesis of cephalotaxine (antileukemic agent) (figure 1b)- Electronic and electrostatic properties of co-crystal of decavanadate – cytosine,compound implied in the activity or inhibition of various enzymes (phosphotransferases, Ca2+
ATP-ase, adenylate kinase, …)- Experimental and theoretical electrostatic properties of salicyladehyde thiosemicarbazone,a pharmacophore of trombopoietin mimics, one of the simplest ligands in thethiosemicarbazone family.

ab
Figure 1. a) Molecular surface of a styryl-quinoline based compound colored by theoretical electrostatic
potential values. b) Molecular surface of cephalotaxine colored by experimental electrostatic potential
values.

The Effect of Disk Chopper Phasing on Neutron Beam
Spectrum of SuperHRPD at J-PARC

P-147

Teguh Yulius Surya Panca Putra1,2, Shuki Torii2, Junrong Zhang2, Takashi Muroya2,
Setsuo Sato2, Takashi Kamiyama2
1
The Graduate University for Advanced Studies (SOKENDAI), SOKENDAI-KEK Office,
1-1 Oho, Tsukuba 305-0801, Japan (panca@post.kek.jp)
2
High Energy Accelerator Research Organization, KEK Tokai Campus, 2-4 Shirakata
Shirane, Tokai, Naka, Ibaraki 319-1195, Japan

Experimental results on various phasing of disk chopper at Super High Resolution Powder
Diffractometer (SuperHRPD) BL08 of J-PARC are reported. SuperHRPD is a neutron powder
diffractometer at Materials and Life Science Facility (MLF), Japan Proton Accelerator
Research Complex (J-PARC). SuperHRPD looks at a decoupled poisoned hydrogenmoderator and within approximately 100 m total flight path, SuperHRPD is characterized by
its world best resolution Δd/d = 0.03% at d < 4 Å with d-range 0.5 < d [Å] < 60. Identificationof individual intensities of Bragg reflection can be more easily conducted with this highresolution of SuperHRPD. It will also enable the study of more complicated structure
resulting in better reliability in obtained structure parameters.
- 212 -

AsCA’09

PosterThree disk choppers are used to select the desired wavelength range of the neutron beam fromthe source, whose repetition rate of 25 Hz. First disk chopper (DC1) was installed at 7.1 mfrom the moderator, while DC2 and DC3 installed at 12.725 m and 12.775 m, respectively.
During the experiment, DC1 were kept rotated at frequency of 8.33 Hz, while DC2 and DC3
were open stopped. Phasing of DC1 was varied from -50o until +30o in 5o increment, relative
to the position of neutron beam guide tube. Fig. 1 shows that pashing configurations of thedisk chopper gave different neutron beam spectrums. Disk chopper phasing in this experiment
selected an area from the initial neutron spectrum leaving the moderator with different
wavelength width. For example, DC1 phasing at +10o (in Fig. 1) will limit the wavelength
until 4.58 Å as shown in path-time diagram in Fig. 2. Disk chopper phasing, therefore, enable
us to pick out any incident wavelength that we choose. The result from this experiment will be
useful in selecting the wavelength width of neutron for experiments with different purposes.

300
Ph +5
200
Ph +10
Ph +15100
Ph +300o20

Ph +2540o

Ph +2060Time (msec)

o

60

o

40

DC3

o

20

o

80

Monitor80

Ph 0

Intensity

λ2 = 4.58 Å

100

400

100

120

Figure 1. Neutron spectrum resulted showing
the effect of disk chopper phasing.

DC2
DC1

0

120

Time (msec)

240

360

Figure 2. Path-time diagram showing DC1 phasing+10o as shown in Fig. 1.

References
1. R.M. Brugger, Mechanical and Time-of-flight Techniques, in: P.A. Egelstaff (Ed.), Thermal Neutron
Scattering, Academic Press, New York, 1965 (Chapter 2)
2. C.G. Windsor, Pulsed Neutron Scattering, Taylor & Francis Ltd., London, 1981
3. J.R.D. Copley, Nucl. Instr. and Meth. in Physics Research A 273 (1988) 67
4. J.R.D. Copley, Nucl. Instr. and Meth. in Physics Research A 303 (1991) 332
5. T. Ishigaki et.al., Journal of Neutron Research 13 (1-3) 2005

A Novel Mounting Tool Using Adhesive for Protein
Crystals

P-148

Tomoya Kitatani1,2, Tomokazu Hasegawa3, Shigeru Sugiyama1,2, Kensaku Hamada3,
Hiroaki Adachi1,2,4, Hiroyoshi Matsumura1,2,4, Satoshi Murakami2,4,5, Tsuyoshi
Inoue1,2,4, Yusuke Mori1,2,4, Kazufumi Takano1,2,4
1
Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan(ktakano@mls.eng.osaka-u.ac.jp)
2
CREST JST, Suita, Osaka 565-0871, Japan
3
PharmAxess Inc., Ibaraki, Osaka 567-0085, Japan
4SOSHO Inc., Osaka 541-0053, Japan
5
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology,
Yokohama 226-8503, Japan

We have developed a novel mounting tool, Crystal Catcher, for protein crystals that directly
captures a crystal from a drop with an adhesive (Kitatani et al., 2008, 2009). This tool has aloop-free structure and can reduce the amount of solution around the captured crystal in- 213 -

AsCA’09

Postercomparison with conventional loop-based mount tools. The crystal caught by the Crystal
Catcher is immediately mounted in a stream of nitrogen gas held at 100K for XRD
measurement. We have developed Crystal Catchers CT-100, CT-200, CT-300 and CT-400,
which adopt different types of adhesive and nozzle materials. CT-100 and CT-300 are suitablefor fragile crystals and crystals in aqueous solutions. CT-200 and CT-400 are appropriate forextracting a protein crystal from high-viscosity or organic solutions. CT-300 and CT-400
enable the capture of small crystals 50μm in size. We are now able to manipulate crystals of
various sizes and in various conditions using the series of the Crystal Catcher devices.
The extra solution around captured crystal not only degrades the quality of data-collection
statistics but also disturbs the initial phase determination by the sulfur single-wavelength
anomalous diffraction (SAD) method. The effect of reducing the solution in this tool is
helpful in the sulfur SAD method. We have evaluated the effects of our tool on a quality andcrystallographic data in the sulfur SAD method using Co Kα radiation.
References
1.
2.

Kitatani et al. (2008) Appl. Phys. Express 1, 037002.
Kitatani et al. (2009) Jpn. J. Appl. Phys. 47, 8995.

P-149

New Possibilities for X-ray Diffractometry: Brighten
Up Your Home-Lab
J. Wiesmann, T. Samtleben , B.Hasse, J. Graf, C.Michaelsen
Incoatec GmbH, Max-Planck-Straße 2, D-21502 Geesthacht, Germany(administration@incoatec.de)The latest developments in new X-ray microfocus sources lead to new possibilities in X-ray
diffractometry. Using the new Incoatec Microfocus Source (IµSTM) with the latest kind of
two dimensional focussing Montel optics, the so called QuazarTM optics, in combination
with a two dimensional detector allows high quality diffractometry measurements with very
good resolution of very small and weakly scattering samples in the home-lab in short time.
Foto of Incoatec Microfocus Source:

The advantages of the new 30 W air cooled IµS with a focal spot size below 50 µm arepresented. The use of IµS is as easy as for all sealed tube systems and the performanceexceeds typical combinations of traditional rotating anodes with multilayer optics. With afocussing optics IµS achieves in a single crystal diffraction set-up a flux above 3•10E08 cps
in a 250 µm spot with Cu-K or a flux above 10E07 cps in an 110 µm spot for Mo-K radiation.
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AsCA’09

PosterFor SAXS experiments there is also an IµS available with a 2 dimensional collimating optics.
Various examples of new application measurements on different X-ray samples are shown,like proteins, small molecules and SAXS, proving the broad field of applicability of the IµS.

P-150

Desktop Minstrel UV™: A Novel Protein Crystal
Monitoring Automation System Using UVFluorescence Microscopy
Jian Xu, Craig Sterling and Michael Willis
Rigaku Automation, 5999 Avenida Encinas, Suite 150, Carlsbad, CA 92008

Identifying protein crystals in crystallization droplets has long been considered a challenging
step in the field of protein crystallography. Although there are numerous automatedcrystallization robots readily available, none have been able to successfully monitor crystal
growth by distinguishing protein crystals from non-protein crystals and detecting crystals
from drops that are otherwise difficult to see with visible light. In order to fulfill this criticalneed, Rigaku has developed a novel protein crystal monitoring automation system, theDesktop Minstrel UV™, which uses UV fluorescence microscopy. The system includes anultraviolet microscope with at least one ultraviolet light emitting diode, providing illumination
with the wavelength matching the absorption of the fluorescing amino acids, such as
tryptophan. To greatly decrease photo-damage to the protein crystals, the fluorescing lightilluminated on the sample is reduced to the minimum and is then digitally recorded by acamera with a CCD sensor. We have conducted crystallization experiments with various
proteins in order to evaluate this system. The resulting UV images from these experiments
clearly reveal the protein crystals from non-protein crystals, such as salts. In addition, this UV
crystal monitoring system is built upon the platform of Rigaku’s state-of-art imaging
automation technology, the Desktop Minstrel™, which makes the evaluation of a large
number of crystallization experiments possible. The Desktop Minstrel UV enables researchers
to accurately harvest protein crystals for data collection or design follow-up experiments.

SAXS/WAXS Experiments with a Single Detector

P-151

Naoto YAGI1,2 and Noboru OHTA1
1
Japan Synchrotron Radiation Institute, SPring-8, 1-1-1 Kouto, Sayo, Hyogo 679-5198,
Japan. (yagi@spring8.or.jp)
2
RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Japan.

There is an increasing demand to record the wide-angle X-ray scattering/diffraction (WAXS)
in small-angle X-ray scattering/diffraction (SAXS) experiments. For this purpose, it iscommon to use two detectors, each one for SAXS and WAXS. However, this method has
drawbacks: (1) The region between the two detectors, medium-angle region, cannot berecorded. (2) The WAXS detector tends to be a linear detector which is unsuitable for acomplicated oriented diffraction patterns. (3) Sometimes it is hard to match exposures of thetwo detectors. It is obviously ideal to cover a large range of the scattering with a single
detector.
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AsCA’09

Poster

For this reason, we have been trying large-area detectors for SAXS/WAXS measurements.
One detector is RIGAKU RAXIS-VII image plate detector at BL40B2 in SPring-8. Thisdetector has an area of 300mm x 300mm with a 100umx100um pixel. In a diffraction patternfrom a lipid, a series of reflections in the small-angle region and the reflections at about 0.41
nm-1 that appears at around 0.24 nm-1. The former is from the lamellar structure, and thelatter from the lateral packing of the lipid molecules in the bilayer.
Another detector we are using is RIGAKU Jupiter210 at BL45XU. The detector waspreviously used for protein crystallography data collection. The hutch B of this beamline wasconverted to the SAXS/WAXS station by bringing a bench for small-angle scattering. The
typical sample-to-detector distance is 500 mm. The X-ray wavelength of 0.09 nm is usuallyused. The beam stop is 2mm in diameter, which enables us to measure the small-angle
region up to 1/30 nm-1. Jupiter210 comprises of four CCDs with tapered fibers. The area is
210mmx210mm. By placing the beam stop at the lower area of the detection area, it ispossible to cover down to 1/0.25 nm-1 in the wide-angle region. Since the readout of
Jupiter210 (<10 sec) is faster than that of RAXIS-VII (>60 sec) and the flux of BL45XU(undulator beamline) is higher than that of BL40B2 (bending magnet beamline), this system issuitable for scanning SAXS/WAXS experiments.
It is clear that a detector with a larger area and fast readout is ideal for SAXS/WAXS
experiment. A example of such a detector is ADSC Quantum-315 or MAR MX-325. Anothertechnique required is a large vacuum window. The design of the entrance “nose” of thevacuum chamber that does not block WAXS is also important.

P-152

Fully automated data collection system atmacromolecular crystallography beamlines in the
Photon Factory
Yusuke Yamada, Naohiro Matsugaki, Masahiko Hiraki, Leonard M.G. Chavas,
Noriyuki Igarashi and Soichi Wakatsuki
Structural Biology Research Center, Photon Factory, Institute of Materials Structure
Science, High Energy Accelerator Research Organization, 1-1 Oho, Tsukuba, Ibaraki,
3050801, Japan (yusuke.yamada@kek.jp)

Structural biology research center in the Photon Factory has pursued the enhancements ofsynchrotron beamlines for macromolecular crystallography [1]. Recently, we have constructed
a new beamline, AR-NE3A, which is dedicated for a high-throughput data collection requiredin pharmaceutical application. At AR-NE3A, we could obtain the highest photon flux at the
sample position among high-throughput beamlines at the Photon Factory. In the experimental
hutch, a high precision diffractometer, a fast-readout and high-gain CCD detector, and asample exchange system able to handle more than two hundred cryo-cooled samples stored ina Dewar, have been installed. Consequently, data set collection from a large number ofsamples can be carried out within a day. To facilitate high-throughput data collection requiredfor pharmaceutical researches, fully automated data collection and processing systems havebeen developed.
In this system, a user prepares a file describing a experimental schedule and data collection- 216 -

AsCA’09

Postercondition of each sample. In each cycle, a sample is exchanged by the sample exchangesystem and centered by recognizing a shape of the loop. After the centering of the sample,
data set collection is carried out based on a user pre-defined condition. Once the data set iscollected, this data set is automatically submitted to data reduction software. Finally, allcycles are completed, a brief summary containing pictures of a sample after the centering,
diffraction image and data reduction statistics is reported.
This system is operated since April 2009 and utilized in actual pharmaceutical research during
beam time term April-June 2009. In the presentation, some results and statistics during thisbeam time term will be shown.

Sample exchange
CCD detector
systemDiffractometer

Figure. Experimental apparatus in the end station of AR-NE3A

Reference
Hiraki et al. “Current status and developments of macromolecular crystallography beamlines at the Photon
Factory” Joint Conference of the Asian Crystallographic Association and Chinese Crystallographic Society
Oct. 22nd –25th , 2009, Beijing, China- 217 -

AsCA’09

PosterDevelopment of a New Rietveld Code as Powder
Diffraction Analysis Suite, Z-Code

P-153

Masao Yonemura1, Takahiro Morishima2, Ryoko Oishi2, Dyah Sulistyanintyas3,
Hidetoshi Oguro3, Kenji Iwase3, Akinori Hoshikawa3, Toru Ishigaki3, Kazuhiro
Mori4, Ryoji Kiyanagi5, Junrog Zhang2, Teguh Panca2, Shuki Torii2, and Takashi
Kamiyama2
1
Institute of Applied Beam Science, Ibaraki University, 4-12-1 Nakanarusawa, Hitachi,
Ibaraki, 316-8511 Japan (yonemura@mx.ibaraki.ac.jp)
2
Institute of Materials Structure Science, High Energy Accelerator Research
Organization, 1-1 Oho, Tsukuba, Ibaraki, 305-0801 Japan
3
Frontier Research Center for Applied Atomic Sciences, Ibaraki University, 162-1
Shirakata, Tokai, Naka, Ibaraki, 319-1106 Japan
4
Kyoto University Research Reactor Institute, Kumatori, Sennan, Osaka, 590-0494
Japan
5
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University,
2-1-1 Katahira, Aoba, Sendai, Miyagi, 980-8577 JapanNew Japanese Spallation Neutron Source (JSNS), Materials and Life Science Facility (MLF)
in Japan Proton Accelerator Research Complex (J-PARC) has been inaugurated. Fourdifferent powder diffractometers (Super High Resolution(S-HRPD), High Throughput(iMATERIA), Engineering(TAKUMI), Total Diffraction(NOVA)) have already put out thefirst great data. Furthermore, two more diffractometers have been proposed. In this situation,
new powerful and useful analysis software for powder diffraction data is desired. Since 2004,
the powder diffraction group in J-PARC has started to develop a new powder diffraction
analysis suite, Z-Code (code-name for the development), which was presented in previous
AsCA and IUCr. Fig.1 shows the overview of Z-Code. It is the integrated environment forfinding out crystal structures using various analysis methods from powder diffraction data.
For example, It has the general functions of Indexing, Peak Searching, Structure Matchingfrom a Data Base, and Conventional Rietveld analysis. Z-Code also supports Texture analysis,
Profile analysis, Fourier synthesis, and Maximum Entropy Method as the advanced analysis
components.

Fig. 1 The overview of Z-Code. Z-Code is still
under development for both professional andbeginners.

We just released and began to test the new Rietveld analysis software called “Z-Rierveld”
with the first users of the powder diffractometers in J-PARC. Z-Rietveld is the one componentof Z-Code. It has a Graphical User Interface (GUI) and many powerful features for therefinement of crystal structures. Z-Rietveld has demonstrated nice refinements of acomplicated structure models using multiple data sets, such as x-ray and neutron ones. In this- 218 -

AsCA’09

Posterpresentation, more features and details of Z-Rietveld will be discussed.

Study of Time Rebinning for Super High Resolution
TOF Neutron Diffraction

P-154

Junrong Zhang, Shuki Torii, Teguh Panca Putra, Takashi Muroya, Takahiro
Morishima, Ryoko Oishi, Takashi Kamiyama
Institute of Materials Structure Science, High Energy Accelerator Research
Organization, 2-4 Shirakata Shirane, Tokai, Ibaraki 319-1195, Japan(jrzhang@post.kek.jp)

High resolution becomes increasingly important for studying tiny structural changes andsubtle microstructures of materials. SuperHRPD@J-PARC is the world highest resolution
neutron powder diffractometer of its type, with the resolution ofΔd/d = 0.03% in thebackscattering detector. However the high resolution is gained at the cost of intensity, byincreasing the neutron flight path. Hence, it is significantly useful to rebin the TOF data on thehigh-precision structure refinements.
The calibration run of NIST Silicon was performed at SuperHRPD. Only the data collected on
the backscattering bank were used for Rietveld analysis. The neutron diffraction pattern isplotted in Fig.1, where the data have been corrected for incident spectrum including thecontribution of holder and empty. Due to the low statistics in some measurements, the time channel
rebinning routine is utilized to enhance the typical 'Rietveld-quality' data. Rebinning acrossthe whole TOF spectrum is carried out in the bin groupings of like 8 or 16, etc, by thesummation of points with increasing steps or weights. (The schemes of weight are shown as
stepwise curves in Fig.1.) It will reduce the estimated standard deviation on each point. The
well-defined instrumental line shape and extremely sharp peaks can be obtained. As indicatedin Fig.2(a), all features are preserved in bin grouping of 8, and however there is clearly a lossof information in Si (311) peak using a bin grouping of 16. That is the price for time rebinning.
Therefore careful consideration must be paid in case of peak overlap and reflection splitting.
In addition, it can be seen from Fig.2(c) that the statistic fluctuation in the background issuppressed largely.
More importantly, time rebinning can decrease the number of points across the diffraction
profile. The data were analyzed with the Rietveld method using the Z-Code, GSAS, and
FullProf software. It was concluded that refinement procedure could be speeded up
dramatically, and the convergence was easier to be approached. High reliable fits and goodbackground subtraction were achieved, that Rp factors given by GSAS are 11.01%, 8.87%,
and 7.97% for data with no binning and in bin groupings of 8 and 16, respectively.
Additionally, we also found that different bin groupings have subtle effects on the structure
and profile function parameters. In summary, the time rebinning is proved to be very effective
for Rietveld refinement of high resolution TOF diffraction data.

- 219 -

AsCA’09

Fig.1 The observed and calculated diffraction
patterns and their differences, with no binningand in bin groupings of 8 and 16, respectively.
The lower and upper stepwise curves illustrate
the schematic representations for bin groupingsof 8 and 16, respectively.

Poster

Fig.2 a), b), and c) are observed Si (311) peak,calculated Si (400) reflection, and background,with no binning and in bin groupings of 8 and16, respectively.

- 220 -

AsCA’09

P-155

PosterEchidna High-Resolution Neutron Powder
Diffractometer at OPAL: one year of experience andexperiments
Maxim Avdeev, James Hester
Bragg Institute, Australian Nuclear Science and Technology Organisation, PMB 1,
Menai, 2234 NSW, Australia (Maxim.Avdeev@ansto.gov.au)

A new high-resolution neutron powder diffractometer “Echidna”* is now fully operational at
the OPAL reactor (Australian Nuclear Science and Technology Organisation) and has been
open to the international community since mid-2008. Access is via calls for proposals twice ayear (May/November) and a “mail-in” service** for rapid turnaround.
The instrument is well suited for studying a wide variety of materials, ranging from those witha high degree of structural disorder to materials with long-period magnetic lattices. This
flexibility arises from the combination of Ge{hhl} monochromators with a continuously
variable take-off angle (90-140º) providing access to wavelengths from 1 Å to 3.2 Å and ad-spacing range of 0.5 to 30 Å.
Selection of 5’ or 10’ primary and secondary collimators, in addition to the natural α1 and α2
horizontal divergence options (~12’-38’ and ~20’-40’ depending on the wavelength used,
respectively), adds considerable flexibility in adjusting the “intensity/resolution” balance.
This enables the instrument configuration to be matched to sample complexity. If required,
Echidna may be configured to reach a resolution of Δd/d~5 x 10-4.
Variable vertical focusing of the monochromator and a large array of 128 position-sensitive
He detectors results in data collection times that are relatively short for a high-resolution 2θ
scanning powder diffractometer. Depending on the selected instrument configuration, sample
composition, and sample size these times are typically between 1 and 6 hours. An extra gainin peak/background ratio is achieved by using a custom-built vacuum chamber for room
temperature experiments.
3

The details of design and data treatment software and recent experimental results will bepresented.
*

www.ansto.gov.au/research/bragg_institute/facilities/instruments/echidna/specifications
www.ansto.gov.au/research/bragg_institute/users

**

P-156

WebCSD – on-line access to the Cambridge
Structural Database and applications in chemical
education
Gary M. Battle
Cambridge Crystallographic Data Centre (CCDC), 12 Union Road, Cambridge CB2
1EZ, UK (battle@ccdc.cam.ac.uk).

The Cambridge Structural Database (CSD) serves as the worldwide repository ofsmall-molecule organic and metal-organic crystal structure data. As such, this unique databaseof one-half million molecules is a crucially important resource for chemical education.
- 221 -

AsCA’09

PosterHowever, despite this abundance of experimental data, many aspects of structural chemistry
are still taught using 2-D drawings, or idealized 3-D models.
The CSD is provided with a range of sophisticated search and analysis tools. Whilst thesetools enable crystallographers, structural chemists and the drug design community to extract
vital structural knowledge, the requirement to install and become familiar with an extensive
suite of software can be a barrier for the non-expert user.
WebCSD is a new web-based interface to the CSD, offering fast and simple access to crystal
structure data using only a standard web-browser. This talk will describe this on-line tool andhow, through a Discovery Corps Senior Fellowship (DCF) from the National Science
Foundation, the use of crystal structure data has been integrated into the undergraduate
chemistry curriculum in more than 30 institutions in the US.
Acknowledgements: This work is supported is by the Cambridge Crystallographic Data
Centre and the United States National Science Foundation under Grant No. 0725294.

P-157

Enhancing Stability of Enzymes through Modulationof Inter-domain Interactions: A Case Study
Debi Choudhury, Sumana Roy, Sampa Biswas and J. K. Dattagupta
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics,
1/AF Bidhannagar, Kolkata-700064, India, (sampa.biswas@saha.ac.in)Inter-domain interactions are known to play a major role in the stabilization of multidomain
proteins. So engineering higher inter-domain interactions can be a justified approach toincrease the stability of a protein. However, inter-domain motion in a multidomain protein isrelated to protein function like enzyme catalysis and thus engineering inter-domaininteractions sometimes may lead to a loss of protein function. Aim of this study was torationally design mutant(s) with enhanced thermostability for multidomain enzymes retaining
their full activity. Papain is an archetype enzyme of the papain family which has twointeracting domains and the active-site cleft lies at the interface between these domains. We
therefore chose papain as a model protein for enhancing stability which may also be of benefit
for industry. From the three dimensional X-ray structures of three thermostable proteases ofthe papain family, Ervatamins A, B and C, we could identify three residues which were thought
to be responsible for higher inter-domain interactions in these enzymes and we carried out
replacement of these three amino acids at the corresponding positions of papain through SDM.
In the process, we were able to generate a double and a triple mutant of papain which were
found to be experimentally more thermostable than the wild type. The optimum temperatureof activity of these mutants increased by 10-12 ºC and their half-life of activity at 65 ºC was
20-30 min longer than the wild type. The kinetic experiments on these two mutants also
confirmed that catalytic efficiency has not significantly changed. In-silico molecularsimulation studies and normal mode analysis on the mutants were carried out to establish themolecular and structural basis for the changed properties. Such an approach for enhancing
stability can be extended for other multidomain proteins.

- 222 -

AsCA’09

PosterWide-Angle incidence Waveguides Using X-Ray
Diffraction

P-158

S.-L. Chang1 , C.-J. Huang1, L.-S. Cai1, H.-Y. Chen1, C.-H. Chu1, M.-T. Tang2, Yu. P.
Stetsko2, B.-Y. Shew2
1.
Department of Physics, National Tsing Hua University, Hsinchu,Taiwan, 300.
(slchang@phys.nthu.edu.tw)2
National Synchrotron Radiation Research Center, Hsinchu, Taiwan, 300.

We report on the diffraction phenomena of X-rays in nano-scale waveguides in the wide-angle
incidence geometry. This type of waveguides is different from the conventional types where
grazing incidence or normal incidence of X-rays is adopted. In order to bend a wide-angle
incident beam along the crystal surface, the (113) reflection of silicon at the 8.8785keV isused. The waveguides are prepared on a [001] Si wafer of 6 inches in diameter and 675 um inthickness. The designed waveguides are along [110] direction. The sizes of the waveguides
are 5mm long and 700, 450, 400, and 350 nm wide, respectively. The sample wave guides areprepared by using microelectronic lithographic techniques to etch out the Si wafer by 1 um in
depth. The waveguides are then plated with gold for about 150 nm in thickness on the top, theleft and right surface and 300 nm for the bottom. Detailed analysis on the interference among theexisting eight modes of wave propagation in this waveguide will be discussed.

Study on Structural Biology

P-159

Ko-Hsin China, b & Shan-Ho Choua, b, *aInstitute of Biochemistry
National Chung-Hsing University, Taichung, 40227, TaiwanbNational Chung Hsing University Biotechnology Center
National Chung-Hsing University, Taichung, 40227, Taiwan

C-di-GMP controls the transition between pathogenicity and biofilm formation in eubacteria,
yet not much is known about how this nucleotide exerts its action in cells. In the plant
pathogen Xanthomonas campestris, the expression of a number of pathogenicity genes isregulated by the levels of c-di-GMP and also by the CAP-like protein XcCLP. In thismanuscript, we report the structural insights into the interaction between c-di-GMP and
XcCLP in gene regulation. We have determined the crystal structure of an active XcCLP
variant using X-ray crystallography, and have shown using EMSA and Biacore experimentsthat XcCLP binds target promoter DNA with sub-mmolar affinity in the absence of any ligand.
Detailed structural comparisons of XcCLP with constitutively active CRP variants from
Escherichia coli showed that changes of several crucial residues in XcCLP culminate in a
substantial structural transition leading to the formation of an active conformation suitable for
DNA binding. Competitive EMSA experiments of the XcCLP/DNA complex titrated withc-di-GMP indicated that c-di-GMP inhibits XcCLP from binding cognate DNA. Modelingstudies of XcCLP/c-di-GMP complex indicated that c-di-GMP interposes between the XcCLP
dimerization and DNA-binding domains, reorienting the DNA-contacting helix. These results
strongly suggest that XcCLP is a c-di-GMP responsive transcriptional regulator adopting an
intrinsically active DNA-bound conformation, yet its DNA-binding capability is abrogatedwhen bound with c-di-GMP. XcCLP is therefore the first transcription factor in the CRP/FNR
superfamily observed to regulate Xcc pathogenicity genes expression in a manner negatively- 223 -

AsCA’09

Postercontrolled by c-di-GMP.

The Structural analysis of the FAS1 domain 4 of β
ig-h3 for relationship with corneal dystrophy.

P-160

Jiho Yoo1, Jongsoo Jeon1, Kuglae Kim1, Eugkweon Kim3, Jongsun Kim2, Hyun-Soo
Cho1*.
1
Department of Biology, college of Life Science and Biotechnology, Yonsei Uviversity,
134 Shinchon-dong, Seodaemun-gu, Seoul 120-749, Republic of Korea.
(hscho8@yonsei.ac.kr)
2
Department of Microbiology and Brain Korea 21 Project of Medical Sciences3
Department of Biochemistry and Molecular Biology, Yonsei University college ofMedicine, Seoul, Republic of Korea

The βig-h3 is a kind of extracellular matrix proteins and involved in cell adhesions. It has
been reported that mutations on the βig-h3 gene cause amyloid deposits and induce a corneal
dystrophy disease in human eyes. In order to elucidate the molecular basis of the βig-h3 forinducing amyloid deposits and a corneal dystrophy, we determined the crystal structure of the
βig-h3 FAS1 domain 4. It shows a canonical FAS1 domain structure which consists of six
α-helices and six β-strands. Interestingly, R555 residue of which the mutations are the ones ofthe frequently founded in corneal dystrophy patients is exposed outward. On the other hand,most other mutations for a corneal dystrophy are found inside of the protein suggesting themutations would induce folding problems. Along with results of molecular dynamics
simulations and CD spectrums, the crystal structure of the βig-h3 FAS1 domain 4 suggeststhat R555 mutations cause a local structural change especially in the a5-a6 loop resulting in
disturbance of the protein-protein interactions and gives us the insight for the molecularmechanism for a corneal dystrophy.

Structural analysis of a prokaryotic Kir channel
captured in multiple conformations

P-161

Oliver B. Clarke1,2, Alessandro T. Caputo1,2, Brian J. Smith1, Jacqueline M. Gulbis1
1
Walter and Eliza Hall Institute of Medical Research, 1G Royal Pde, Parkville 3052,
Melbourne, Victoria, Australia (clarke@wehi.edu.au; jgulbis@wehi.edu.au)
2
Department of Medical Biology, University of Melbourne, Parkville 3052, Victoria,
Australia

Inward rectifiers (Kir; IRK) are a family of ligand-gated K+ channels with diverse roles in thephysiology of higher organisms. They stabilise the resting membrane potential, and are crucial
in the regulation of cardiac [1] and pancreatic [2] function. We are carrying out a systematic
study of gating in inward rectifier K+ (Kir) channels, utilising the prokaryotic channel
KirBac3.1 as a model system to obtain insights into the function and regulation of mammalian
Kirs. The recently reported crystal structure of a chimeric channel comprising the pore of theprokaryotic KirBac1.3 and the cytoplasmic regions of mouse Kir3.1 revealed seamlessintegration of mammalian and prokaryotic segments [3]. Their physical accord established thevalidity of using prokaryotic channels for investigating molecular aspects of the mammaliansystem.
We have recently solved several new crystal structures of a prokaryotic inwardly rectifying- 224 -

AsCA’09

Posterpotassium channel, KirBac3.1. In comparison with previously solved structures of both
KirBac3.1 and KirBac1.1, our structures reveal intriguing differences.
Most strikingly, the cytoplasmic assembly is rotated with regards to the transmembrane
domain, forming a novel interface between the cytoplasmic assembly and the amphipathic
slide helices of the transmembrane region. This interface is stabilized by a salt-bridge between
a highly conserved aspartate on the slide helix and an arginine contributed by the cytoplasmic
domain of an adjacent subunit.
Rearrangement of the cytoplasmic subunit interfaces is observed in some of the structures,
including reconfiguration of a functionally important salt bridge, disruption of which is
implicated in the genesis of Andersen’s syndrome.
The implications of these structures for current models of the gating process in Kir channels
will be discussed.
References
[1]
[2]
[3]

F. M. Gribble, S. J. Tucker, S. Seino, F. M. Ashcroft, Diabetes.
F. M. Ashcroft, S. J. Ashcroft, D. E. Harrison, The Journal of Physiology 400, 501
M. Nishida, M. Cadene, B. T. Chait, R. MacKinnon, EMBO J 26, 4005.

P-162

Crystallization and Preliminary X-ray analysis of PNP
4-mono-oxygenase from Pseudomonas putida
DLL-E4
Zhongli Cui, Weidong Liu , Wenjing Shen
College of Life Sciencess,Nanjing Agricultural University, 6 Tongwei Road, Nanjing,
210095 P.R.China (czl@njau.edu.cn)

p-nitrophenol (PNP, also known as 4-nitrophnol or 4-NP), is the mostcommon and important in terms of quantities manufactured and extent
of environmental contamination. It is used for synthesis of medicines,
dyes, explosives, leather colouring, wood preservatives, and rubber
chemicals (Uberio, 1997).The strain Pseudomonas putida DLL-E4(Liu Zhi 2003) degrading methyl parathion (MP) was isolated fromsoil polluted by MP for long term, and it can use PNP as sole carbon
and nitrogen sources. We successfully cloned pnpA gene(genbank
accession number: FJ376608) from a DNA fragment which exhibits
PNP 4-monooxygenase activity from Pseudomonas putida DLL-E4, we expressed pnpA in
Escherichia coli with a C-terminal 6-his tag and purified it to homology by Ni-NTA column.
Crystallization conditions were performed by Hampton Research Crystallization
Kits(Hampton Research). Diffraction-quality oblique parallelepiped shape crystals wereobtained with hanging drop vapor diffusion method performed at 293 K by mixing 3µl 10
mg/ml protein with 3μl reservoir solution and equilibrated against 500 µl mother liquor, themother liquor contains 20 mM HEPES (pH 7.0), 15% PEG 4000, and 15% isopropane. The
crystals reached dimensions of up to 0.025 x 0.1 x 0.1mm(figure in topright) after 2 days.
- 225 -

AsCA’09

Poster

Diffraction data were collected from a single crystal at the beam line BL17U of Shanghai
Synchrotron Radiation Facility (Shanghai, P.R. China) using a MAR 225 CCD area detector(MAR Research). The diffraction data for the crystal were integrated and scaled using
HKL-2000 (Otwinowski & Minor, 1997)The collected data has 97.9% completeness and withan overall R-merge of 7.8 % on intensity, and the space group of the crystal belongs to theorthorhombic P212121 with unit-cell parameters a = 54.47, b = 77.56, c = 209.17. Based on
the subunit Molecular Weight is 47.3 kDa (including six histidine residues), there were twomolecules in the asymmetric unit and the Matthews coefficient VM was 2.33 Å3 Da-1,
corresponding to a solvent content of 47.35% (Matthews, 1968), the estimated mosaicity ofthe data is 0.117°. Further attempts to solve the structure by multiwavelength anomalous
diffraction (MAD) method (Hendrickson et al., 1990) using selenomethionine-substituted
protein are currently under way.
References
1.
2.
3.
4.
5.

Uberio, V. & Bhattacharya, S. K. (1997). Water Environment Research, 69, 146-156.
Liu, Z., Hong, Q. & Zhang X. Z. (2003). China Environmental Science, 23, 435-439.
Otwinowski, Z. & Minor, W. (1997). Methods Enzymol. 276, 307-326.
Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497
Hendrickson, W. A., Horton, J. R. & LeMaster, D. M. (1990). EMBO J. 9, 1665-1672.

How to interpret the quarterly charged[Ni(dmit)2]-1/4? ⎯ Structure and electricalP-163

conductivity of (n-Bu4N)[Ni(dmit)2]4MeCN

Qi Fang 1,*, Wen-Tao Yu 1, Chun-Li Guo 1, Wei Xu 2
1State Key Laboratory of Crystal Materials, Shandong University, Jinan 250100, China,(fangqi@sdu.edu.cn)
2
Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, China

Z[M(dmit)2]x (Z is mono-cation) type conductive and super-conductive complexes havereceived great attentions. Here we report the structure and conductivity of the new(n-Bu4N)[Ni(dmit)2]4 MeCN.
We grew the crystal in situ of the reaction: 4[Ni(dmit)2]- + 3Ag+ → 3Ag + 4[Ni(dmit)2]-1/4.
The X-ray diffraction data were collected on a Bruker P4 diffractometer by Mo Kα radiation
at 293 K. Crystal data: P-1 space group; a, b, c = 12.029(1), 14.795(2), 23.076(3) Å; α, β, γ =102.85(1), 103.82(1), 96.31(1)˚; V = 3829.8(7) Å3; and R1, wR2 = 0.0476, 0.0881 (I >2σ (I)); S= 1.002; Δρmax, Δρmin = 0.358, -0.295 e/Å3.
As shown in Fig. 1, the Lnσ of the single crystal (σ is conductivity) has a linear dependence
on T-1, indicating a semi-conductive behavior with a low activation energy being Ea = 0.12 eV.
The planar coordination anions are parallel arranged in tetras (see Fig. 2). Within a tetrad{4[Ni(dmit)2]-1/4}, the interplanar distance is 3.56 Å and the Ni…Ni distances are 4.05, 4.06,
and 4.08 Å. Between tetrads, the interplanar distance (3.63 Å) and Ni…Ni distance (4.91 Å)
are larger.
As shown in Fig.3, the IR spectra of (n-Bu4N)[Ni(dmit)2]4MeCN shows two C=C peaks at1349 and 1265 cm-1 with the intensity ratio of 1:3. Meanwhile, the IR C=C peaks of- 226 -

AsCA’09

Poster(n-Bu4N)[Ni(dmit)2] and [Ni(dmit)2] are located at 1349 and 1266 cm-1, respectively. This
indicates that the tetrad {4[Ni(dmit)2]-1/4} may consist of one mono-anion [Ni(dmit)2]- andthree neutral [Ni(dmit)2].
-2(n-Bu4N)[Ni(dmit)2]4 MeCN

-1

Ln[σ (Ω cm )]

-4

−1

-6
-8

c: [Ni(dmit)2]

1266

-10
-1

-1

T (K )

-12
0.004

0.006

0.008

0.010

b: (Bu4N)[Ni(dmit)2]

Fig. 1 Lnσ ~T -1 curve (σ is conductivity)
Transmittance (%)

100

1349

1349

a: (Bu4N)[Ni(dmit)2]4

1265

0
1400

1200

1000

800

600

400

-1

Wavenumber (cm )Fig. 2 Crystal structure of (n-Bu4N)[Ni(dmit)2]4MeCN

P-164

Fig. 3 IR spectra of several complexes

The structure of the ribosome with elongation factor
G trapped in the post-translocational state
Yong-Gui Gao, Maria Selmer1, Christine M. Dunham1, Albert Weixlbaumer1, Ann
C. Kelley and V. Ramakrishnan
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United
Kingdom (yggao@mrc-lmb.cam.ac.uk)

Elongation factor G (EF-G) is a GTPase that plays a crucial role in the translocation of tRNAs
and mRNA during translation by the ribosome. We report a crystal structure refined to 3.6 Å
resolution of the ribosome trapped with EF-G in the post-translocational state using theantibiotic fusidic acid. Fusidic acid traps EF-G in a conformation intermediate between the
GTP and GDP forms. The interaction of EF-G with ribosomal elements implicated instimulating catalysis, such as the L7/L12 stalk and the L11 region, and of domain IV of EF-G
with P-site tRNA and mRNA shed light on various aspects of EF-G function in catalysis andtranslocation. The stabilization of the mobile stalks of the ribosome also results in a more
complete description of its structure. As the first ribosome GTPase structure, the present
research also paves way for study on other GTPase bound to ribosome.
Keywords: Elongation factor G, EF-G, ribosome, translation, translocation, fusidic acid

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AsCA’09

PosterGrowth and Characterization of α and γ-glycine single
crystals

P-165

T.P.Srinivasan1,2, S.Anandhi1 and R.Gopalakrishnan1
1Department of Physics, Anna University Chennai, Chennai – 600 025, Tamil Nadu,
India.(krgkrishnan@yahoo.com and krgkrishnan@annuniv. edu)
2
Deparment of Physcis, K.L.N. College of Engineering, Madurai , Tamil Nadu,
India.(tps176@yahoo.com)

Complexes of amino acids with inorganic salts have been of interest as materials for opticalsecond harmonic generation (SHG), and all amino acids except glycine contain chiral carbon
atoms and perhaps crystallize in the non-centrosymmetric space group [1]. Dipolar molecules
possessing an electron donor group and an electron acceptor group contribute to large second
order optical nonlinearity arising from the intramolecular charge transfer between the twogroups opposite nature. Due to this dipolar nature, amino acids have been considered as
potential candidates for NLO applications [1]. Although the salts of amino acids like
L-Arginine [2], L-Histidine [3] and L-Proline [4] are reported to have NLO properties; thecomplexes of glycine with inorganic salts are not explored for optical SHG so far, sinceglycine, the simplest amino acid, does not possess the asymmetric carbon, it is NLO inactive.
Out of the number of semi organic single crystals of glycine that have been already reported,
most of them are not NLO active [5-7]. Glycine has three polymorphic crystalline forms α, β,γ [8,9]. Both α and β forms crystallize in centrosymmetric space groups ruling out thepossibility of optical second harmonic generation. But γ-glycine crystallizes in
non-centrosymmetric space groups P31 making it a possible candidate for NLO applications
and it is difficult to grow the γ-glycine crystals [10,11]. The thermodynamic stabilities of thethree polymorphs of glycine at room temperature are in the order γ > α > β [12]. It has
recently been reported that complexes of the γ- glycine can be efficient in optical SHG withinorganic salt sodium nitrate [1]. Ferroelectrocity was discovered for glycine silver nitrate[13]. It was also reported that glycine combines with CaNO3 [14] and LiNO3 [15] to form
single crystals but none of these are reported to have nonlinear optical property. To the best of
the knowledge of the authors there is no report available on the growth and characterization ofpure and γ- glycine.
The nonlinear optical single crystals of α-glycine and γ-glycine were grown by the slow
evaporation solution growth method from aqueous solution as shown in figure 1(a) and 1 (b).
The title compound was synthesized and purified by repeated recrystallization process. Fromthe single crystal XRD analysis it is confirmed that the grown α-glycine crystallizes inmonoclinic system with space group P21/n and γ-glycine crystallizes in hexagonal with spacegroup P31[16]. The determined lattice parameter values of α-glycine and γ-glycine crystals
are in-line with the literature. In the FT-IR spectrum, the peak observed at 3167.51cm-1 of
α-glycine and 3171.36cm-1 of γ-glycine is assigned to NH3 asymmetric stretching mode whichis related to the hydrogen bond strength. The bands at 1329cm-1 in the IR spectra are morereasonably assignable to NO3- ion in γ-glycine [17]. The range and percentage of opticaltransmission were ascertained by recording UV–Vis–NIR spectrum. It is observed that thelower cut-off wavelength of α-glycine and γ-glycine are 233nm and 257nm respectively. In
γ-glycine, 100% transparency is observed in the wavelength region between 330nm and
800nm. It is to be noted that the optical transparency below 330nm in the UV region is the- 228 -

AsCA’09

Postermost desirable characteristics for any nonlinear optical application such as second harmonic
generation. Its second harmonic generation relative efficiency was measured by Kurtz andPerry powder technique using Nd:YAG laser and was observed to be 135mV for γ-glycine andto 95mV for potassium dihydrogen orthophosphate. Group theoretical analysis of thefundamental modes of α-glycine crystal predicts that there are 120 vibrational optical modes
and are seen to decompose into Γ117 = (30Ag+29Au+30Bg+28Bu) apart from three acoustic
modes 1Au+2Bu. γ -glycine crystal predicts that there are 90 vibrational optical modes and areseen to decompose into Γ90 = (44A + 43E ) apart from three acoustic modes 1A+2E. The
factor group analysis for α-glycine and γ-glycine crystals was performed by following theprocedures outlined by Rousseau et al.[18]. Dielectric and thermal characteristics of low
temperature solution grown single crystals of α-glycine and γ-glycine have been carried out.
The dielectric constant and dielectric loss have been measured as a function of frequency inthe range 50Hz – 5MHz and temperature range between 311K, 323K and 373K. It is foundthat dielectric constant decreases with increasing frequency for both α and γ -glycine
crystals. Dielectric constant and dielectric loss are low for the γ -glycine compared to α
glycine[19].

Figure 1(a).As grown γ- glycine

Figure 1(b).

As grown α-glycine

References[1] M.N. Bhat, S.M. Dharmaprakash, J. Cryst. Growth 235 (2002) 511.
[2] D. Eimert, S. Velsko, L. Davis, F. Wang, G. Loiaceono, G. Kennedy, IEEE J. Quantum Electron 25 (1989) 179.
[3] M.D. Aggarwal, J. Choi, W.S. Wang, K. Bhat, R.B. Lal, A.D. Shield, B.G. Penn, D.O. Frazier, J. Cryst. Growth 204 (1999)
179.
[4] R.D.A. Hudson, A.R. Manning, J.F. Gallagher, M.H. Garcia, Tetrahedron Lett. 43 (2002) 8375.
[5] B. Brezina, Mat. Res. Bull. 6 (1971) 401.
[6] J.K.M. Rao, M.A. Vishwamitra, Acta Cryst. B 28 (1972) 1484.
[7] S. Natarajan, J.K.M. Rao, Z. Kristallogr. 152 (1984) 179.
[8] G. Albrecht, R.B. Corey, J. Am. Chem. Soc. 61 (1939) 1087.
[9] E. Fischer, Ber. Dtsch. Chem. Ges. 38 (1905) 2917.
[10] Y. Iitaka, Acta Crystallogr. 11 (1958) 225.
[11] Y. Iitaka, Acta Crystallogr. 14 (1961) 1.
[12] I. Weissbuch, V. Yu. Torbeev, L. Leiserowitz, M. Lahav, Angew. Chem. Int. Ed. 44 (2005) 3226.
[13] R. Pepinsky, Y. Okaya, D.P. Eastman, T. Mitsui, Phys. Rev. 107 (1957)1538.
[14] S. Natarajan, K. Ravikumar, S.S. Rajan, Z. Kristallogr. 168 (1984) 75.
[15] J.Baran, M.Drozd, A. Pietraszko, M. Trzebiatowska, H. Ratajczak, J. Polish. Chem. 77 (2003) 1561.
[16].Yochi Iitaka, Acta Cryst. (1961),14,1.
[17] J.Baran, A.J.Barnes, H.Ratajczak,Spectrochim. Acta Part A: Mol. Biomol. Spectrosc.51A(1995) 197.
[18] D.L. Rousseau, R.P. Bauman, S.P.S. Porto, Journal. Raman Spectrosc. 24 (1993) 91.
[19] C.P.Smyth, Dielectric Behaviour and Structure, McGraw Hill, New York 1995.

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P-166

PosterUnusual arrangement of EF hand motifs in Calcium
binding protein-1 of Entameoba histolytica and its
functional implications
Shivesh Kumar, Ruchi Jain and S. Gourinath
School of Life Sciences, Jawaharlal Nehru University, New Delhi – 110067

Calcium plays a pivotal role in the pathogenesis of amoebiasis, a major disease caused byEntamoeba histolytica. A repository of EF-hand containing calcium-binding proteins (CaBPs)
from E. histolytica share a high sequence similarity, they bind to different target proteins in aCa2+ dependent manner, leading to regulation of different functional pathways. The crystal
structure of the Entamoeba histolytica Calcium Binding Protein-1 (EhCaBP1) has been
determined at 2.4 Å resolution. Only two out of the four expected EF-hand motifs could bemodelled into the electron density map. Unlike CaM, the first two EF-hand motifs in
EhCaBP1 are connected by a long helix and form a dumbbell shaped structure. Owing todomain swapping oligomerization, three EhCaBP1 molecules interact in a head-to-tail manner
to form a triangular trimer. Three glycine residues in the central linker region connect the twodomains of the protein that imparts flexibility and is the major cause of the disorder of the
C-terminal of the protein. The oligomeric state of EhCaBP1 imparts reduced flexibility
between domains and may be responsible for the limited target reorganisation. To understandthe mode of target binding, co-crystallisation of EhCaBP1 with Phenylalanine shows that Phebinds to the hydrophobic pocket of the assembled-domain. The Phe bound assembled domainshows only 1.23Å RMS deviation with the N-terminal domain of CaM, bound to hydrophobic
IQ-motif of cardiac Ca2+ channel. The hydrophobic residue Phe of the peptide (bound to CaM
N-terminal domain) and Phe bound to EhCaBP1 assembled-domain are located at the similar
regions. Functional studies clearly show the involvement of N-terminal domain as thefunctional domain of EhCaBP1 in activating kinase and localization in phagocytic cup. To
validate the full-length structure, the initiatives have been taken to determine the structures of
the individual domains. The crystal structure of N-terminal domain has been determined at 2.5
Å resolution. The structure is similar to the N-terminal domain of the full-length protein withthe extended conformation of the EF-hand motifs connected with a long central helix. Thesestudies clearly demonstrate that the N-terminal domain in trimeric form has most of thefunctions in comparison to the full length EhCaBP1 and N-terminal domain also has calcium
dependent target binding activity.

Crystal structure of human Bfl-1 in complex with BAK
BH3 peptide

P-167

Rongjin Guan1, Rong Xiao1, Li Zhao1, Eileen White2, Celine Gelinas2, Guy
Montelione1
1
Center for Advanced Biotechnology and Medicine (CABM), Rutgers, The State
University of New Jersey
2
Robert Wood Johnson Medical School, UMDNJ, 679 Hoes Lane West, Piscataway NJ
08854

The Bcl-2 family proteins are crucial regulators of apoptotic pathways and are therefore
considered important therapeutic targets in anticancer therapies. Bfl-1, or A1, is a pro-survival- 230 -

AsCA’09

Postermember of the Bcl-2 family. Bfl-1 is a transcriptional target of nuclear factor-kB (NF-kB) thatis overexpressed in many human tumors and is a means by which NF-kB inhibits apoptosis.
Recently we have expressed and purified human Bfl-1 with its C-terminal 24 amino acids
removed, after tremendous efforts on expressing the full-length protein without any success.
We mixed the Bfl-1 protein with a 16 aa BH3 peptide of human BAK and further purified thecomplex, which was then crystallized. The X-ray diffraction data were collected on beamline
X4C at Brookhaven. The complex structure was determined by molecular replacement andrefined to 2.2 Å resolution. Bfl-1 adopts the canonical bcl-2 family fold which comprises 8
α-helices. The BAK peptide was half buried in a primarily hydrophobic groove in Bfl-1,
which is formed by helices α5 and α8 (bottom of the groove) and those from α2, α3, α4 andthe α4-α5 loop (sides of the groove). The BAK peptide forms seven hydrogen bonds andnumerous vdW contacts with Bfl-1 residues from helices 4, 5, 8 and 4-5 loop. We
compared these interactions with those found in Bfl-1: Bim complex structure reported
recently. Analysis the features of the drug targeting groove in Bfl-1 and Mcl-1 also explained
why ABT-737 (a potential anti-cancer drug mimic BH3 domains of BH3-only proteins) canbind to Bcl-xL but can not engage Bfl-1 and Mcl-1. This provides important structural
information for designing new anti-cancer drugs targeting Bfl-1.

P-168

Secondary Extinction and Diffraction Behaviors in
Single Crystals
Hua-Chen Hu
China Institute of Atomic Energy, Beijing102413, China, (hchu3310@gmail.com)

The X-ray and neutron diffraction processes in mosaic crystals with different shapes such asplane, cylinder and sphere are systematically investigated and solved within the framework of
Darwin’s transfer equations.
Plane and Deformed Crystals Universal expressions for the secondary extinction factor in
X-ray and neutron crystallography are developed for the first time[1-2], based on a generalsolution of the power transfer equations from plane crystals. The vital key to the successful
explanation of the solution of Darwin’s equations, with a clear physical interpretation, is theintroduction of a parameter ξ, the ratio of absorption cross section μ to diffraction crosssection σ. As a result of these new development, the author was invited to rewrite chapter 6.4，
Vol.C of the International Tables of Crystallography (ITCr)(2004) since the existing formulaeof the integrated reflecting power ratio (IRPR) for asymmetrical Bragg and Laue geometry
given in the ITCr (2001) are only the limiting cases of the present generalized formulae for ξ0→ ∞. The maximum reduced depth of radiation penetration as well as the optimal reduced
thickness for both Bragg and Laue geometry are given in the paper[1]. They are importantparameters for monochromator design. An unique method ”layer coupling model” [3] wasdeveloped for the calculation of IRPR from bent or gradient mosaic crystal. It is now acceptedinternationally as ”the discrete form of Darwin’s equations”.
Cylindrical and Spherical crystals During the past four decades, the essence of thediffraction geometry for a cylindrical crystal, which is the key for determining the IRPR of
spherical crystals (the most common shape of sample used in experiment), remains obscure.
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AsCA’09

Poster

As a result, the previously published theory was valid only within a small region (μR< 2.5).
By analyzing the power ratio distribution, an exact and unique description of the diffraction
geometry for a cylindrical crystal was obtained for the first time[4-5]. When μR>4, thediffraction geometry is essentially that of the Bragg-Bragg case, almost restricted to the fg
region, but with a continuously varying asymmetry parameter (Fig.1). This explanation ofdiffraction geometry is universal, and it should be of importance to the further investigation of
all kinds of cylindrical crystals in the future, even for ideal crystal, etc. The construction of aseries of extensive extinction factor tables corresponding to a wide range of θ, σR and μR
values (0.05≤ Sin θ ≤ 0.9, 0 <σR ≤ 30, 0≤ μR ≤ 30) and its 4D fitting formulae for cylindricaland spherical crystals with several kinds of mosaic distributions are underway.

Figure 1 Diffraction Geometry and reflection
profile for a cylindrical crystal with
ξ = 0.5，σR = 0.5，μR=1.25.

References[1] Hu, H. C. Acta Cryst. A53, 484-492, (1997).
[2] Hu, H. C. Acta Cryst. A53, 493-504, (1997).
[3] Hu, H. C. J. Appl. Cryst. 25, 731-736. (1992).
[4] Hu, H. C. Acta Cryst. A59, 493-297-310, (2003).
[5] Hu, H. C.，Yang, Z. Acta Cryst. A60, 562-564, (2004).

P-169

The Development of A “Unified” Microfluidic
Technology for Protein Crystallization
Jiang Huang
GN Biosystems, Inc., 25495 Whitesell St., Hayward, California 94545, U.S.A.
(jiang.huang@gnbiosystems.com)

Dialysis protein crystallization is a well-established and effective method for protein
crystallization. However, it is labor-intensive, time-consuming, cost-prohibitive (due to large
protein consumption) and difficult to automate. The disposable XZ™ dialysis crystallography
plate has been developed to specifically address these issues. With the XZ™ microfluidic
dialysis technology, 96 dialysis protein crystallization trials as low as 15nL/reaction can be
setup in 4 minutes. Other advantages of the XZ™ plates are: high-throughput setup andimaging compatibility, clear path to structure due to directly scalable and easy crystal retrieval
designs and it’s compatibility with in-situ x-ray diffraction data collection, and simple
sample/reagent loading protocols. Furthermore, with minor changes in protocol or design,vapor diffusion, microbatch and interface diffusion crystallization methods can all be carriedout using the XZ™ plates. Large volume (4μl/dialysis chamber, 96 well plate) XZ™ plate- 232 -

AsCA’09

Posterdesign is also developed to facilitate high throughput 2-D membrane protein crystallization.

P-170

ProSeed: A General Method to Introduce Beneficial
Nuclei to Promote Protein Crystallization
Jeff E. Habel1, Liwei Hung1,2
1
Lawrence Berkeley National Lab , Berkeley, CA 94720, USA (jhabel@lbl.gov)
2
Los Alamos National Lab, Los Alamos, NM 87545, USA (lwhung@lanl.gov)

After over a decade of high-throughput technology development, crystallization remains oneof the most crucial bottlenecks in protein structure determination. Figures taken from recent
Protein Data Bank indicate that the success rate from purified proteins to diffraction quality
crystals is only 18%. Most of the disappointment can be attributed to failure in obtaining
initial crystallization leads. Various techniques have been reported to help solve this criticalproblem. Nevertheless, these practices tend to be protein specific and are often case dependent.
Development remains a hit-and-miss process.
Two factors are essential to effective crystallization events: phase transition, and nucleation.
Although the former can often be extrapolated from initial screening experiments, the latter
continues to be a semi-random process. While careful observations of screening experiments
may help identify potential crystalline targets for seeding experiments, it remains less thanpractical when throughput and automation become factors of consideration. To solve these
problems we developed a universal method to introduce beneficial nuclei into crystallization
process helping to eliminate the nucleation factor. In our test case, after nuclei wereintroduced into a set of 282 ‘failed’ conditions, 82 new conditions yielded crystals. While aset of control experiments demonstrated other factors contributed to crystal formation(dilution, precipitant synergy, etc.), the results suggest that a significant number of failures incrystallization were due to lack of nucleation. Our method is general and semi-automatedwith a script designed for the Art Robbins PHOENIX robot. This method may not only
improve success rates for high-throughput crystallization projects, but also for those whose
successes are critical. Current ongoing research salvaging our structural genomics targets will
also be presented.

P-171

Automated Ligand Identification in PHENIX
Liwei Hung, Thomas C. Terwilliger
Los Alamos National Lab, Los Alamos, NM 87545, USA (lwhung@lanl.gov)

Over 60% macromolecular structures in the Protein Data Bank (PDB) contain bound small
molecule ligands. In the case where there is no knowledge about the bound ligand, to interpretthe unknown electron density is a rather difficult task in crystallographic model building.
We have implemented an automated ligand identification strategy in the framework of the
PHENIX software suite using the RESOLVE ligand identification algorithm. The
Resolve_ligand_identification task carries out fitting of a library of ligands to a given electron
density map. Subsequently it conducts statistical analysis and ranking of the ligand fitting- 233 -

AsCA’09

Posterresults. The Resolve_ligand_identification task works with the ligand library provided with
PHENIX suite by default. This library contains the 200 most frequently observed ligands in
the PDB. The program is also capable of fitting and ranking ligands in a custom ligand libraryprovided by the users. The current version takes advantage of multi-threading computing
environment, and provides a mechanism for users to incorporate biological knowledge in theprocess of identifying potential ligands in their protein structures.

P-172

Crystal Structure of the TNF-α Inducing Protein (Tipα)from Helicobacter pylori: Insights into its DNA
Binding Activity
Jun Young Jang1, Hye-Jin Yoon1, Ji Young Yoon1, Hyoun Sook Kim1, Sang Jae
Lee1, Kyoung Hoon Kim1, Do Jin Kim1, and Se Won Suh1,2
1
Department of Chemistry, Seoul National University, 151-747, Seoul, Korea(sewonsuh@snu.ac.kr)
2
Department of Biophysics and Chemical Biology, Seoul National University, 151-747,
Seoul, Korea (sewonsuh@snu.ac.kr)

Helicobacter pylori infection is one of the highest risk factors for gastroduodenal diseases
including gastric cancer. TNF-α is one of the essential cytokines for tumor promotion andthus a H. pylori protein which induces TNF-α is believed to play a significant role in gastriccancer development in humans. The HP0596 gene product of H. pylori strain 26695 was
identified as the TNF-α inducing protein (Tipα). Tipα is secreted from H. pylori as dimers andenters the gastric cells. It was shown to have a DNA binding activity. Here we havedetermined the crystal structure of Tipα from H. pylori. Its monomer consists of two
structural domains (“mixed domain” and “helical domain”). Tipα exists as a dimer in the
crystal and the dimeric structure represents a novel scaffold for DNA binding. The surface
electrostatic potential of Tipα dimer and the docking calculations suggest that a positively
charged surface patch that is formed across the two monomers by the loop between helices α1
and α2 may be important in DNA binding.

Determination of structural and magnetic phase
diagram of solid solution of BiFeO3-BaTiO3 system

P-173

Ryoji Kiyanagi1, Tadashi Yamazaki1, Yuma Sakamoto1, Hiroyuki Kimura1, Yukio
Noda1, Kenji Ohoyama2
1
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University,
Sendai 980-8577, Japan (kiyanagi@tagen.tohoku.ac.jp)
2
Institute of Material Research, Tohoku University, Sendai 980-8577, Japan

BiFeO3 (BFO) is known as a perovskite-type multiferroic material with ferroelectricity (TC ~1000 K) and antiferromagnetism (TN ~ 650 K). Solid solutions of BFO with other perovskite
materials have been intensively studied for the exploration of better multiferroicity. BaTiO3(BTO) is a well-known ferroelectric material (TC = 406 K) with the perovskite structure.
Dielectric measurements on BFO-BTO solid solutions ((1-x)BFO+xBTO) showedenhancement of spontaneous polarization. Furthermore, the material exhibits a weakferromagnetism. Structural studies so far reported are based on X-ray powder diffraction at- 234 -

AsCA’09

Posterroom temperature. The result suggested that the material changes its structure at x = 0.33 fromhexagonal to cubic. However, the spontaneous polarization, according to the dielectricmeasurement, persists in the concentration of x > 0.33. In order to elucidate the inconsistency
between the structure and the dielectric property and to draw a phase diagram of(1-x)BFO+xBTO system, structural investigation was conducted by means of neutron and
X-ray powder diffraction.
The diffraction patterns, especially the neutron powder diffraction patterns, clearly showed
the existence of the hexagonal phase in a wide range of x. The hexagonal phase coexists withthe cubic phase in 0.2 < x < 0.6 and with the tetragonal phase in 0.6 < x < 0.8. The
spontaneous polarization observed in the dielectric measurement probably arises from thecoexisting hexagonal phase.
Variation of TN with respect to x was examined by monitoring the intensity of a magneticreflection, and the structural phase transition temperature (TS) was estimated from thevariation of the intensity of a hexagonal-phase-specific reflection. Both temperatures were
found to decrease as x increases. The decrease of TN can be attributed to decrease of themagnetic moment of Fe3+, and the change in TS may be caused by a small distortion inducedby the surrounding cubic or tetragonal structure.
Acknowledgements: This work has been supported by a Grant-In-Aid for Scientific Research(A), No. 21244051, and Grant-In-Aid for Scientific Research on Priority areas ``Novel Statesof Matter Induced by Frustration'', No. 19052001, from the Ministry of Education, Culture,
Sports, Science and Technology.

Development of laboratory SAXS spectrometer

P-174

Seok-Gn Ryu1, Chang-Hee Lee2, Myungkook Moon2, Jongkyu Cheon2, Hyun Hoon
Song1,Woon Bo Shim1
1Department of Advanced Materials, Hannam University, Daejeon, Korea(songhh@hnu.kr )2HANARO Center, Korea Atomic Energy Research Institute, 150 Deokjin-dong,
Yuseong-gu, Daejeon 305-353, Korea (leech@kaeri.re.kr)

Small angle X-ray scattering is well known classical technique and recently it has renaissancein some sense in structural biology in addition to widely used nano-scale studies because
SAXS requires neither crystals nor special sample preparation, and is not limited bymolecular mass but applicable under nearly physiological conditions. Even SAXS permits
quantitative analysis of kinetic processes like assembly and disassembly, and allows one to
study structural transitions and conformational changes on which biological function often
relies.
Though SAXS beamlines at synchrotron are very powerful and produces high quality data,home-made SAXS machine using laboratory source could play a lot of roles from educationand training to advanced researches, too. Based on 2-dimensional position-sensitive gas
detector technology which has been developed at HANARO center, we have built home-madeSAXS machine using the unused port of an already running rotating anode source for X-ray
diffractometer and Osmic mirror. Most of the components are of off-the-shelf parts and- 235 -

AsCA’09

Posterdeveloped in-house and it, therefore, is very flexible under measuring conditions and isrelatively cheap to construct. We report here our experience of home SAXS machinedevelopment and early results with several improvement points, too.

Fig.1 home-made SAXS spectrometer

P-175

Fig.2 Background, silver behenate and chicken tendon patterns

Coordination Polymers of
N-(7-hydroxy-4-methyl-8-coumarinyl)-amino acids:
Fabrication of Crystalline, Gel and Fiber Materials
Wei Lee Leong, Jagadese J. Vittal
Department of Chemistry, National University of Singapore, Singapore 117543.
(chmjjv@nus.edu.sg)

Considerable efforts have been devoted to study the rational design, properties, function andapplications of crystalline materials while the discovery of gels has been largely serendipitousat the initial stage and, currently, evolve to design and understanding of the gelation process.
Development of coordination polymers from crystalline materials to soft materials such as
gels and fibers would provide a new insight in studies and applications of functional
materials.
Recently, we found that metal complexes of N-(7-hydroxy-4-methyl-8-coumarinyl)-aminoacids can be fabricated into crystalline, gel and fiber materials by interplay of metal ions,solvent and intermolecular interactions (Scheme 1). The Cu(II), Ni (II) and Zn (II) complexes
have been shown to display fascinating structures including heptanickel hexagonal cluster,heterobimetallic metallocrown, pentanickel cluster, helical and zigzag coordination polymers.
It may be noted that variation of metal ions has facilitated the assembly of such diverse
structural architectures. Interestingly, Zn(II) and Mg(II) coordination polymers canself-assemble into gel materials in the absence of long chain hydrophobic groups. The 1D
coordination polymeric strands aggregate and further self-assemble into a 3D network
structure through noncovalent interactions to entrap water molecules. The most striking
finding is that the dramatic enhancement of fluorescence properties of coumarin chromophore
upon the formation of coordination polymeric hydrogel. Furthermore, Mg(II) coordination
polymer can be obtained as random cross linking gel and well-aligned nanofiber by changing
the chirality of amino acid backbone and pH of the solution. Our studies provide more insight
into the self-assembly process of crystalline and amorphous materials that demandwidespread of practical applications.

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AsCA’09

Poster

References
1. W. L. Leong, A. Y.-Y. Tam, S. K. Batabyal, L. W. Koh, S. Kasapis, V. W.-W. Yam, J. J. Vittal, Chem.
Commun., 2008, 3628.
2. W. L. Leong, S. K. Batabyal, S. Kasapis, J. J. Vittal, Chem. Eur. J., 2008, 14, 8822.
3. W. L. Leong, S. K. Batabyal, S. Kasapis, J. J. Vittal, submitted.

P-176

RainbowMEM: A New Maximum Entropy Analysis
Package
Hui LI1, Jiaju LI2, Xiaolong CHEN3 and Ze ZHANG1
1 Beijing University of Technology, 100124, Beijing, China (huilicn@yahoo.com)
2 Institute of Geology and Geophysics, CAS, 100029, Beijing, China
3 Institute of Physics, CAS, 100080, Beijing, China

A new maximum entropy analysis package, RainbowMEM, was developed. This package iswritten with Visual Basic (VB) language, which has graphic interface (GUI) and runs underWindows operation system (OS). This package contains three modules: maximum entropy
charge density calculation module, molecule topology analysis module and 3D charge density
gradient display module. In this package, mixed radix fast Fourier transforms (MRFFT)
algorithm was adopted. Therefore, the calculation efficiency of RianbowMEM is quite high.
The maximum grid amount which RainbowMEM can deal with is 27,000,000. This amount is
big enough to deal with most inorganic and organic crystal materials.
1. Maximum Entropy Charge Density Module
Example: K2Al2B2O7

Fig.2 This figure shows the Al-O and B-O layer,
whose bond type is a covalence ion mixed bond.
The charge density grids range from 0.5e/Å3 to
2.5e/Å3 intervals 0.038e/Å3.

Fig.1 The comparison of the maximum entropy charge
density (the left part) and the ab initio calculation charge
density (the right part, CASTEP[1]) of K2Al2B2O7. This
figure shows the K atoms layer, whose bond type is an
ion bond basically. The charge density grids range from
0.5e/Å3 to 2.5e/Å3 intervals 0.038e/Å3.

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AsCA’09

PosterFig. 3. The 3D maximum entropy charge density of GaN. (a) Calculated by RainbowMEM program. (b) Calculated by
MEED[2] program. The isosurface value is 1.25e/Å3.

2. Molecule Topology Analysis Module
In this module, the critical point position, charge density value, Hessian matrix andeigenvalue can be supplied.

Fig.4 The interface and calculation result of molecule topology analysis module

3. 3D charge density gradient display module

Fig.5 The interface of 3D charge
density gradient display module

Fig. 6 Bond critical point (Arrow) of
Al-O bond in K2Al2B2O7

Fig. 7 Bond critical point (Arrow)of B-O bond in K2Al2B2O7

Conclusion
With the charge density information, the physical and chemical properties of the materials canbe analyzed more directly. Restoring the accurate charge density with experimental diffraction
data became a promising research field in the crystallography. In this work, the authors
developed a new X-ray charge density maximum entropy analysis program, RainbowMEM,
which can deal with either powder or single crystal X-ray diffraction data. This program also
supplied the molecule topology analysis and 3D charge density gradient display function
which is convincing to the charge density analysis.
Acknowledgements: This work is financial supported by the National Natural Science
Foundation of China (NSFC) Project 10704004.
References[1] M. D. Segall, P. J. D. Lindan, M. J. Probert, C. J. Pickard, P. J. Hasnip, S. J. Clark, and M. C.
Payne, J. Phys.:Cond. Matt., 14(11), 2717-2743, (2002)- 238 -

AsCA’09

Poster[2] M. Sakata and M. Sato, Acta Cryst., A46, 263-270, (1990)

P-177

Crystallization Force: A Density Functional Theory
Concept for Characterizing Molecular Packing in
Organic Crystals
Tonglei Li
Department of Pharmaceutical Sciences, University of Kentucky, 725 Rose Street,
Lexington, KY 40536, U.S. (tonglei@uky.edu)

Because of the rich diversity in functional groups and the flexibility in molecularconfiguration and conformation, organic compounds are inclined to polymorphic formation insolid state, which can be greatly affected by the selection of solvent and other crystallization
conditions. Intermolecular interactions are typically of weak forces such as van der Waals andstronger short-range ones including hydrogen bonding that determine the spatial packing oforganic molecules during the crystallization process. In order to uncover the underlying
mechanism that drives a molecule to have various packing motifs in solid state, an electronic
concept or function within the framework of conceptual density functional theory (DFT) is
developed, namely, crystallization force. The concept aims to describe the local change inelectronic structure as a result of the self-assembly process of crystallization in order toquantify the locality of intermolecular interactions that directs the molecular packing in
crystal.
Crystallization force stems from how the electronic structure of a molecular system responds
to a perturbation to the number of electrons in the system. Conceived within the framework of
DFT, it is developed in our laboratory as the following:
dqα
f α+
dq
G α = Φ α− −αfαwhen dqα > 0

G α = Φ α+when dqα < 0where Φ+α and Φ–α are the nucleophilic and electrophilic nuclear Fukui functions of atom α
and f+(r) and f–(r) are the nucleophilic and electrophilic electronic Fukui functions at positionr, respectively. The change in atomic charge (or, equivalently, the negative of the change inatomic population) of atom α because of the molecular packing of crystallization is dqα. As
such, the crystallization force, Gα, can be regarded as the inherent nuclear Fukui function
associated with crystallization. Due to its physical nature as Hellmann-Feynman force, a Gα
may thereby quantify the local binding force in a crystal.

- 239 -

AsCA’09

PosterFigure 1. Isosurfaces of electron density (in gray) and electronic
Fukui functions of isonicotinic acid with nucleophilic in red (a) andelectrophilic in blue (b); nuclear Fukui functions are illustrated asarrows. For simplicity, not all electronic structures are drawn.
Hydrogen bonds are shown in pink dash lines (c). Crystallization
forces are represented as arrows (d).

Figure 1 shows one example of crystallization forces calculated of isonicotinic acid. The
calculations were done with Crystal 06 by using the basis set of B3LYP/6-21G**. The
molecules form hydrogen bonds in the crystal between the –OH and N. Large nucleophilic
Fukui functions are located mainly at the –COOH while large electrophilic at the ring.
Because some atoms gain electrons and others lose when the molecule “moves” from the gas
or liquid phase to the crystalline phase, the crystallization force provides a unified expression
to embody these Fukui functions. The crystallization forces nicely depict the hydrogenbonds in both directionality and magnitude (Figure 1d).

P-178

Crystal structure of a lead(II) complex with furan-2ylmethylene salicyloyl hydrazine
Ying-Ying Zhang, Shi-Xiong Liu*
Department of Chemistry, Fuzhou University, Fuzhou 350002, P.R. China(shixiongliu@yahoo.com)

A lead(II) complex with furan-2-ylmethylene salicyloyl hydrazine, [Pb(C12H9N2O3)2]n (1),has been synthesized and structurally characterized. Complex 1 crystallizes in tetragonal,
space group P 41212, with a = 9.477(3) and c = 26.352(6) Å, V = 2367(1) Å3, Z = 4, Dc =1.868 g/cm3, F(000) = 1280, μ = 7.176 mm-1, S = 1.084, the final R = 0.0344 and wR = 0.0524
for 2286 observed reflections with I > 2σ(I).
The lead complex possesses C2 point symmetry and is located on a twofold crystallographic
axis 2[110]. The Pb atom is coordinated by six oxygen donors and two nitrogen ones fromfour hydrazine ligands L1, in which there are two kinds of Pb-O bond distances. The bondlengths of Pb1-O2 (carbonyl), Pb1-O2A, Pb1-N2 (hydrazine), and Pb1-N2A (carbonyl) are
2.310(4), 2.310(4), 2.544(4) and 2.544(4) Å, respectively, which are in the normal Pb-O and
Pb-N bond distance range. At the same time, interatomic distances of Pb1-O3 (furfural),
Pb1-O3A, Pb1-O1B(phenol) and Pb1-O1C are 2.976(5), 2.976(5), 2.909(4) and 2.909(4) Å,
respectively. Therefore, lead atom in the title complex is in a holodirected eight-coordinatedpolyhedron.
Every lead complex molecule [Pb(C12H9N2O3)2] connects four adjacent complex mole cules
by four hydrazine ligands L1. Every hydrazine ligand L1 acts as a biconnectors to coordinate
to two lead atoms of two lead complex molecules. Therefore, complex 1 features a 3D
coordination network.
- 240 -

AsCA’09

Poster

Acknowledgements: This project was financially supported by the Natural Science
Foundation of China ((No. 20431010 and 20171012), the Natural Science Foundation of
Fujian Province, China (E0110010).

Structures, Luminescence of Lanthanide-Organic
Frameworks

P-179

Tian-Fu Liu1, Rong Cao*1, Wen-Hua Sun*2
1
State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the
Structure of Matter, Chinese Academy of Sciences, Fujian, Fuzhou, 350002, P. R. China.
(Liutiafu@fjirsm.ac.cn)
2
Key Laboratory of Engineering Plastics, Institute of Chemistry, Chinese Academy of
Sciences,Beijing, 100080, People’s Republic of China. (whsun@iccas.ac.cn)

A series of coordination polymers [Ln2(Hcbmp)(ox)3(H2O)2] (Ln = Sm (1), Eu (2), Gd (3)H2cbmp = 2-(carboxylic acid)-6-(2-benzimidazolyl)pyridine, ox = oxalic acid ) has beenhydrothermally synthesized and structurally characterized. Single-crystal X-ray analysis
reveals that they are isostructural and crystallize in C2/c space group. Oxalate ligands and Lnions compose an infinite bi-layer structure. The water molecules ， both solvated andcoordinated，are arranged between the layer. The Hcbmp ligands distribute on both sides ofthe layer chelating with Ln metal ions. So the resulting configuration shows a perfect
sandwich structure in the b direction (Figure 1). Meanwhile, the luminescent properties were
investigated at room temperature. Complex 1 and 2 exhibit strong fluorescent emissions in thevisible and near-infrared region. As shown in Figure 2, transitions from the excited 4G5/2
state to different J levels of the lower 6H2/9 state were observed in the emission spectrum ofcomplex 1. The complex 2 gave typical Eu emission spectrum containing the expectedsequence of 5D0-7FJ (J=0,1,2,3,4.) (Figure 3). Thus, these complexes could be anticipated as
good candidates for efficient luminescent materials and fluorescent probes.

Figure 1- 241 -

AsCA’09

Poster4

6

G5/2- H9/2

5

7

D0- F2

Sm

Eu
4

6

relative intensity

relative intensity

G5/2- H7/2

6

4

G5/2- H5/2
4

6

G5/2- H11/2

5

5

7

5

7

5

D0- F0

450

500

550

600

650

700

750

800

500

wavelength(nm)7

D0- F3

600

650

700

750

wavelength(nm)Figure 2

P-180

550

7

D0- F4

D0- F1Figure 3

Cubic Lipid Phase & Bicelle Crystallization of
Membrane ProteinsHartmut Luecke

Cubic Lipid Phase (CLP): The CLP method for membrane protein crystallization has beenrefined to allow large-scale screening of various membrane proteins. The various parameters(CLP lipid, water content, bilayer lipid additive, pH, ionic strength, precipitating agent etc.)
can be varied. Three distinct seven-transmembrane proteins where crystallized and theirhigh-resolution structures determined.
Bacteriorhodopsin (BR): High-resolution maps from X-ray diffraction of bacteriorhodopsin
crystal obtained in CLP and some of its photointermediates have yielded insights to how theisomerization of the bound retinal drives ion transport. Although some important mechanistic
details are still undecided, the events of the photochemical cycle are now understood to reflectchanges in specific hydrogen bonds of protein groups and bound water molecules in response
to motions of the retinal chain. A nearly complete lipid bilayer is also present in the
x-ray-derived atomic model.
Sensory Rhodopsin (SR): Atomic resolution structures of a phototaxis receptor in haloarchaea,
the first sensory member of the widespread microbial rhodopsin family, have yielded insights
into spectral tuning and the interaction face with its membrane-embedded transducer. Spectral
differences between the sensory rhodopsin and light-driven proton pump bacteriorhodopsin
depend largely on the repositioning of a conserved arginine residue in thechromophore-binding pocket. Information from the structures combined with biophysical andbiochemical analysis have established a model for receptor activation and signal relay
involving light-induced helix tilting in the receptor transmitted to the transducer by lateraltransmembrane helix-helix interactions.
Anabaena SR (ASR): The structure of a sensory rhodopsin from the cyanobacterium
Anabaena has been determined to 1.9 Å resolution. This represents the first eubacterial
rhodopsin structure. In comparison to the archaeal rhodopsins BR and SR there are many
striking rearrangements and shifts in hydrogen bonding patterns on both the extracellular andthe cytoplasmic half of the receptor. Also, the cytoplasmic face, which is thought to interact
with the soluble transducer, is structurally well defined and very different from that of thearchaeal rhodopsins. The structure of the soluble transducer of this photoreceptor (ASRT) has- 242 -

AsCA’09

Posteralso been determined - it forms a C4 tetramer with a new all-beta fold. Studies
characterizing the interaction between transmembrane photoreceptor and soluble transducer
are underway.
Xanthorhodopsin (XR): a light-driven ion pump from the halophilic eubacterium Salinibacter
ruber found in saltern crystallizer ponds of Spain, contains a blue-absorbing carotenoid thatfunctions as a light-harvesting antenna for its retinal chromophore. In addition to theadaptations to bind and accurately position the carotenoid antenna for efficient excited-stateenergy transfer to the retinal, XR exhibits major structural differences to the previously
studied microbial pumps and photoreceptors, in particular near the initial proton acceptor,
Asp-96 (Asp-85 in BR), which forms a salt bridge with a histidine conserved inproteorhodopsin, as well as in the region of Arg-93 (Arg-82 in BR) and in the BC loop. The
rearrangement of the latter causes the formation of a large aqueous pocket, which is accessible
to the bulk solvent, in a region where the proton release group of bacteriorhodopsin (Glu-194,
Glu-204, ordered waters) is located.

P-181

New Inorganic Second-order NLO Materials Based onLone Pair Cations
Jiang-Gao Mao, Ting Hu, Yong Zhou, Chuan-Fu Sun and Fang Kong
State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the
Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, P. R. China(mjg@fjirsm.ac.cn)

The search of new second-order nonlinear optical (NLO) materials is of current interest andgreat importance owing to their applications in photonic technologies. Currently, the mostwidely used such materials are inorganic crystals based on borates such as β-BaB2O4 (BBO)
and LiB3O5 (LBO) and phosphates such as KH2PO4 (KDP) and KTiOPO4 (KTP).1 It isreported that systems contain a lone pair cation such as Se(VI), Te(IV) and I(V) are apt toform non-centrosymmetric structures (NCS) with good second-order NLO properties.2 Ourgroup has been working on NLO materials based on lone pair cations for many years. Some
compounds showing good second-order NLO properties are summarized below.
1. Combinations of borate and selenite.
The combination of B-O and Se(IV)-O bonds led to a new type of second-order NLO
compound, Se2B2O7 with a SHG efficiency of 2.2xKDP. Its structure features a 3D network
composed of B2O78- anions made of two corner-sharing BO4 groups which are further bridged
by lone pair containing Se(IV) cations in an asymmetric SeO3E(E is lone pair) geometry. It isstable up to 350 °C.
2. Combinations of two types of lone pair cations.
A serial of noncentrosymmetric (NCS) mixed metal iodates, namely, Ln3Pb3(IO3)13(µ-O) (Ln= La, Ce, Pr, Nd), have been synthesized by hydrothermal reactions of Ln2O3 (Ln = La, Ce, Pr,
Nd), PbCl2, I2O5 and H2O at 200 °C.
All four isostructural compounds exhibit a three-dimensional crystal structure that consists of- 243 -

AsCA’09

PosterLnO9 polyhedra that are connected by asymmetric IO3 group with the Pb2+ inserted into thevoids of the thus formed network via Pb-O bonds. SHG measurements on the La, Pr and Ndcompounds indicate that they display SHG responses of 2×KDP, 1×KDP and 0.8×KDP,
respectively. The La, Pr and Nd compounds are also thermally stable up to 500, 500 and 420
oC, respectively.
3. Combinations of d0-Transition metal ion and a lone pair cation.
By incorporation of Mo(VI) and Te(IV), Ag2Mo3Te3O16 with a large SHG response of 8xKDP
was obtained. Its structure features one-dimensional [Mo3Te3O16]2- anionic chains composedof [Mo3O14]10- clusters interconnected by [Te3O8]4- anions via corner-sharing, such 1D chainsare further interconnected by Ag+ ions into a 3D network.
By combination of V(V) and Te(IV) we obtained Cd4V2Te3O15 with a moderate strong SHG
efficiency of about 1.4 times of KDP. Its structure features a 3D network in which thecadmium tellurite layers are bridged by "isolated" VO4 tetrahedra and 1D vanadium oxide
chains of corner-sharing VO4 tetrahedra. It is thermally stable up to about 840 ºC andtransparent in the IR region. Furthermore, its large crystal crystals could be grown from thestoichiometric melts theoretically.
By the combination of Nb5+ cation with d0 electronic configuration and lone pair containing
iodate anion, a new SHG material, BaNbO(IO3)5 has been prepared. Its anionic structure canbe considered to be “zero-dimensional”, composed of an axially distorted NbO6 octahedron
linked with five IO3- groups and one terminal O2- anion with the Ba2+ cations acting as spacers
between these anions. It exhibits a very large SHG signal of about 14 x KDP and isphase-matchable. It has also high thermal stability and wide transparent region.
References
1. P. Becker, Adv. Mater. 1998, 10, 979-992.
2. Chang, H.-Y.; Kim, S.-H.; Halasyamani, P. S.; Ok, K. M. J. Am. Chem. Soc. 2009, 131, 2426.
3. (a) Kong, F.; Huang, S.-P.; Sun, Z.-M.; Mao, J.-G.; Cheng, W.-D. J. Am. Chem. Soc. 2006, 128,
7750-7751; (b) Jiang, H.-L.; Huang, S.-P.; Fan, Y.; Mao, J.-G.; Cheng, W.-D. Chem. Eur. J. 2008, 14,1972; (c) Hu, T.; Qin, L.; Kong, F.; Zhou, Y.; Mao, J.-G. Inorg. Chem. 2009, 48, 2193; (d) Zhou, Y.; Hu,
C.-L.; Hu, T.; Kong, F.; Mao, J.-G. Dalton Trans. 2009, Advanced Papers; (e) Sun, C.-F.; Hu, C.-L.; Xu,
X.; Ling, J.-B.; Hu, T.; Kong, F.; Long, X.-F., Mao, J.-G. J. Am. Chem. Soc. 2009, Articles ASAP.

P-182

Crystal structure and phase transitions in
C5H10NH2PbI3
Munehiko Nakatsuma, Miwako Takahashi, Kota Takano, Takuro Kawasaki,
Kunimitsu Kataoka and Ken-ichi Ohshima
Institute of Materials Science, University of Tsukuba, Japan(nakatsuma@jb.bk.tsukuba.ac.jp)

The lead-halide perovskites material C5H10NH2PbI3 is one-dimensional semiconductor. In the
crystal, semiconducting parts of one-dimensional chains of face-sharing lead-iodide octahedra
are separated by barrier parts of C5H10NH2+ molecules. The crystal structure at room
temperature is orthorhombic with space group of C2221 (No.20) [1]. It has been shown by
Raman scattering, DSC and optical absorption measurements that the structure undergoes- 244 -

AsCA’09

Postertemperature-induced successive phase transitions: phase I above 284.5 K, phase II for 255.5 K
to 284.5 K, phase III for 250 K to 255.5 K, and phase IV below 250 K. The transitions arefound to involve rotational/orientational ordering of the C5H10NH2+ molecules [2], but precise
structure at each phase has not been determined yet. In order to determine the structures for
low temperature phases, we have performed single crystal X-ray diffraction measurements.
Single crystals of C5H10NH2PbI3 were grown by solution method. The integrated intensities
were collected with Rigaku R-AXIS RAPID. Data collections for phase II and III werecarried out at 275K and 265K, respectively. The structures in phase II is determined to be
monoclinic P21 (No.4) with lattice parameters a= 10.110(3)Å, b= 8.149(2)Å, c= 15.923(3)Å,β = 99.980 (8)º and volume V= 1292.06(53) Å3 (Fig.1). In the phase III, the structure is
identified to be P21 with lattice parameters a= 17.310(26)Å, b= 8.205(12)Å ,c= 20.091(25)Å,β = 115.829(60)º, and V= 2568.49(22) Å3, which is twice as large as that of phase I (Fig.2). It
is found that displacement and distortion of lead-iodide octahedra play an important role in
the phase transitions.

Fig. 1

Fig. 2

References
1.
2.

G.V.Gridnova, E.A.Ziger, V.M.Kkoshkin,S.V.Lindemann,Yu.T.Struchkov,V.E.shklover:
Akademii Nauk 278(1984)414
S. Oishi, K. Matsuishi and S. Onari: private communication.

P-183

Doklady

Crystallographic structure and luminescence
properties of Y(Ta,Nb)O4:Eu3+,Tb3+ phosphors
Mihail Nazarov, Do Young Noh, Su Woong Lee
Department of Materials Science and Engineering, Gwangju Institute of Science andTechnology, 1 Oryong-dong, Buk-gu, Gwangju 500-712, Republic of Korea(Nazarov@gist.ac.kr)

Crystallographic analysis plays an essential role in luminescence investigations of phosphors.
The detailed X-ray diffraction (XRD) analysis, energy dispersive spectroscopy (EDS),Electron probe micro analysis (EPMA), Infrared and Raman spectroscopy as well as
photoluminescence (PL), cathodoluminescence (CL) and X-ray luminescence (XL) werecarried out in order to enlarge the understanding of the radiative processes in yttrium tantalate(YTaO4) and niobate (YNbO4)
phosphors activated by europium and terbium. However, tothe best of our knowledge, no work has been reported using doubly activators for Y(Ta,Nb)O4
phosphors.
Three types of host lattices with double activation by rare earth elements Eu3+ and Tb3+ were
- 245 -

AsCA’09

Posterprepared by solid state reaction method. General formula of the investigated phosphors is
Y1-x-yEuxTbyTa1-zNbzO4, denoted as Y(Ta,Nb)O4:Eu3+,Tb3+. For the samples we measured, x =0.025, y = 0.025 and z = 0; 0.15 or 1.
The crystalline structure and order degree of phosphor samples were evaluated on the basis of
Synchrotron X-ray Diffraction (SR-XRD) patterns and FT-IR spectra. The high resolution andthe excellent detectors for SR-XRD (Pohang Accelerator Laboratory, Korea) permit theidentification and quantification of trace phases not possible use other means especially for
double activated phosphors. The results show that the compound YTaO4 has a fergusonite(distorted sheelite) structure with I2-C23 space group symmetry and site symmetry C2 for themolecular TaO4. Monoclinic M’ structure of YTaO4 is differ from monoclinic M-structure of
YNbO4. FT-IR spectra put in evidence that the vibrations corresponding to NbO43- groups
and TaO43- groups are different. The shape of FT-IR spectra in the domain of MO4 groupvibrations (where M = Ta, Nb) illustrates the change of the metal-oxygen bonds number: sixin octahedron coordination YTaO4 and four in tetrahedral coordination YNbO4. In
M'-YTaO4:Eu3+,Tb3+, the Y atoms are surrounded by 8-coordinated oxygen atoms forming a
distorted cube. From our calculations the Y-O averaged distance is 2.37Å. The Ta atoms are ina distorted octahedral coordination with four shorter Ta-O bonds at 1.96Å and 1.87Å and twolonger at 2.23Å. The total amount of atoms inside of the M'-YTaO4 structure is: 2 yttrium
atoms, 2 tantalum and 8 oxygen atoms. Following the same procedure, we calculated anddrew the crystallographic structure of YNbO4:Eu3+,Tb3+. The Y atoms are also surrounded by
8-coordinated oxygen atoms forming a distorted cube. The Y-O averaged distance is 2.35Å.
The Nb atoms are in a distorted octahedral coordination, with four shorter Nb-O at 1.94Å and1.83Å and two longer at 2.43Å. Adding Eu3+ and Tb3+ appears to have negligible effect on the
crystallographic structure and on the shape of infrared spectra in low activator concentrations,but terbium activation decreases the absorbance in YNbO4.
PL, CL and XL illustrate very high intensity of Eu emission in both matrixes, whereas Tb
incorporation is very effective only in YTaO4. Contribution of both rare earth activators isobserved in the all spectra, from this, we can vary the concentration of these activators and geta broad variation of visible photoluminescence colors. These phosphors may be applied to the
X-ray intensifying screens for medical diagnosis, cold cathode lighting and in many different
optoelectronic devices.

P-184

Structural Membrane Proteomics – X-ray Structure of
Sulfide:Quinone Oxidoreductase on The
Hyperthermophilic Eubacteria Aquifex aeolicus
Guohong Peng, Marco Marcia, Ulrike Wedemeyer, Ye Gao, Tao Wang, Tanja
Hedderich, Chuli Zhang & Hartmut Michel
Max Planck Institute of Biophysics Frankfurt am Main60439, Germany,(guohong.peng@mpibp-frankfurt.mpg.de)Proteins from hyperthermophilic organisms are considered to be more stable and more rigid
than their mesophilic counterparts. Therefore, the possibility of obtaining stable,
homogeneous and crystallizable membrane protein complexes should be better withcomplexes from thermophilic organisms than with complexes from mesophilic ones. Thus, we- 246 -

AsCA’09

Posterhave purified and characterized a number of proteins and protein complexes from native
membranes of Aquifex aeolicus using conventional biochemical techniques, identified these
proteins by mass spectrometry, and followed by crystallization trials. For those originallyannotated as hypothetical or putative proteins in Aquifex genome, we try to determine theirfunctions. So far we are able to identify 72 protein chains which belong to 38 membraneproteins/protein complexes. All of protein complexes that we have purified to homogeneity in
sufficient amount, have yielded diffracting crystals. Two structures of these protein complexes
had been determined. One of them is sulfide:quinone oxidoreductase. Surprisingly it is atrimeric, periplasmic intergral monotopic membrane protein involving into energy conversion
process. The X-ray structure of this enzyme reveals basic mechanisms of sulfide respirationand detoxification.

P-185

Kinetics of Crystalline-Non-Crystalline Phase
Transition in Sucrose
Son Van Phung 1, Taro Fujita2, Miwako Takahashi1 and Ken-ichi Ohshima1
1
Institute of Materials Science, University of Tsukuba, Tsukuba 305 -8573, Japan,(ohshima@bk.tsukuba.ac.jp)
2
Microphase Co.., Ltd., Tsukuba 300 – 2651, Japan, (fujita@bk.tsukuba.ac.jp)

Sucrose is one of the most important ingredients in foods and has great potentialities for new
functional materials. Melting points among sucrose crystals with high purity are different
from each other, which were reported as in a temperature range between 433 and 464K1). The
measurements were used by macroscopic techniques, e.e. differential scanning calorimeterand thermal gravimetry-differential thermal analysis (TG-DTA). Though there are several
proposals for understanding of different melting points based on the content of the impurity,
different preparation and so on, no detailed structural studies have been performed for such
big difference of melting points. It is helpful to try the time-dependent data collection of themelting points at the fixed temperature for clearing the inconsistency.
The in-situ X-ray diffraction measurements in sucrose have been performed for investigating
the kinetics of crystalline-non-crystalline phase transition. The characteristic time until the
integrated intensity of (111) Bragg reflection becomes half was observed in a temperature
range between 413 to 433K from analyzing time-dependent X-ray diffraction intensity data.
The time called as incubation time is interpreted with the use of Avrami’s idea.
435

Temperature / K

430
425
420
415
410
405

0

20

40

60

80

100

120

140

Incubation time / minutes

Fig 1. Temperature vs. incubation time

References
M. Okuno, S. Kishihara, M. Otsuka, S. Fujii and K. Kawasaki : Int. Sugar J. 105 (2003) 29.
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P-186

Poster

Metal Coordination Polymers containing tetrapyridyl
based Ligands
Abdul Malik Puthan Peedikakkal1, Jagadese J. Vittal*1
Department of Chemistry, National University of Singapore, 3 Science Drive 3,
Singapore 117543 (chmjjv@nus.edu.sg)

Coordination polymers or Metal-organic frameworks are an interesting class ofmolecule-based on metal-connecting nodes and bridging ligands. They have received
considerable attention due to their potential applications in hydrogen storage, CO2 separation,
heterogeneous catalysis and having interesting magnetic, optical, electronic properties.
Nitrogen based ligands are important in constructing such materials. Here we have shownvarious structural motifs with specific topologies can be synthesized from 1,2-bis(4pyridyl)ethylene, 4,4'-bpe(L1) and (1,2,3,4-tetrkis (4-pyridyl)cyclobutane, 4,4'-tpcb (L2)ligands using transition metal ions. L2 was synthesized from L1 using photochemical [2+2]cycloaddition and isomerization reaction. L1 acts as a linear spacer in forming the networks
with metal-connecting nodes. On the other hand, one of the cyclobutane isomers of L2,
namely, rtct-4,4’-tpcb acts as an excellent four connecting tetrahedral node that have beenutilized in fabricating three dimensional framework structures. The formation ofmultidimensional frameworks including linear, zig-zag, ladder, interpenetrated andnon-interpenetrated networks with interesting topologies will be discussed during the talk.

Fig. 1, A perspective view of three dimensional network structures with specific topologies formed by L1
and L2 using metal ions (Zn(II) and Co(II).

References
1)
2)
3)

Peedikakkal, A. M. P.; Lip. L. Koh.; Vittal, J. J. Chem Communications, 2008, 441-443.
Peedikakkal, A. M. P.; Vittal, J. J. Chem-A European Journal, 2008, 14, 5329-5334.
Peedikakkal, A. M. P.; Vittal, J. J. Crystal Growth & Design, 2008, 8, 375-377.

P-187

Structural basis for the mechanism of respiratorycomplex I
Leonid Sazanov, John Berrisford
MRC Mitochondrial Biology Unit, Cambridge, UK (sazanov@mrc-mbu.cam.ac.uk)

Complex I of respiratory chains plays a central role in cellular energy production, but themechanism of this highly efficient enzyme is currently unknown. Dysfunction of complex I is
- 248 -

AsCA’09

Posterimplicated in many human neurodegenerative diseases and aging. Previously, we have solved
the first structure of the hydrophilic domain of complex I [1,2]. The domain represents thecatalytic core of the complex and consists of eight different subunits of 280 kDa total mass. It
contains all known redox centres of the enzyme – 9 Fe-S clusters and the primary electron
acceptor flavin mononucleotide.
Here, we present several X-ray structures of the oxidized and reduced hydrophilic domain ofcomplex I from Thermus thermophilus, which were determined at up to 3.1 Å resolution.
They reveal the mode of interaction with substrate NADH and conformational changes in thecomplex upon reduction. Fe-S cluster N2 is the electron donor to quinone and is coordinatedby unique motif involving two consecutive (tandem) cysteines. An unprecedented “on/off
switch” (disconnection) of coordinating bonds between the tandem cysteines and this cluster
was observed upon reduction. Comparison of structures suggests a novel mechanism ofcoupling between electron transfer and proton translocation, which will be discussed.
References[1] Hinchliffe, P., and Sazanov, L. A. (2005) Science 309, 771-774[2] Sazanov, L. A., and Hinchliffe, P. (2006) Science 311, 1430-1436

Structural basis for translational inhibition by thetumour suppressor Pdcd4

P-188

Portia G Loh1, Hsin-Sheng Yang2, Haiwei Song1
1
Institute of Molecular and Cell Biology, Proteos, Singapore(haiwei@imcb.a-star.edu.sg)
2
Graduate Center for Toxicology and Markey Cancer Center, College of Medicine,
University of Kentucky, Lexington, KY, USA

Programmed cell death protein 4 (Pdcd4) is a novel tumor suppressor protein, which functions
as an inhibitor of translation initiation and consequently prevents neoplastic transformation andtumour invasion. Loss of Pdcd4 expression is correlated to tumor progression in lung, colon,
prostate, and breast cancers. The inhibition of translation initiation by Pdcd4 is achieved throughspecific interactions of its two tandem MA3 domains with the eukaryotic translation initiation factors
eIF4A. We have solved the crystal structures of an N-terminal-truncated Pdcd4 in free form andin complex with eIF4A. Upon binding to eIF4A, Pdcd4 undergoes a marked conformationalchange to form a heterotrimeric complex with eIF4A, with one Pdcd4 binding to two eIF4A
molecules in two different modes. The binding of Pdcd4 to eIF4A is required to inhibit the
enzymatic activity of eIF4A, translation initiation, and AP-1-dependent transcription. Both
MA3 domains are required to efficiently compete with the C-terminal domain of eIF4G(eIF4Gc) for binding to eIF4A whereas a single MA3 is sufficient to inhibit translation. Our
structural and mutational analyses reveal that Pdcd4 inhibits translation initiation by trappingeIF4A in an inactive conformation, and blocking its incorporation into the eIF4F complex.
These results may help design drugs that mimic the action of Pdcd4 to treat cancers whichhave lost Pdcd4 expression.

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Poster

Exploring the Bond topological and Electrostatic
properties of Benzimidazole molecule via
Experimental and Theoretical Charge Density Study

P-189

Arputharaj David Stephen,a Reji Thomas,b Vijayan Narayayanasamyc and Poomani
KumaradhasaaDepartment of Physics, Periyar University, Salem-636 011, India(davidstephen_dav@yahoo.co.in)bChemistry and Physics of Materials Unit, Jawaharlal Nehru Centre for Advanced
Scientific Research, Jakkur, Bangalore-560 064, IndiacNational Physical Laboratory, Dr. K.S. Krishnan Road, NewDelhi-110 012, India

The experimental electron density distribution of Benzimidazole has been determined frommultipole refinement model using accurate high resolution X-ray diffraction intensity datacollected at 100K. The theoretical charge density distribution was calculated from high level
ab initio and Density functional theory calculations, using MP2 and B3LYP methods with thebasis set 6-311G**. The bond topological analysis of the experimental electron density shows
the difference of charge density distribution in the homo and heteroatomic bonds. The
molecular charge density difference between theory and experiment explicitly reveals theinfluence of crystal field effect in the experimental electron density distribution. The
isosurface electrostatic potential shows the electro positive and negative regions in themolecule. A large negative potential found at the vicinity of nitrogen atom. The bond
topological analysis on intermolecular hydrogen bond confirms the strength of interaction
from ρbcp and ∇2ρbcp values.

Isosurface representation of experimental electrostatic potential of Benzimidazole molecule
Blue: positive potential (+0.5 eÅ-1), red: negative potential (-0.2 eÅ-1)

X-Ray Based Enzyme Design for Alkaloid Libraries

P-190

Joachim Stoeckigt
College of Pharmaceutical Sciences, Institute of Materia Medica, Zhejiang University,
383 Yu Hang Tang Road, Hangzhou, Zhejiang Province, 310058, P.R. China.
(joesto2000@yahoo.com)

Medicinal plants are a rich source of natural products with high pharmacological andtherapeutic value. It is estimated that less than 10% of higher plants from rain forests are wellinvestigated for the occurrence of biological active compounds and remaining 90% of theplants are unexplored. Because of drastic environmental changes, a higher demand of palm oil
production and climate influences, rain forests are shrinking world wide dramatically. This
results in irreversible loss of still unknown secondary metabolites, loss of their enzymes of- 250 -

AsCA’09

Posterbiosynthesis and loss of the corresponding genes.
The lecture will summarize enzymatic and genetic approaches for generation of novel
libraries of biologically important alkaloids based on the biosynthesis of alkaloids of the plantRauvolfia serpentina, an Indian medicinal plant from Ayurvedic medicine. In particular thefollowing points will be discussed :-detection, purification and partial sequencing of the new enzymes
heterologous enzyme expression in E. coli and crystallization
x-ray analysis and exploration of enzyme mechanisms
rational enzyme re-design and generation of new alkaloid libraries

Recently obtained structural results are illustrated in the following network of Rauvolfia
alkaloids :References
1.
2.
3.
4.

Yang, L., Hill, M., Wang, M., Panjikar, S., Stoeckigt, J. Angew. Chemie. 2009, (in press).
Stoeckigt, J., Panjikar, S. Nat. Prod. Rep. 2007, 24, 1382-1400.
Barleben, L., Panjikar, S., Ruppert, M., Koepke, J., Stöckigt, J. Plant Cell. 2007, 19, 2886-2897.
Loris, E., Panjikar, S., Ruppert, M., Barleben, L., Unger, M., Schubel, H., Stöckigt, J. Chem. Biol.
2007, 14, 979-985.

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AsCA’09

PosterCrystal Structure of Porcine Reproductive andRespiratory Syndrome Virus (PRRSV) Leader
Protease Nsp1α

P-191

Yuna Sun1, $, Fei Xue2, $, Yu Guo3, Ming Ma1, Ning Hao1, Xuejun C. Zhang1,
Zhiyong Lou2,*, Xuemei Li1, *, and Zihe Rao
1National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of
Science, Beijing, 100101, China, ( lixm@sun5.ibp.ac.cn)
2Structural Biology Laboratory, Tsinghua University, Beijing, 100084, China,(louzy@xtal.tsinghua.edu.cn)
3College of Life Sciences and Tianjin State Laboratory of Protein Science, Nankai
University, Tianjin 300071, China

Porcine Reproductive and Respiratory Syndrome Virus (PRRSV), a positive strand RNA
virus that belongs to the Arteriviridae family of Nidovirales, has been identified as thecausative agent of porcine reproductive and respiratory syndrome (PRRS). Nsp1-alpha is theamino (N)-terminal protein in a polyprotein encoded by the PRRSV genome and is reported tobe crucial for subgenomic (sg) mRNA synthesis, presumably by serving as a transcription
factor. Before functioning in transcription, nsp1-alpha proteolytically releases itself from
nsp1-beta. However, the structural basis for the self-releasing and biological functions of
nsp1-alpha remains elusive. Here we report the crystal structure of nsp1-alpha of PRRSV(strain XH-GD) in its naturally self-processed form. Nsp1-alpha contains a zinc finger domain(which may be required for its biological function), a papain-like cysteine protease (PCP)
domain with a zinc ion unexpectedly bound at the active site (which is essential for proteolytic
self-release of nsp1-alpha), and a carboxyl-terminal extension (which occupies the substratebinding site of the PCP domain). Furthermore, we determined the exact location of thensp1-alpha self-processing site at Cys-Ala-Met180//Ala-Asp-Val, from crystallographic data
and N-terminal amino acid sequencing. The crystal structure also suggested an in cis
self-processing mechanism for nsp1-alpha. Furthermore, nsp1-alpha appears to have a dimericarchitecture both in solution and as a crystal, with a hydrophilic groove on the molecularsurface that may be related to nsp1-alpha's biological function. Compared with existing
structure and function data, our results suggest that PRRSV nsp1-alpha functions differently
from other reported viral leader proteases, such as FMDV Lpro.

P-192

Structure and guest release behavior comparison ofinclusion crystals of 1,1,2,2- tetrakis (4- hydroxy
phenyl) ethane and imidazole derivatives
Takenori Takeda1, Akiko Sekine1, Hidehiro Uekusa1, Natsuki Amanokura1,
Masami Kaneko2 and Hiroshi Suzuki2
1
Department of chemistry and materials science, Tokyo Istitute of Technology, 2-12-1,
Ohokayama, Meguro-ku, Tokyo, 152-8551, Japan (takeda.t.ab@titech.ac.jp)
2
Nippon Soda Co.Ltd, 2-1-2-chome, Ohtemachi, Chiyodaku, Tokyo 100-8165, Japan

1,1,2,2-tetrakis(4-hydroxyphenyl)ethane, TEP (Fig.1) is a tetrapodal host molecule which has
four hydroxyl phenyl groups in different directions to form different types of hydrogenbonding host frameworks. Inclusion compound of TEP and imidazole derivative (Fig.2), an
anionic polymerization initiator of epoxy resin, is an industrial material that has controlled- 252 -

AsCA’09

Posterpolymerization initiation temperature depending on the guest release temperature [1]. In thisstudy, a series of inclusion crystal structures were analyzed to reveal the relationships
between the guest release temperature and crystal structure.
Seven analyzed inclusion crystals have the guest release temperatures within the range of
160-220°C. In both imidazole (166°C) and 2-phenylimidazole (220°C) inclusion compounds(1 and 7), guests are stacked in similar channel structure parallel to a-axis (Fig.3). These
guests were connected with hosts by 1: OH…N, 7: OH…N and NH…O hydrogen bondings.
The reason why 7 has the highest guest release temperature of the seven can be explained thatthe guest release motion from the channel was prevented by a bulky substituent.
4-methylimidazole and 1-methylimidazole have the same molecular weight, but quite
different thermal stability (mp. -60°C and 46°C). It is interesting that their inclusion crystals(3 and 4) were isomorphs. Guests were arranged in the layer parallel to bc plane, andconnected to the hosts by OH...N hydrogen bonding, and also NH…π and CH…π interaction,
respectively. In spite of the different stability of the guest imidazoles, they have similar
guest release temperature indicating that the stability of the guest in the inclusion crystal
depends on the crystal structure. 2-methylimidazole, 2-n-propylimidazole, and 2-ipropylimidazole inclusion compound (2, 5, and 6) were the ethyl acetate solvates, and thethermogravimetry measurements showed the release of the ethyl acetate and imitazole occur
in two stages.

Fig.1:TEP

Fig.2:imidazole derivativeFig.3: Channel structure
1 (left, b axis projection) 7 (right, c axis projection)

Reference
N. AMANOKURA et al. Polymer Journal, Vol. 39, No. 8, pp. 845–852 (2007)

P-193

Calcium binds to LipL32, a lipoprotein from
pathogenic leptospira, and modulates fibronectinbindingJung-Yu Tung1, Shao-Wen Chou1, Chien-Chih Lin, Yi-Ching Ko2, Chih-Wei Yang2,
and Yuh-Ju Sun1
1
Institute of Bioinformatics and Structural Biology, National Tsing Hua University,
Hsinchu, Taiwan (d934605@oz.nthu.edu.tw)
2
Kidney Institute and Graduate Institute of Clinical Medical Science, Chang Gung
Memorial Hospital, Taiwan

Tubulointerstitial nephritis is a cardinal renal manifestation of leptospirosis. LipL32, avirulence factor of pathogen Leptospira, is the major lipoprotein of outer membrane proteins.
- 253 -

AsCA’09

Poster

LipL32 recognizes extracellular matrix components and adheres to the host cell to evade an
immune response. The crystal structure of Ca2+-bound LipL32 was determined at 2.3 Å.
LipL32 consists of a novel polyD sequence with a cluster of seven aspartate residues to form
a continuous acidic surface patch for Ca2+ binding. A significant conformational change was
induced when Ca2+ bound to LipL32. The binding of fibronectin F30 to LipL32 wasmonitored by Stains-all dye and which interaction is associated with Ca2+. Based on the
Ca2+-bound LipL32 crystal structure and the Stains-all circular dichroism results, a
LipL32-F30 complex model was proposed. The fibronectin-binding site of LipL32 is near tothe polyD region, and LipL32 interacts with F30 through significant electrostatic interactions.
The Ca2+ binding to LipL32 might be important for extracellular matrix interaction with thehost cell in Leptospira.

P-194

Purification, crystallization and preliminary data
analysis of Proteorhodopsin
Ning Wang, Tingting Ran, Weiwu Wang
Nanjing Agricultural University, 1 Weigang Road, Xuanwu District, Nanjing, Jiangsu,
210095, China (wwwang@njau.edu.cn)

Proteorhodopsins (PRs), are seven TM light-driven proton pumps using retinal as
chromophore, which genes were isolated from marine micro-plankton(1-3). Sequence
analysis shows that PRs share less than 30% identity with all other microbial rhodopsins, suchas bacteriorhodopsin (Br), sensory rhodopsin (SR), anabaena rhodopsin.
To understand the light driven proton pumping mechanism of PRs, PRs were overexpressed in
E. coli and purified by IMAC, the protein purity was then analyzed by SDS PAGE. The
purified protein was crystallized by vapor diffusion method with MPD as precipitant. The
crystal grew to full size (0.02X0.02-0.04X0.2 mm) within a few days. The X-ray diffraction
data were collected to 3.3 Å by using synchrotron radiation at SLS (Swiss Light Source).
Preliminary x-ray diffraction data analysis has shown that the crystal belongs to orthorhombic
space group P21212, with 5-6 PR molecules in the asymmetric unit; the unit cell parameters
were a=161, b=169 and c=64 Angstrom. Using molecular replacement to solve the structure
did not success due to the low sequence similarity with its homologs, the selenomethionine
crystal deravitive and heavy atom deravitives are in preparation.

A. Purification of PR

Keywords:

B. Crystallization of PR

C. The diffraction pattern of PR crystal

Proteorhodopsins (PRs), Crystallization, Protein purification

References- 254 -

AsCA’09
1.
2.
3.
4.

PosterBéjà O, et. Al. Bacterial rhodopsin: evidence for a new type of phototrophy in the sea. Science.
289(5486):1902-6. (2000)
Béjà O, et. Al. Proteorhodopsin phtotrophy in the ocean. Nature. 411(6839):786-9. (2001)
Venter JC, et. Al. Environmental genome shotgun sequencing of the Sargasso Sea. Science.
304(5667):66-74. (2004)
Rusch DB, et. Al. The Sorcerer II Global Ocean Sampling expedition: northwest Atlantic througheastern tropical Pacific. PLoS Biol. 5(3):e77. (2007)

Structure, mechanistic action, and essential residuesof laminaripentaose-producing β-1,3-glucanase
1

P-195

1

2

1

Wen-Ching Wang , Hsin-Mao Wu , Sheng-Wen Liu , Ming-Tsung Hsu , Jong-Yih
3
2
Lin , and Yaw-Kuen Li ,1
Institute of Molecular and Cellular Biology & Department of Life Science, National
Tsing Hua University, Hsinchu, Taiwan;
2
Department of Applied Chemistry, National Chiao Tung University, Hsinchu, Taiwan;
3
Department of Mechanical Engineering, National Chung Hsing University, Taichung,TaiwanLaminaripentaose-producing β-1,3-glucnase (LPHase), a member of glycoside hydrolase
family 64, cleaves a long-chain polysaccharide β-1,3-glucan into specific pentasaccharide
oligomers. We have solved the crystal structure of LPHase from Streptomyces matensis
DIC-108 to 1.62 Å resolution using multiple-wavelength anomalous dispersion methods. The
LPHase structure shows a barrel domain and a mixed (α/β) domain, forming a wide-open
groove between the two domains. The liganded crystal structure was also solved to 1.80 Å,
showing an overall identical conformation with the native enzyme. Within the wide groove, alaminaritetraose molecule is found to sit in an electronegatively charged central region and is
proximal to several conserved residues including two carboxylates (Glu154 and Asp170) and
four other sugar-binding residues (Thr156, Asn158, Trp163, and Thr167). Molecular modelingusing a laminarihexaose as a substrate suggests roles for Glu154 and Asp170 as acid and basecatalysts, respectively, whereas the side chains of Thr156, Asn158, and Trp163 demarcate subsite+5. Site-directed mutagenesis of Glu154 and Asp170 confirms that both carboxylates are
essential for catalysis. Together, our results suggest that LPHase uses a direct displacement
mechanism involving Glu154 and Asp170 to cleave a β-1, 3-glucan into specificα-pentasaccharide oligomers.

P-196

A novel (4,8)-connected 3D metal-organic framework
based on in situ ligand
Peng Li, Jiaying Lou, Yaming zhou, Linhong Weng*
Shanghai Key Laboratory of Molecular Catalysis and Innovative Materia1, China.
Department of Chemistry, Fudan Unviersity, Shanghai 200433, China,(lhweng@fudan.edu.cn)

Design and construction of metal-organic frameworks (MOFs) whose topological paradigms
consistent with those of natural minerals, have attracted considerable due to its potential
application for these materials.1, 2 However, there is an unfavorable lack of investigation of- 255 -

AsCA’09

Posterbinodal high-connected structures, such as (4,8)-connected framework. Previous examples of(4,8)-connected frameworks are reminiscent of binary inorganic compounds fluorite CaF2(flu),3, 4 one of the most important and frequently encountered structure type in minerals, andPoCl2 (scu)5 which is built from square-planar and cubical nodes.
Here in this report, one 3D MOF [Zn3(bdc)2(4-bph)]n·2n(H2O) (1) (H2bdc =1,4-benzenedicarboxylic acid, 4-bph = N,N’-bis(4-picolinoyl) hydrazine) was isolated byhydrothermal method, the 4-bph was synthesized in situ via the hydrolysis of
2,5-bis(4-pyridyl)-1,3,4-oxadiazole) (4-bpo) with the aid of acid. Compound 1 is constructedfrom a distorted planar four-connected node and a distorted eight-connected node, and eachfour-connected node connects four eight-connected nodes, while each eight-connected node
links four four-connected nodes and four eight-connected nodes. Consequently, the net of 1
defines a new type of (4, 8)-connected topological framework which is unobserved anddifferent from the known flu and scu network topologies (Fig. 1).

Fig. 1 A scheme of novel (4,8)-connected network structure constructed of a trimetalilc cluster (cyan pellet)
and a planar four-connected 4-bph building block (blue pellet).

References
1.
2.
3.

Rosi, N. L.; Kim, J.; Eddaoudi, M.; Chen, B. L.; O'Keeffe, M.; Yaghi, O. M. J. Am. Chem. Soc. 2005,
127, (5), 1504-1518; Mueller, U.; Schubert, M.; Teich, F.; Puetter, H.; Schierle-Arndt, K.; Pastre, J. J.
Mater. Chem. 2006, 16, (7), 626-636.
Chun, H.; Kim, D.; Dybtsev, D. N.; Kim, K. Angew. Chem.-Int. Edit. 2004, 43, (8), 971-974; Zou, R.
Q.; Zhong, R. Q.; Du, M.; Kiyobayashi, T.; Xu, Q. Chemical Communications 2007, (24), 2467-2469.
Ma, L. Q.; Mihalcik, D. J.; Lin, W. B. J. Am. Chem. Soc. 2009, 131, (13), 4610-4612.

P-197

Solvent-Dependent Assembly of Ni(II) Coordination
Polmers: Structural Variation from 1D to 2D
Jiaying Lou, Peng Li, Yaming Zhou, Linhong Weng*
Shanghai Key Laboratory of Molecular Catalysis and Innovative Materia1, China.
Department of Chemistry, Fudan Unviersity, Shanghai 200433, China,(lhweng@fudan.edu.cn)

The assembly of coordination polymers by design is one aim of crystal engineering because
their structures are intimately related to their outstanding bulk properties.[1,2]Twocoordination
polymers{[Ni(3-bpo)2(p-BDC)(H2O)2]·(H2O)2}n(1)
and{[Ni(3-bpo)(p-BDC)]·(H2O)4}n (2) based on mixed ligands, where 3-bpo =2,5-bis(4-pyridyl)-1,3,4-oxadiazole and p-BDC = 1,4-benzenedicarboxylic acid, have beensynthesized under solvothermal reactions by different solvent system. Compound 1,
synthesized from CH3OH, forms a infinite 1-D chain structure (Fig. 1) and 2, synthesized- 256 -

AsCA’09

Posterfrom 2-BuOH, shows a 2-D layered structure bridged by both ligands 3-bpo and p-BDC witha square cavity of 9.82×10.68 Å2 (Fig. 2). Their structures range from a 1D chain to a 2D
network, showing the solvent effect on the structures of the complexes.

a)b)Fig. 1 a) A portion view of 1 with atom labels of the asymmetric unit. Hydrogen atoms are omitted forclarity; b) The 1D chian for compound 1. Ni, cyan; C, grey; O, red; N, blue.

a)b)
Fig. 2 a) A portion view of 2 with atom labels of the asymmetric unit. Hydrogen atoms are omitted forclarity; b) The 2D grid network (4, 4) net construction for compound 2. Ni, cyan; C, grey; O, red; N, blue.
The green rods stand for 3-bpo, the yellow rods stand for p-bdc.

References[1][2]

J. Lee, O. K. Farha, J. Roberts, K. A. Scheidt, S. T. Nguyen, J. T. Hupp, Chem. Soc. Rev. 38 (2009)1450-1459.
P. Horcajada, C. Serre, G. Maurin, N. A. Ramsahye, F. Balas, M. Vallet-Regi, M. Sebban, F.
Taulelle, G. Ferey, J. Am. Chem. Soc. 130 (2008) 6774-6780.

Structural basis for the inhibition of human MTHFS
by N10-substituted folate analogues

P-198

Dong Wu1, Yang Li1, Gaojie Song1, Chongyun Cheng1, Rongguang Zhang2, Andrzej
Joachimiak2, Neil Shaw1, and Zhi-Jie Liu1
1
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academyof Sciences, Beijing 100101, China.(wudong@moon.ibp.ac.cn)
2Structural Biology Center, Argonne National Laboratory, IL 60439 USA.

5,10-Methenyltetrahydrofolate synthetase (MTHFS) regulates the flow of carbon through theone-carbon metabolic network, which supplies essential components for the growth andproliferation of cells. Inhibition of MTHFS in human MCF-7 breast cancer cells has beenshown to arrest the growth of cells. Absence of the three-dimensional structure of human
MTHFS (hMTHFS) has hampered the rational design and optimization of drug candidates.
Here, we report the structures of native hMTHFS, a binary complex of hMTHFS with ADP,hMTHFS bound with the N5-iminium phosphate reaction intermediate, and an
enzyme-product complex of hMTHFS. The N5-iminium phosphate captured for the first timein our crystal structure unravels a unique strategy used by hMTHFS for recognition of the- 257 -

AsCA’09

Postersubstrate and provides structural basis for the regulation of enzyme activity. Binding of
N10-substituted folate analogues places Y152 in the middle of the channel connecting ATP
binding site with the substrate binding pocket, precluding the positioning of ;-phosphate for anucleophilic attack. Using the structures of hMTHFS as a guide, we have probed the role ofresidues surrounding the active site in catalysis by mutagenesis. The ensemble of hMTHFS
structures and the mutagenesis data yield a coherent picture of the MTHFS active site,
determinants of substrate specificity, and new insights into the mechanism of inhibition of
hMTHFS.
References
1.
2.
3.
4.
5.
6.

Appling, D. R. (1991) Compartmentation of folate-mediated one-carbon metabolism in eukaryotes.
FASEB J. 5, 2645-2651
Fox, J. T., Stover, P.J. (2008) Folate-mediated one-carbon metabolism. Vitam Horm. 79, 1-44
Field, M. S., Szebenyi, D.M., Perry, C.A., Stover, P.J. (2007) Inhibition of 5,10methenyltetrahydrofolate synthetase. Arch Biochem Biophys. 458, 194-201
Jolivet, J. (1997) Human 5,10-methenyltetrahydrofolate synthetase. Methods Enzymol. 281, 162-170
Jolivet , J., Dayan, A., Beauchemin, M., Chahla, D., Mamo, A., Bertrand, R. (1996) Biochemical andMolecular Studies of Human Methenyltetrahydrofolate Synthetase Oncologist. 1, 248–253
Field, M. S., Szebenyi, D.M., Stover, P.J. (2006) Regulation of de novo purine biosynthesis bymethenyltetrahydrofolate synthetase in neuroblastoma. J Biol Chem. 281, 4215-4221

P-199

High-resolution crystal structure and functional
analysis of a truncated thylakoid lumen protein
AtTLP18.3 reveal its novel phosphatase activity
Hsin-Yi Wu1, Mao-Sen Liu, Tsan-Piao Lin1, and Yi-Sheng Cheng1,21Institute of Plant Biology, National Taiwan University, No. 1, Sec. 4, Roosevelt Road,
Taipei, 10617 Taiwan, (chengys@ntu.edu.tw)
2
Department of Life Science, National Taiwan University, Taipei, Taiwan

AtTLP18.3 is an 18.3 kDa thylakoid lumen protein with 285 amino acids. The protein can bedivided to three regions based on sequence analysis: a chloroplast transit peptide, a domain of
unknown function (DUF477) and a transmenebrane α-helix(TMH). Previous studies indicatedthat the AtTLP18.3 protein is an auxiliary protein of photosystem II (PSII) repair cycle.(Sariet al., 2007) In order to clarify the possible molecular function of the AtTLP18.3 protein, thecrystal structures of the truncated AtTLP18.3 without targeting signal and TMH were resolved.
Since there is no any methionine residue in the truncated AtTLP18.3 protein, L127M andL157M were introduced for MAD method by site-directed mutagenesis. The crystals of nativeand double mutated AtTLP18.3 shows isomorphous in space group P212121 with unit-cellparameters a = 46.9, b = 49.8, c =76.7 Å, α=β=γ=90°. Finally, the structure of mutant was
resolved at a resolution 2.6 Å using single-wavelength anomalous dispersion (SAD) method,
and the native structure was resolved at 1.6 Å resolution. For further structural comparison,
the native structure of truncates AtTLP18.3 was submitted to the DALI and CATH database to
search similar folding of protein with known function. The results showed that the structure of
AtTLP18.3 resembled to various inorganic pyrophosphatase. The enzymatic activity of
AtTLP18.3 was further identified by alkaline/acid phosphatase assay. Therefore, we proposedthat the function of AtTLP18.3 will act as phosphatase to remove the phosphate group from- 258 -

AsCA’09

Posterdamage protein for repair cycle.
References
1.
2.

Mulo, P., Sirpio, S., Suorsa, M., and Aro, E.M. (2008). Auxiliary proteins involved in the assemblyand sustenance of photosystem II. Photosynth Res 98, 489-501.
Sari, S., Allahverdiyeva, Y., Suorsa, M., Paakkarinen, V., Vainonen, J., Battchikova, N., and Aro, E.-M.
(2007). TLP18.3, a novel thylakoid lumen protein regulating photosystem II repair cycle. Biochem J
406, 415-425.

P-200

Crystallization processes of inorganic functional
materials: both experimental and theoretical studies
Dongfeng Xue* and Congting Sun
Department of Materials Science and Chemical Engineering, School of Chemical
Engineering, Dalian University of Technology, Dalian 116012, China(dfxue@chem.dlut.edu.cn)

Crystallization represents a kind of phase transition, which can be regarded as a process
related to bond formation and breaking [1]. Some basic relations were quantitatively derived
on the basis of energy viewpoint, starting from both thermodynamics and kinetics. According
to the chemical bonding characteristics of constituent atoms, relative growth rate of all
crystallographic planes can be quantitatively determined by the particular distribution ofvalence electrons, which is called as the chemical bonding theory of single crystal growth [2-4].
The ideal morphology of some important functional crystals such as ferroelectric andpiezoelectric ZnO, Cu2O, KH2PO4, and LiNbO3, has been successfully predicted by using thechemical bonding theory, which consists well with our experimental results. Someobservations concerning the morphology evolution can also be kinetically simulated by thepresent theory [5,6]. The obtained results indicate that the microscopic constituent chemicalbonds can help us to comprehensively understand the crystallization mechanism on the basisof quantitative calculations of growth rate in different crystal faces. The chemical bonding
theory builds up a link between the crystallographic structure, growth morphology andmicroscopic chemical bonds of crystal materials, which provides us a useful microscopic tool
to quantitatively understand single crystal growth behaviors.
References[1] http://www.serialspublications.com/journals1.asp?jid=445&jtype=1[2] C. Sun, D. Xue, Chemical Bonding Theory of Single Crystal Growth: a Crystallographic Viewpoint,
Astrophysics and Condensed Matter (Horizons in World Physics, Volume 262), Nova Science
Publishers, Ed. Thomas G. Hardwell, 2008, Chapter 8, pp. 215-234.
[3] X. Yan, D. Xu, D. Xue, Acta Materialia 55(17) (2007) 5747-5757.
[4] D. Xu, D. Xue, J. Crystal Growth 310 (2008) 1385–1390.
[5] J. Liu, D. Xue, Adv. Mater. 20 (2008) 2262-2267.
[6] J. Liu, H. Xia, D Xue, L. Lu, J. Am. Chem. Soc. 131 (2009) 12086-12087.

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P-201

PosterChemical Bonding Characteristics and Structural
Formability of Perovskite Compounds
Na Li, Dongfeng Xue*
Department of Materials Science and Chemical Engineering, School of Chemical
Engineering, Dalian University of Technology, 158 Zhongshan Road, Dalian 116012,
China (dfxue@chem.dlut.edu.cn)

The crystallographic structure of perovskite compounds has long been a hot topic that attracts
much attention in the materials science community, particularly, quantitative studies ofperovskite structures may lead to the findings of novel functional materials, and can further
enhance various performances especially relevant to ferroelectricity, superconductivity,
catalysis, colossal magnetoresistance and so on. Even numerous theoretical models have been
proposed, the accurate prediction of perovskite structures still remains many challenges inboth fundamental and applied aspects. With the aid of advanced computer techniques, we may
develop some useful theoretical models or methods to effectively analyze and tentatively
predict perovskite structures, which may combine the geometric configurations with thechemical bonding characteristics of constituent elements. In this chapter, we review recent
theoretical studies of perovskite materials and structures, and their applications to predict newcompounds. In particular, we introduce some new advances on the chemical bonding method
and artificial neural networks modeling method in predicting the structural stability andformability of ABO3-type perovskites, and identify some opportunities for continued researchand specific areas where significant advancement are highly demanded.

P-202

Structural basis of nucleotide exchange and clientsbinding by a novel hsp70-cochaperone bag2
Zhen Xu, Richard C Page, Saurav Misra
The Cleveland Clinic Foundation,9500 Euclid Ave, Cleveland, Ohio 44195 USA(misras@ccf.org)

Molecular chaperones such as Hsp70 are required to assist most proteins to fold into precise
three-dimensional conformations and to fulfill their biological functions. The relatively
recently identified chaperone-associated ubiquitin ligase CHIP (C-terminus of Hsp70
interacting protein) can alter chaperone activity from protein folding to protein degradation. In
contrast, the co-chaperone Bag2, which has previously been classified as a member of the Bag
domain family of Hsp70 nucleotide exchange factor (NEF), carries out nucleotide exchange,
substrate binding, and inhibition of CHIP-mediated protein degradation. Here we report thestructural basis of Bag2 function. The free and Hsp70-bound crystal structures of the so-called
BNB domain of Bag2 show that Bag2 is structurally distinct from other known Bag family of
Hsp70 NEFs. NMR-based mapping demonstrates that the Bag2 substrate binding sites overlap
with the Hsp70 interaction sites, suggesting that Hsp70 may directly displaces substrates from
Bag2 onto its own substrate binding domain. Preliminary data suggests that a novel
interaction between Bag2 and ubiquitin plays a role in Bag2-mediated inhibition of CHIP.
Our structural data begin to elucidate how Hsp70, CHIP and Bag2 coordinate with each otherto regulate the fate of unfolded proteins.
- 260 -

AsCA’09

Poster

Structure of st0929, a putative glycosyl transferase
from Sulfolobus tokodaii

P-203

Charles B.C. Cieloa, Seiji Okazakia, Tatsuo Hikageb, Atsuo Suzukia, Tsunehiro
Mizushimaa, Ryoji Masuic, Seiki Kuramitsuc, Takashi Yamane *aaDepartment of Biotechnology, Graduate School of Engineering, Nagoya University,
Nagoya 464-8603, Japan (yamane@nubio.nagoya-u.ac.jp)
bHigh Intensity X-ray Laboratory, Nagoya University, Nagoya 464-8603, Japan
cDepartment of Biological Sciences, Graduate School of Science, Osaka University,
Osaka 560-0043, Japan

Trehalose (α-D-glucopyranosyl α-D-glucopyranoside), is a naturally occurring, non-reducing
disaccharide used industrially as a food additive, artificial sweetener, and chemical stabilizer
for cosmetics and pharmaceuticals. A novel two-enzyme system was reported for the efficient
production of trehalose from starch.1) This enzyme system involves the sequential action of
maltooligosyl trehalose synthase (MTSase, EC: 5.4.99.15) and maltooligosyl trehalosehydrolase (MTHase, EC 3.2.1.141). MTSase catalyzes the conversion of the maltose
α-1,4-glucosidic bond into the trehalose α-1,1-glucosidic bond.
The 704-residue hypothetical glycosyl transferase, st0929, was recently isolated from
Sulfolobus tokodaii. In order to elucidate its function, the structure of st0929 was determinedat 1.9 Å resolution utilizing the molecular replacement method. Sulfolobus acidocaldarius
maltooligosyl trehalose synthase2) (SaMTSase), which has 52% sequence identity with st0929,
was used as a search template. The overall structure of st0929 is essentially identical to that of
SaMTSase. Likewise, the st0929 putative active site contains highly conserved residues thatcomprise the MTSase active site, including the catalytic triad and various subsites. It was ofparticular interest to note that the subsite +1 architecture of the putative active site is
essentially identical to the unique subsite +1 architecture found in SaMTSase. The st0929
putative subsite +1 is formed by a cluster of tyrosine residues reported to be required for
efficient glycosyl transferase activity. It also has sufficient dimensions to enclose the reducing
end of a putative oligosaccharide substrate. We therefore propose that st0929 also plays a rolein the synthesis of trehalose on the basis of the close sequence and structural resemblance
between st0929 and SaMTSase.
References
1.
2.

Kubota, M., Sawatani, I., Oku, K., Takeuchi, K. and Murai, S. (2004). J.Appl. Glyosci. 51, 63-70.
Kobayashi M., Kubota, M. and Matsuura, Y. (2003). J. Appl. Glycosci. 50, 1-8.

- 261 -

AsCA’09

P-204

Poster

Dimerization is important for the GTPase activity ofchloroplast translocon components atToc33 andpsToc159
Yi-Hung Yeh1, Muppuru M. Kesavulu1, Hsou-min Li1, Shu-Zon Wu1, Yuh-Ju Sun2,
Emadeldin H.E Konozy1 and Chwan-Deng Hsiao1
1Institute of Molecule biology, Academia Sinica, Taipei, Taiwan 115,
2
Institute of Bioinformatics and Structural Biology, National Tsing Hua University,
Hsinchu, Taiwan 300,

Arabidopsis Toc33 (atToc33) is a GTPase and a member of the Toc (translocon at theouter-envelope membrane of chloroplasts) complex that associates with precursor proteinsduring protein import into chloroplasts. By inference from the crystal structure of psToc34, a
homologue in pea, the arginine at residue 130 (Arg130) has been implicated in formation of
the atToc33 dimer and inter-molecular GTPase activation within the dimer. Here we report the
crystal structure at 3.2 Å resolution of an atToc33 mutant, atToc33(R130A), in which Arg130
was mutated to alanine. Both in solution and in crystals, atToc33(R130A) was present in its
monomeric form. In contrast, both wild-type atToc33 and another pea Toc GTPase homologue,
pea Toc159 (psToc159), were able to form dimers in solution. Dimeric atToc33 and psToc159
had significantly higher GTPase activity than monomeric atToc33, psToc159 andatToc33(R130A). Molecular modeling using the structures of psToc34 and atToc33(R130A)
suggests that, in an architectural dimer of atToc33, Arg130 from one monomer interacts withthe β-phosphate of GDP and several other amino acids of the other monomer. These results
indicate that Arg130 is critical for dimer formation, which is itself important for GTPase
activity. Activation of GTPase activity by dimer formation is likely to be a criticalregulatory step in protein import into chloroplasts.

Synthesis, Structure and Properties of Ba8Au5Ge40

P-205

Hui Zhang*1,2, Walter Schelle1, Michael Baitinger1, Mei-Bo Tang2, Zhen-Yong
Man2, Hao-Hong Chen2, Xin-Xin Yang2, Jing-Tai Zhao2, Yuri Grin1
1
Max-Planck-Institute for Chemical Physics of Solids, Nöthnitzer str. 40, 01187
Dresden, Germany, (huizhang@cpfs.mpg.de)2
Key Laboratory of Transparent Opto-Functional Inorganic Materials, Chinese
Academy of Sciences (Shanghai Institute of Ceramics), 1295 Dingxi Road Shanghai,
200050, China.

Ba8Au5Ge40 is prepared by reaction of BaGe, Au and Ge by induction furnace in an Ar filled
glove box and plate cooling. Its composition, crystal structure and physical properties areinvestigated. Rietveld refinement revealed Ba8Au5Ge40 crystallized in Clathrate I-type
structure (Fig.left) with unit cell parameter a = 10.8004(1) Å. The profile reliable (R) factors
are R = 2.76, Rw = 4.72, Rex = 2.34, chi2 = 4.07, respectively. The refined XRD pattern of
Ba8Au5Ge40 is given in Fig. right. The low temperature heat capacity, magnetic properties andthermoelectric properties will be discussed.

- 262 -

AsCA’09

PosterThe crystal structure (left) and refined XRD pattern (right) of Ba8Au5Ge40

Purification, crystallization and preliminary X-ray
diffraction analysis of human THRSP

P-206

Wenzheng Zhang1,Wei Peng2,Weihong Zhou1, Mark Bartlam1, Zonghao Zeng2 andZihe Rao1,2,3
1College of Life Sciences and Tianjin State Laboratory of Protein Sciences, Nankai
University, Tianjin 300071, China (zhangwzh@nankai.edu.cn)
2
National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese
Academy of Sciences, Beijing 100101, China
3
Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China(raozh@@nankai.edu.cn)

THRSP（Spot 14，S14) is a small (about 17 kDa) acidic (pI 4.68) nuclear protein with nosequence similarity to other functional motifs. It initially came to attention in 1982 through its
marked and rapid induction by thyroid hormone. The S14 gene encodes a protein that is
predominantly expressed in lipogenic tissues, such as the liver, white and brown adipose
tissues and the lactating mammary glands, where its expression is rapidly regulated byhormones and dietary constituents. It recently showed that S14 acts at the transcriptional levelin the transduction of signals for increased expression of genes encoding lipogenic
enzymes.These result suggest that the THRSP is a transcriptional fator of the lipogenic
enzymes and could function in the regulation of lipid synthesis.
In humans, the S14 locus resides in the chromosome region 11q13, which is frequently
amplified in breast tumours, and as a result, it has been suggested that this protein could playa role in the metabolism and growth of these kinds of tumours. The S14 gene is amplified insome breast cancers and is strongly expressed in most. Thus, S14 is a marker for aggressive
breast cancer and a potential target as well. Future effort will center on validation of S14 as atherapeutic target and producing antagonists of its action.
Now, we have finished the purification, crystallization and preliminary X-ray diffraction
analysis of human THRSP. This result has established a good foundation for the study ofstructure and function of human THRSP.

- 263 -

AsCA’09

Poster

Structure of main protease from a global infectious
human coronavirus, HCoV-HKU1

P-207

Qi Zhao1, Shuang Li1, Fei Xue1, Yilong Zou1, Cheng Chen1, Mark Bartlam1,2 &Zihe Rao1,2,3
1 Tsinghua-Nankai-IBP Joint Research Group for Structural Biology, Tsinghua
University, Beijing 100084, China.
2 College of Life Sciences, Nankai University, Tianjin 300071, China.
3 National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese
Academy of Sciences, Beijing 100101, China.

Human coronavirus HKU1 (HCoV-HKU1) is a new coronavirus that was first identified in
Hong Kong in 2005. Infection by HCoV-HKU1 occurs worldwide and causes syndromes suchas common cold, bronchitis and pneumonia. The coronavirus main protease (Mpro), which isa key enzyme in viral replication via a cascade of proteolytic processing of replicase
polyproteins, has been recognized as an attractive target for rational drug design. In this study,
we report the structure of HCoV-HKU1 Mpro in complex with a Michael acceptor based
inhibitor N3. The structure of HCoV-HKU1 serves as a high quality model for group 2A
coronaviruses, which differ from group 2B coronaviruses such as SARS-CoV. The structure
together with activity assays supports the relative conservation at the P1 position discoveredin genome sequencing. Combined with structural data from other Mpros, this Structure
provides insights into both substrate preference and antiviral-design against coronaviruses.
Reference
Zhao, Q., S. Li, F. Xue, Y. Zou, C. Chen, M. Bartlam, and Z. Rao. 2008. Structure of the main proteasefrom a global infectious human coronavirus, HCoV-HKU1. J Virol.

Expression，Purification, Crystallization andPreliminary X-ray Analysis of Cytochrome P450
153C1 from Novosphingobium aromaticivorans
DSM12444

P-208

Weihong Zhou1, Wen Yang1, Stephen G. Bell4, Mark Bartlam1, Luet-Lok Wong4 andZihe Rao1,2,3
1College of Life Sciences and Tianjin State Laboratory of Protein Sciences, Nankai
University, Tianjin 300071, China (zhouwh@nankai.edu.cn)
2
National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese
Academy of Sciences, Beijing 100101, China
3
Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China
4
Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory,
South Parks Road, Oxford OX1 3QR, UK

Cytochrome P450 enzymes constitute a large family of hemoproteins that catalyze themonooxygenation of a great variety of endogenous and exogenous organic compounds. They
have been found throughout the biosphere from bacteria to higher plants and animals andparticipate in the biosynthesis of physiologically important compounds such as steroids andhormones, in fatty acid oxidation as well as detoxification of exogenous compounds from theenvironment. They play an important role in medicine, agriculture, detection and protection ofenvironment, chemosynthesis and so on.
- 264 -

AsCA’09

PosterNovosphingobium aromaticivorans DSM12444 (Novosphingobium aromaticivorans F199) isa gram-negative bacte-rium which is known to degrade a range of hydrocarbons. The
bacterium contains a high proportion of genes encoding proteins involved in the
catabolism and transport of aromatic compounds including many oxygenase enzymes.
CYP153C1 from Novosphingobium aromaticivorans DSM12444 was observed to bindseveral substrates, especially linear alkanes, such as heptane, octane and nonane which arehighly pollution to the environment. CYP 153C1 has potential biotechnological applications
such as the degradation of linear alkanes compounds. The three-dimensional structure will
provide valuable information on substrate binding and electron transfer，and structure basis
for its application in protein engineering.
The recombinant CYP153C1 was highly expressed in Escherichia coli and purified;well-diffracting crystals were obtained by the hanging-drop vapor diffusion method. Crystals
suitable for X-ray crystallography have been obtained and diffraction data were collectedin-house to 2.7 Å resolution from a single crystal. The crystals belong to the space group
P321 with unit-cell parameters a =86.2 Å, b =86.2 Å, c =123.9 Å. The structure determinationand substrates soaking are on the way.
References
1. Nelson, D. R. Mining database for cytochrome P450 genes. Methods Enzymol. 2002, 357, 3-15
2. Mansuy, D.; Renaud J. –p., Heme-thiolate proteins different from cytochrome P450 catalyzingmonoxygenations. in Cytochrome P450 Structure, Mechanmism and Biochemistry Ortiz de Montellano,
P. R. ed Plenum Press: New York and London, 1995; pp. 537-574
3. Stephen G. Bell, Luet-Lok Wong, P450 enzymes from the bacterium Novosphingobium
aromaticivorans BBRC， 2007，360，666-672- 265 -

Author Index

AsCA’09

Index

Dominique Bourgeois.................................................... 53
U. Burkhardt .................................................................. 59

Ａ

Laure Bourgeois ............................................................ 60
Anindita Biswas ............................................................. 73

Dean R. Artis .................................................................. 18

Stuart Bloor ................................................................... 73

Shinobu Aoyagi ........................................................ 34, 70

Richard Bunker .............................................................. 74

Shin‐ichi Adachi ............................................................. 53

Wei Bao ......................................................................... 76

Motoyasu Adachi ........................................................... 54

Stuart R. Batten ............................................................. 86

Hapipah Mohd Ali.......................................................... 64

R. K. Bedi ....................................................................... 91

A. M. Abdullah ............................................................... 69

Erik Brostromer ............................................................. 97

Masato Akutsu............................................................... 73

Gary D. Brayer ............................................................. 116

Satoko Akashi ................................................................ 74

Rui Bao ........................................................................ 121

Nobuyuki Abe ................................................................ 76

Hans Peter Bächinger .................................................. 123

Taka‐hisa Arima ..................................................... 76, 200

Xiaoyun Bai ................................................................. 123

Takahisa Arima .............................................................. 83

Gerard Bricogne .......................................................... 132

Patryck K. K. Allen .......................................................... 85

Michela Bollati ............................................................ 132

Shannon Wing Ngor AU................................................. 97

Randy Bledsoe............................................................. 136

Intekhab Alam ....................................................... 99, 115

William Burkhart ......................................................... 136

Yasuhisa Asano .................................................... 100, 126

Mark Bartlam ................................ 140,147, 151, 262, 263

Naoya Akao ................................................................. 134

Lin Bai.......................................................................... 142

Joo Chuan Ang ............................................................. 138

Mohan M. Bhadbhade ................................................ 155

Masahide Aoki ............................................................. 154

Roger Bishop ............................................................... 155

Junji Akimoto ............................................................... 165

Horst Borrmann .......................................................... 175

Yuki Azuma .................................................................. 166

Günter Blobel .............................................................. 182

G N AnilKumar ............................................................. 168

Nada Bosnjaković‐Pavlović .......................................... 185

Janice Aber .................................................................. 186

Marianna Biadene ....................................................... 203

Takashi Asano .............................................................. 190

Matt Benning .............................................................. 203

Natsuki Amanokura ............................................. 192, 251

Gary M. Battle ............................................................. 220

Toru Asaka ................................................................... 200

Sampa Biswas.............................................................. 221

D. S. Adipranoto........................................................... 206

John Berrisford ............................................................ 247

Kazuya Aizawa ............................................................. 206

Michael Baitinger ........................................................ 261

Hiroaki Adachi ............................................................. 212

Stephen G. Bell............................................................ 263

Maxim Avdeev ............................................................. 220
S.Anandhi .................................................................... 227

Ｃ

Ｂ

Jijie Chai ........................................................................ 15
Hanna Cho..................................................................... 18

Edward N. Baker ........................................................ 2, 88

Ivana Cheung ................................................................ 18

Gideon Bollag ................................................................ 18

John Cantwell ................................................................ 18

Ryan Bremer .................................................................. 18

Chi‐Ming CHE ................................................................ 19

Ricardo A. Bernal ........................................................... 43

Stephen Sin‐Yin, CHUI ................................................... 19

P.D. Butler ...................................................................... 49

Dongfeng Chen.............................................................. 22- 266 -

AsCA’09

Index

Chien‐Hung Chang ......................................................... 49

Chun‐Lung Choi ........................................................... 157

Je‐Wei Chang ................................................................. 49

M.Y. Chern ................................................................... 171

Wei‐Tsung Chuang ......................................................... 49

Wenyan Chen .............................................................. 176

Yi‐Jiun Chen ................................................................... 49

Deepak Chopra............................................................ 195

Zia‐Fung Chang.............................................................. 49

S.‐Y. Chen ..................................................................... 204

Weiyu Cao ..................................................................... 50

Y.‐Y. Chang ................................................................... 204

Jacques‐Philippe Colletier ............................................. 53

C.‐H. Chu ............................................................. 204, 222

Chongyun Cheng ....................................... 56, 89, 92, 256

S.‐L. Chang ........................................................... 204, 222

H.H. Chen ...................................................................... 59

William Clegg .............................................................. 205

Hao‐Hong Chen ..................................... 62, 156, 163, 261

Leonard M.G. Chavas .................................................. 215

Xiaolong Chen ....................................................... 68, 236

Debi Choudhury .......................................................... 221

Yuh Min Chook .............................................................. 73

H.‐Y. Chen .................................................................... 222

Elaine Chiu ..................................................................... 74

L.‐S. Cai ........................................................................ 222

Fu‐Rong Chen ................................................................ 79

Alessandro T. Caputo................................................... 223

Kittipong Chainok .......................................................... 86

Hyun‐Soo Cho ............................................................. 223

Yu‐Chun Chuang ............................................................ 87

Oliver B. Clarke ............................................................ 223

Ming‐Hung Chu ............................................................. 98

Zhongli Cui .................................................................. 224

Yi‐Wei Chang ................................................................. 98

Jongkyu Cheon ............................................................ 234

Yi‐Sheng Cheng ...................................................... 98, 257

Rong Cao ..................................................................... 240

Chen‐Hsi Chu ................................................................. 99

Shao‐Wen Chou .......................................................... 252

Chin‐Yi Chen .................................................................. 99

Cheng Chen ................................................................. 263

Ki Joon Cho ............................................................ 99, 115
Charles B.C. Cielo ................................................. 100, 260

ＤAngela R. Criswell ........................................................ 101
Jungwoo Choe ............................................................. 102
Leonard Chavas ........................................................... 104

Paul J. Dyson ................................................................. 15

LiQing Chen ......................................................... 107, 149

Karl Dawson .................................................................. 19

Yuxing Chen ......................................................... 108, 121

Jingqi Duan .................................................................... 30

Yun‐Seok Choi.............................................................. 108

Mhairi Donohoe ............................................................ 43

Yunje Cho ............................................................ 110, 128

Gautam R. Desiraju ....................................................... 46

Shan‐Ho Chou...............................118, 130, 145, 174, 222

Miao Du ........................................................................ 47

Ko‐Hsin Chin ........................................ 118, 130, 174, 222

Wei Ding .................................................................57, 205

Nei‐Li Chan .................................................................. 119

Ivan Dikic ....................................................................... 73

Wei‐Ti Chen ................................................................. 121

Xiuhua Dong .................................................................. 73

Jeong Ho Chang ........................................................... 128

Roman Dronyak ............................................................. 79

Kun‐Wei Chan .............................................................. 131

Mohammad Dadashipour ........................................... 100

Yu Wai Chen ................................................................ 139

Lyudmila G. Doudeva ................................... 113, 137, 146

Hong Cui ...................................................................... 143

Kesheng Dai................................................................. 117

Shoudeng Chen ........................................................... 151

Nyssa Drinkwater ........................................................ 122

Yutao Chen .................................................................. 151

Jianping Ding ....................................................... 136, 139

Isa Y. H. Chan ............................................................... 155

Aiping Dong................................................................. 143

Christine Cardin ........................................................... 156

Prabal Dasgupta .......................................................... 158

Howard Colquhoun ..................................................... 156

Erik W. Debler ............................................................. 182

Qigao Cao .................................................................... 156

S. Dudziak .................................................................... 183- 267 -

AsCA’09

Index

J. K. Dattagupta ........................................................... 221

Taishi Goto .................................................................... 67

Christine M. Dunham .................................................. 226

Hongmei Gu .................................................................. 73
Ang Gao ........................................................................ 92
Shunji Goto ................................................................. 105

E

Gwang Hyeon Gwon.................................................... 110
Pontus Gourdon .......................................................... 119

Alison Edwards .............................................................. 39

Gary Grunewald .......................................................... 122

Olga Esteban .................................................................. 43

Shihui Guo................................................................... 129

H. Eisaki ......................................................................... 75

Shuyuan Guo ............................................................... 140

Aled Edwards ............................................................... 143

Yong Gong ................................................................... 142

Elena Evdokimova ....................................................... 143

Masaki Gouda ............................................................. 147
Yu Guo ................................................................. 151, 251
Yu Gan ......................................................................... 156

Ｆ

K.V.Arjuna Gowda........................................................ 158
Ramakrishna Gowda ................................................... 158

Yoshinori Fujiyoshi ..................................................... 6, 42

Yuri Grin .............................................................. 175, 261

Daniel Fong.................................................................... 18

T. M. Gesing................................................................. 183

Didier Fournier .............................................................. 53

Bruce Garetz ............................................................... 186

Joseph D. Ferrara ........................................................... 55

Zoltan Gal .................................................................... 188

Mamoru Fukunaga .................................................. 76, 77

Nour Eddine Ghermani ............................................... 210

Arno Fey ........................................................................ 77

Jacqueline M. Gulbis ................................................... 223

Yingang Feng ............................................................... 101

Chun‐Li Guo ................................................................ 225

Tomomi Fujii ................................................................ 102

Yong‐Gui Gao .............................................................. 226

Yukito Furukawa .................................................. 105, 209

R.Gopalakrishnan ........................................................ 227

Satoshi Fujii ................................................................. 134

Celine Gelinas.............................................................. 229

Yu Hang Fong ............................................................... 139

Rongjin Guan............................................................... 229

Shirou Fanahashi ......................................................... 189

S. Gourinath ................................................................ 229

Qi Fang ........................................................................ 225

Ye Gao ......................................................................... 245

Taro Fujita .................................................................... 246

Ｈ
Ｇ
Eran Hodis ....................................................................... 8
Sam Gillette ................................................................... 18

Gaston Habets ............................................................... 18

Richard F. Garrett..................................................... 26, 51

Meenhard Herlyn .......................................................... 18

J. Graf .................................................................... 40, 213

Nikolas K. Haass ............................................................ 18

Xiang Gao ...................................................................... 41

Peter Hirth .................................................................... 18

Colin R. Groom .............................................................. 48

Jeff Hurd ........................................................................ 19

Peter T. A. Galek ............................................................ 48

Linna Huang .................................................................. 20

Elliot P. Gilbert ............................................................... 51

Jianhua He............................................................. 23, 149

Y.Grin ............................................................................. 59

Guido Hansen.........................................................27, 132

Kai Guo .......................................................................... 62

Tim R. Hercus ................................................................ 27

Xiangxin Guo ......................................................... 62, 156

J.A.K. Howard ................................................................ 32

Hermann Gies ................................................................ 66

Ryuta Hirohata .............................................................. 38- 268 -

AsCA’09

Index

B. Hasse ................................................................. 40, 213

Shota Hasegawa .......................................................... 164

F. Hertlein ...................................................................... 40

Hiroshi Hayakawa ........................................................ 165

W.A. Hamilton ............................................................... 49

Chibon Hyon ............................................................... 170

Yu‐Shan Huang .............................................................. 49

Xiaozhen Hua .............................................................. 172

Makoto Hanesaka .......................................................... 50

André Hoelz ................................................................ 182

William A. Hamilton ...................................................... 51

Altaf Hussain ............................................................... 183

Eric Hovestreydt .................................................... 61, 203

T.Hattori ...................................................................... 187

Kenneth J. Haller ............................................... 63, 86, 91

Akinori Hoshikawa ....................................... 191, 206, 217

Hisashi Hibino ................................................................ 67

Jack W‐H.Kan............................................................... 195

A. Hussain ...................................................................... 69

Ross W Harrington ...................................................... 205

Hiroshi Hashimoto ......................................................... 74

Makoto Hayashi .......................................................... 206

Kodai Hara ..................................................................... 74

Kazuya Hasegawa ........................................................ 209

Tomo Hanafusa.............................................................. 74

Kensaku Hamada......................................................... 212

Hiraka Haruhiro ............................................................. 77

Tomokazu Hasegawa ................................................... 212

Satoru Horio .................................................................. 77

James Hester ............................................................... 220

Maiko Hamabe .............................................................. 82

C.‐J. Huang................................................................... 222

Venkatesha R. Hathwar ................................................. 87

Hua‐Chen Hu ............................................................... 230

Ton‐That Hung ............................................................... 88

Jiang Huang ................................................................. 231

Marco Hill ...................................................................... 95

Jeff E. Habel................................................................. 232

Chwan‐Deng Hsiao ........................ 98, 106, 121, 134, 261

Liwei Hung .................................................................. 232

Tatsuo Hikage ...................................................... 100, 260

Ting Hu........................................................................ 242

Sojung Han .................................................................. 102

Tanja Hedderich .......................................................... 245

Yasuo Hata ................................................................... 102

Ning Hao ..................................................................... 251

Masahiko Hiraki ................................................... 104, 215

Ming‐Tsung Hsu .......................................................... 254

Kunio Hirata ................................................................. 105
Takaaki Hikima............................................................. 105

I

Yu‐Yuan Hsiao ...................................................... 106, 146
Mingdong Huang ......................................... 107, 129, 149
Zixiang Huang .............................................................. 107

Prabha N. Ibrahim ......................................................... 18

Yong‐Xing He ....................................................... 108, 121

Simon Iremonger .......................................................... 19

Seung Kon Hong .......................................................... 109

Katsumi Imada .............................................................. 27

Nien‐Tai Hu .................................................................. 119

Bo Brummerstedt Iversen ............................................. 32

Cheng‐Yang Huang............................................... 121, 134

Naoko Imamoto ............................................................ 38

Nam‐Chul Ha ....................................... 127, 128, 144, 150

Tetsuya Ishikawa ........................................................... 38

Kwang Yeon Hwang ..................................................... 127

Y. Ishikawa ..................................................................... 39

Rolf Hilgenfeld ..................................................... 132, 152

Takashi Ida..................................................................... 67

Chwan‐Den Hsiao ........................................................ 133

Kenji Iwasaki.................................................................. 72

Mien‐Chie Hung .......................................................... 134

Fumiyo Ikeda ................................................................. 73

Annie Hassell ............................................................... 136

A. Iyo ............................................................................. 75

Haiying Hang ............................................................... 142

M. Ishikado.................................................................... 75

Hongyu Hu ................................................................... 149

S. Ishida ......................................................................... 75

Shoshi Higuchi ............................................................. 159

T. Ito .............................................................................. 75

Ichiro Hisaki ......................................................... 160, 197

Kyoko Ito‐Shinzawa ....................................................... 92

Tomoaki Hinoue .................................................. 160, 197

Noriyuki Igarashi ................................................. 104, 215- 269 -

AsCA’09

Index

Junji Inokoshi ............................................................... 131

Roger D. Kornberg ......................................................... 29

Naoko Itoda ................................................................. 161

Jungeun Kim.................................................................. 36

Sayaka Ina .................................................................... 161

Kenichi Kato .................................................................. 36

Sho Ikeda ..................................................................... 161

H. Kimura ...................................................................... 39

Susumu Ikeda .............................................................. 191

R. Kiyanagi..................................................................... 39

Kenji Iwase................................................... 191, 206, 217

S‐A. Kim......................................................................... 39

Toru Ishigaki................................................. 191, 206, 217

Michael T. Kirchner ....................................................... 46

Kohei Ishimoto ............................................................ 199

Ryota Kuroki .................................................................. 54

Fujio Izumi ................................................................... 207

Samroeng Krachodnok .................................................. 63

Tsuyoshi Inoue ............................................................. 212

Koji Kato ........................................................................ 72
David Komander............................................................ 73
Masato Kawasaki........................................................... 73

Ｊ

Ryuichi Kato .................................................................. 73
Tobias Kensche .............................................................. 73

Minghua Ju .................................................................... 30

Shunsuke Kobayashi ...................................................... 74

Ru Jia ............................................................................. 30

Toshiaki Kogame............................................................ 74

Dylan Jayatilaka ............................................................. 32

H. Kito ........................................................................... 75

Xiu‐Juan Jiang ................................................................ 47

K. Kihou ......................................................................... 75

U‐Ser Jeng ..................................................................... 49

K. M. Kojima .................................................................. 75

Fan Jiang ................................................................ 57, 205

R. Kumai ........................................................................ 75

Liangbao Jiang ............................................................... 68

Kazuhisa Kakurai............................................................ 76

Laurie Jackson ............................................................... 73

Hiroyuki Kimura ............................................... 76, 77, 233

Andrzej Joachimiak ........................................ 92, 143, 256

Ryoji Kiyanagi ......................................... 77, 206, 217, 233

Longguang Jiang .................................................. 107, 149

Hae Joo Kang ................................................................. 88

Yong‐Liang Jiang .................................................. 108, 121

Davinder Kaur ............................................................... 91

Young‐Ho Jeon ............................................................. 108

Kyung Hyun Kim .................................................... 99, 115

Woo‐Suk Jung .............................................................. 112

Hidenobu Komeda .............................................. 100, 126

Jun Young Jang ............................................ 115, 148, 233

Hideo Kitamura ........................................................... 105

Xiao Ling Jin ................................................................. 127

Yoshiaki Kawano .......................................................... 105

Hua‐Ci Jhang ................................................................ 137

Eunice EunKyeong Kim ........................................ 108, 109

Tao Jiang ...................................................................... 142

Jae‐Hong Kim .............................................................. 108

Hong Ji ......................................................................... 162

Hyoun Sook Kim ........................... 109, 111, 115, 148, 233

Teng‐Teng Jin ............................................................... 163

Kook Han Kim .............................................................. 109

Jongsoo Jeon ............................................................... 223

Soon‐Jong Kim ............................................................ 109

Ruchi Jain..................................................................... 229

Jin Seok Kim ................................................................ 110
Kyeong Kyu Kim ........................................................... 111
Kyoung Hoon Kim................................. 111, 115, 148, 233

Ｋ

Myung‐Il Kim............................................................... 112
Pan‐Hsien Kuo ............................................................. 113

Jun Kong ........................................................................ 18

Tatsuya Kawaguchi ...................................................... 123

Sung‐Hou Kim................................................................ 18

Akira R. Kinjo ............................................................... 125

Takashi Kumasaka ... 24, 105, 191, 206, 211, 217, 218, 209

Hong‐Man Kim .....................................................127, 144

Young Ki KIM ................................................................. 25

Mi‐Sun Kim ................................................................. 129

Jack King‐Scott............................................................... 27

Yuri Kusov.................................................................... 132- 270 -

AsCA’09

Index

Kosaraju Vamsi Krishna................................................ 144

Jie‐Oh Lee...................................................................... 17

Takayoshi Kinoshita ..................................................... 147

Billy Lam ........................................................................ 18

Do Jin Kim.................................... 148, 233, 109, 111, 115

Catherine Luu ................................................................ 18

Hiroyuki Kurobe ........................................................... 154

Jennifer Liu .................................................................... 18

I.A.Khazi ....................................................................... 158

John T. Lee .................................................................... 18

Kimiyoshi Kaneko ........................................................ 159

Ling Li ...................................................................... 18, 30

Takuro Kawasaki .......................................... 161, 164, 166

Kam‐Hung, LOW ............................................................ 19

Kunimitsu Kataoka ....................................... 164, 165, 243

Roy V. A. L ..................................................................... 19

Norihito Kijima ............................................................ 165

Zhuojia Lin ..................................................................... 20

Jin‐Gyu Kim.................................................................. 167

Yuntao Liu ..................................................................... 22

Youn‐Joong Kim ........................................................... 167

Gwo‐Huei Luo ............................................................... 25

M K Kokila............................................................ 168, 169

Keng S. Liang ...................................................... 25, 49, 79

S. Kumar ...................................................................... 168

Kye Hong LEE ................................................................ 25

S. S. Karki ..................................................................... 168

Angel F. Lopez ............................................................... 27

K. Chandra Kumar ........................................................ 169

Jinzhong Lin ................................................................... 30

Tsuyoshi Kumagai ........................................................ 170

Adelaine K.W. Leung ..................................................... 31

Isao Kagomiya.............................................................. 179

Jade Li ........................................................................... 31

Yuji Karakane ............................................................... 181

C‐H. Lee ......................................................................... 39

Stephan Kutik .............................................................. 182

Feiran Lu ....................................................................... 41

J. Kawamura ................................................................ 187

Xiaodan Li ...................................................................... 42

O. Kamishima .............................................................. 187

Lawrence K. Lee ............................................................ 43

Masami Kaneko ........................................................... 192

Chin‐Yen Liu .................................................................. 49

Naoki Koyasu ............................................................... 199

Din‐Goa Liu ................................................................... 49

Koji Kimoto .................................................................. 200

Kuei‐Fen Liao................................................................. 49

Yoshio Kaneko.............................................................. 200

Ming‐Tao Lee ........................................................ 49, 207

Brendan J. Kennedy ..................................................... 201

Ying‐Huang Lai .............................................................. 49

Tomoya Kitatani ........................................................... 212

Zhi‐Jie Liu ............................. 56, 89, 92, 96, 101, 126, 256

Eugkweon Kim ............................................................. 223

Kong Mun Lo ................................................................. 64

Jongsun Kim ................................................................ 223

See Mun Lee ................................................................. 64

Kuglae Kim................................................................... 223

Jianhua Lin .................................................................... 66

Ann C. Kelley................................................................ 226

Hui LI ..................................................................... 68, 236

Shivesh Kumar ............................................................. 229

Jeffrey W. Lynn ............................................................. 71

Fang Kong .................................................................... 242

Wen‐Hsien Li ................................................................. 71

akuro Kawasaki ............................................................ 243

C. H. Lee ........................................................................ 75

Poomani Kumaradhas.................................................. 249

Gene‐Hsiang Lee ........................................................... 87

Yi‐Ching Ko .................................................................. 252

Yang Li ................................................ 89, 92, 96, 101, 256

Seiki Kuramitsu ............................................................ 260

Lei Li .............................................................................. 96

Emadeldin H.E Konozy ................................................. 261

Kwok Ho LAM ................................................................ 97

Muppuru M. Kesavulu ................................................. 261

Lan‐Fen Li .............................................................. 97, 137
Thomas King Wah LING ................................................. 97
Kai‐Lun Liu ..................................................................... 98

ＬJi‐Hye Lee .............................................................. 99, 115
Pierre LeMagueres ...................................................... 101
Yu‐Hua Lo ............................................................ 106, 121

Yingfang Liu ........................................................... 16, 151- 271 -

AsCA’09

Index

Jae‐Jin Lee ................................................................... 108

Shi‐Xiong Liu................................................................ 239

Kong‐Joo Lee ............................................................... 108

Tian‐Fu Liu ................................................................... 240

Ming Luo ............................................................. 108, 123

Hartmut Luecke .......................................................... 241

Sang Jae Lee ................................ 109, 111, 115, 148, 233

Su Woong Lee ............................................................. 244

Sangho Lee .................................................................. 111

Portia G Loh ................................................................ 248

Michael C. Lawrence ................................................... 114

Chien‐Chih Lin ............................................................. 252

Chunmin Li .................................................................. 116

Jiaying Lou ........................................................... 254, 255

Guoming Li .......................................................... 117, 123

Jong‐Yih Lin ................................................................. 254

Yazhuo Li ..................................................................... 117

Peng Li ................................................................. 254, 255

Shu‐Ju Liao .................................................................. 118

Sheng‐Wen Liu ............................................................ 254

Li‐Ying Lin .................................................................... 119

Yaw‐Kuen Li................................................................. 254

Xiangyu Liu .................................................................. 119

Mao‐Sen Liu ................................................................ 257

Yong Liu ....................................................................... 123

Tsan‐Piao Lin ............................................................... 257

Mieszko Lis .................................................................. 125

Na Li ............................................................................ 259

Kangseok Lee ....................................................... 127, 144

Hsou‐min Li ................................................................. 261

Jihye Lee ...................................................................... 128

Shuang Li ..................................................................... 263

Andrea C. LeBlanc........................................................ 137
Carmay Lim.................................................................. 137

Ｍ

Xiang Liu ...................................................................... 137
Jhih‐Min Lin ................................................................. 138
Wei Lin ........................................................................ 139

Eric Martz ........................................................................ 8

Seow Yi Lim ................................................................. 144

John Moult ...................................................................... 8

Yunhai Luo ................................................................... 147

Thomas C. W. Mak ........................................................ 14

Jian Li ........................................................................... 149

Adhirai Marimuthu ....................................................... 18

Shuaiyi Liang ................................................................ 151

Shumeye Mamo ............................................................ 18

Xuemei Li ............................................................. 151, 251

Russell E. Morris ............................................................ 20

Zhiyong Lou ......................................................... 151, 251

C. John McAdam ........................................................... 21

M. Gerry J. Lesley ........................................................ 157

P. Munshi....................................................................... 32

Sung‐Woo Lee ............................................................. 167

Eiichiro Matsubara ........................................................ 38

Chih‐Hao Lee ............................................................... 171

Kazuhiro Maeshima....................................................... 38

K.S. Laing ..................................................................... 171

M‐K. Moon .................................................................... 39

Duosheng Li ................................................................. 172

C.Michaelsen......................................................... 40, 213

Li Hui............................................................................ 173

Mike Merrick ................................................................. 42

Li Jia‐Ju ........................................................................ 173

Shoji Maeda .................................................................. 42

Tso‐Ning Li ................................................................... 174

Todd B. Marder ............................................................. 44

Ying Liang .................................................................... 175

Yushi Matsumoto .......................................................... 44

Gousheng Liu ............................................................... 176

Hiroyasu Masunaga ....................................................... 50

Xinchun Liu .................................................................. 176

Z.Y. Man ......................................................................... 59

Matthew Lundy ........................................................... 196

Barry C. Muddle ............................................................ 60

Weidong Liu ................................................................ 224

Zhen‐Yong Man ..................................................... 62, 261

Chang‐Hee Lee ............................................................ 234

Peter Metcalf ................................................................ 74

Wei Lee Leong ............................................................. 235

Yoshiki Murakumo ........................................................ 74

Jiaju LI .......................................................................... 236

K. Miyazawa .................................................................. 75

Tonglei Li ..................................................................... 238

Kaoru Mitsuoka ............................................................. 80- 272 -

AsCA’09

Index

Daisuke Morikawa ......................................................... 83

Koichi Momma ............................................................ 207

Keith S. Murray .............................................................. 86

Hiroyoshi Matsumura ................................................. 212

Mohammad Hedayetullah Mir ...................................... 90

Satoshi Murakami ....................................................... 212

Kazumasa Muramoto .................................................... 92

Yusuke Mori ................................................................ 212

Kazunori Maeda ............................................................ 92

Guy Montelione .......................................................... 229

Masao Mochizuki .......................................................... 92

Myungkook Moon ....................................................... 234

Tsunehiro Mizushima .......................................... 100, 260

Hartmut Michel ........................................................... 245

Hyunjin Moon.............................................................. 102

Marco Marcia .............................................................. 245

Naohiro Matsugaki .............................................. 104, 215

Masami Kaneko ........................................................... 251

Edward J.Meehan ........................................................ 107

Saurav Misra ............................................................... 259

Xiao‐Xiao Ma ....................................................... 108, 121

Ryoji Masui .................................................................. 260

John G. Menting .......................................................... 114
Cristina de Matteis ...................................................... 117

Ｎ

Geng Meng .......................................................... 117, 123
Jennifer L Martin ......................................................... 122
Michael McLeish.......................................................... 122

Hoa Nguyen .................................................................. 18

Kazunori Mizuno.......................................................... 123

Kiyoshi Nagai ................................................................. 31

Keita Miyama............................................................... 123

Eiji Nishibori ............................................................ 34, 70

Koichi Masakiyo ........................................................... 123

Yoshinori Nishino .......................................................... 38

Tatsuya Morimoto ....................................................... 123

Y. Noda .......................................................................... 39

Jeroen R. Mesters ........................................................ 132

So Nakagawa ................................................................. 42

Wei Mi ......................................................................... 137

Shingo Nagano .............................................................. 44

Jun Ma ......................................................................... 139

Mangayarkarasi Nagarathinam ..................................... 60

Masahiro Morita.......................................................... 147

Philip N.H. Nakashima ................................................... 60

Nao Miyano ................................................................. 147

M. Nakajima .................................................................. 75

Ming Ma .............................................................. 151, 251

Yukio Noda ....................................................... 76, 77, 233

Bholanath Mondal ....................................................... 158

Jie Nan........................................................................... 97

Daiju Matsumura ......................................................... 159

Atsushi Nisawa ............................................................ 105

Jun'iciro Mizuki ............................................................ 159

Poul Nissen.................................................................. 119

Mikiji Miyata........................................................ 160, 197

Haruki Nakamura ........................................................ 125

Krishnaiah . M.............................................................. 169

Ki Hyun Nam ............................................................... 127

S. Mohan ..................................................................... 169

Tetsuko Nakaniwa ....................................................... 147

Takashi Miyamoto ....................................................... 177

Yasuo Nishihata ........................................................... 159

Jin Mizuguchi ............................................... 178, 180, 184

Thanh‐ha Nguyen ......................................... 179, 188, 195

Yingli Ma ...................................................................... 182

Yuki Nakai .................................................................... 181

O. Meier ...................................................................... 183

Munehiko Nakatsuma ......................................... 188, 243

David Miret .................................................................. 186

Kimihiko Nozaki........................................................... 194

Takahiro Morishima ............................. 191, 206, 217, 218

Atsushi Nakagawa ....................................................... 209

Takashi Muroya ........................................... 191, 211, 218

Do Young Noh ............................................................. 244

Masaaki Matsumoto.................................................... 197

Mihail Nazarov ............................................................ 244

Yuji Mizobe .................................................................. 197

Vijayan Narayayanasamy ............................................ 249

Jiang‐Gao Mao..................................................... 198, 242
Yoshio Matsu ............................................................... 200
Kazuhiro Mori ...................................................... 206, 217- 273 -

AsCA’09

Index
Joon Kyu Park .............................................................. 108

Ｏ

HyeJin Park .................................................................. 111
Sun‐Hee Park............................................................... 127

David Owen ................................................................... 12

Shunfu Piao ................................................................. 128

Atsunori Oshima ............................................................ 42

Young Bong Park ......................................................... 128

Yukihiro Ozaki ........................................................ 52, 190

Derek Parks ................................................................. 136

Holger Ott .............................................................. 61, 203

Yingjie Peng ................................................................. 136

Haruo Ohmori ............................................................... 74

Puttaraja.............................................................. 168, 169

Shintaro Ohtani ............................................................. 83

Vedavathi G.Puranik .................................................... 169

Tadao Oikawa .............................................................. 102

Teguh Panca Putra ............................................... 191, 218Haruhiko Ohashi .......................................................... 105

Teguh Panca ................................................................ 217

Kenji Okuyama............................................................. 123

Guohong Peng............................................................. 245

Songying Ouyang ......................................................... 126

Son Van Phung ............................................................ 246

Seiji Okazaki ......................................................... 126, 260

Richard C Page ............................................................ 259

Satoshi Omura ............................................................. 131

Wei Peng ..................................................................... 262

Toru Ohata ........................................................... 105, 209
Ken‐ichi Ohshima ......... 161, 164, 165, 166, 188, 243, 246

Ｒ

Koji Okada ........................................................... 179, 189
Yusuke Oji .................................................................... 190
Ryoko Oishi .......................................... 191, 206, 217, 218

M.J. Rosseinsky ............................................................. 10

Hidetoshi Oguro .................................................. 206, 217

Zihe Rao ................... 16, 56, 140, 147, 151, 251, 262, 263

Noboru OHTA .............................................................. 214

Julie Rice ....................................................................... 18

Kenji Ohoyama ............................................................ 233

Brian H. Robinson ......................................................... 21
T. N. Guru Row ........................................................ 33, 87
C. Malla Reddy .............................................................. 46

Ｐ

Michael Ruf ........................................................... 61, 203
Felix Randow ................................................................. 73

Hongkun Park .................................................................. 4

Rita Martinez ................................................................ 73

Jaime Prilusky .................................................................. 8

Simin Rahighi ................................................................ 73

Lorien J. Parker .............................................................. 15

A. David Rae .................................................................. 86

Michael W. Parker ................................................... 15, 27

Evan G. Robertson ........................................................ 91

Ben Powell ..................................................................... 18

Kyoung‐Seok Ryu ........................................................ 108

Pokka K‐C. Pang ..................................................... 22, 195

Sangkee Rhee .............................................................. 112

Jin Peng ......................................................................... 30

Brian P. Rempel ........................................................... 116

Andrew G. Peele ............................................................ 36

Robert Reid ................................................................. 136

Ross Piltz ....................................................................... 39

Warren Rocque ........................................................... 136

K. Anantha Padmanabhan ............................................. 46

Martin Ruppert ........................................................... 141

L. Porcar......................................................................... 49

Jianbin Ruan ................................................................ 150

James W. Pflugrath ........................................................ 55

Jörg Rademann ........................................................... 152

Abdul Malik Puthan Peedikakkal ........................... 60, 247

Luca Russo .................................................................. 205

Neil G. Paterson ............................................................. 88

Sumana Roy ................................................................ 221

Dinesh Pathak ................................................................ 91

V. Ramakrishnan ......................................................... 226

Ratchadaporn Puntharod .............................................. 91

Seok‐Gn Ryu ................................................................ 234

Santosh Panjikar .............................................. 93, 95, 141

Tingting Ran ................................................................ 253

Yi Ho Park .............................................................. 99, 115- 274 -

AsCA’09

Index
P. M. Shirage.................................................................. 75

Ｓ

S. Shamoto .................................................................... 75
Yuma Sakamoto ............................................... 76, 77, 233

Israel Silman .............................................................. 8, 53

Koh Saitoh ..................................................................... 82

Joel L. Sussman .......................................................... 8, 53

Siegbert Schmid ............................................................ 85

Calvin Settachatgul ........................................................ 18

Gaojie Song ...................................................... 89, 92, 256

Joseph Schlessinger ....................................................... 18

Lianli Sun ....................................................................... 93

Katrin Sproesser ............................................................ 18

Joachim Stöckigt ..............................................93, 95, 141

Keiran S.M. Smalley ....................................................... 18

Xiao‐Dong Su .................................................. 97, 119, 137

Rafe Shellooe ................................................................. 18

Yuh‐Ju Sun ................ 98, 99, 106, 121, 131, 134, 252, 261

Yoshihisa Suzuki............................................................. 18

Atsuo Suzuki ................................................. 100, 126, 260

George Shimizu ............................................................. 19

Bret Simpson ............................................................... 101

Jim Simpson................................................................... 21

Nobutaka Shimizu ....................................................... 105

Roderick G. Stanley........................................................ 21

JinSue Song ................................................................. 108

Kai Sun ........................................................................... 22

Se Won Suh .................................. 109, 111, 115, 148, 233

Herman H‐Y. Sung ................... 22, 157, 179, 188, 195, 200

Sun Young Sohn........................................................... 110

M.A. Spackman ............................................................. 32

Che‐Kun James Shen ................................................... 113

Hiroshi Sawa ............................................................ 34, 70

Brian J. Smith ...................................................... 114, 223

Che Hsiu Shih................................................................. 36

Daron M. Standley ...................................................... 125

Kunihisa Sugimoto ......................................................... 36

Koji Suzuki ................................................................... 126

Chou‐Fu Sheu .......................................................... 36, 87

Se‐Hoon Sim................................................................ 127

T. Samtleben .......................................................... 40, 213

Dong‐Hae Shin ............................................................ 129

Yigong Shi ...................................................................... 41

Xiaoli Shi ...................................................................... 129

Michihiro Suga......................................................... 42, 92

Yi‐Che Su ..................................................................... 130

Alastair G. Stewart ......................................................... 43

Kaoru Suzuki................................................................ 131

Daniela Stock ................................................................. 43

Takeshi Sekiguchi......................................................... 131

Yoshitsugu Shiro ............................................................ 44

Tsubasa Sagara ............................................................ 131

Kentaro Suzuki ............................................................... 45

Christian L. Schmidt .................................................... 132

Tadashi Sugawara .......................................................... 45

Oliver S. Smart ............................................................ 132

Chiu Hun Su ................................................................... 49

Alexei Savchenko ......................................................... 143

Chun‐Jen Su ................................................................... 49

Tatiana Skarina ............................................................ 143

Sono Sasaki .................................................................... 50

Toru Suzuki .................................................................. 147

Harumi, Sato .................................................................. 52

Aixin Song ................................................................... 149

Xiaoli Sun ....................................................................... 52

Lihua Sun..................................................................... 149

Benoît Sanson................................................................ 53

Baolin Sun ................................................................... 150

Neil Shaw..............................................56, 89, 92, 96, 256

Marco F. Schmidt......................................................... 152

Jie Su ............................................................................. 66

Kyung Song .................................................................. 167

Bo Song ......................................................................... 68

J. Saravanan ................................................................ 169

Jirong Sun ...................................................................... 71

Walter Schnelle ........................................................... 175

Tomoyuki Sumizawa ...................................................... 72

Akiko Sekine ................................................. 177, 181, 251

Katherine Suel ............................................................... 73

Yohei Sato ................................................................... 178

Nobuhiro Suzuki ............................................................ 73

Alvin W‐H. Siu.............................................................. 179

Clemens Schulze‐Briese ................................................. 74

Hideki Shima ....................................................... 180, 184

Mamoru Sato................................................................. 74

Kazuyuki Sato ...................................................... 180, 184

Toshiyuki Shimizu .......................................................... 74- 275 -

AsCA’09

Index

Hyuk‐Soo Seo............................................................... 182

Hiroshi Tanaka ............................................................... 34

A. A. Shaikh ................................................................. 183

Masaki Takata.......................................................... 36, 50

Md. Mahbubur Rahman Shakil.................................... 183

Yukio Takahashi ............................................................. 38

Anne Spasojević – de Biré............................ 185, 186, 210

Tomitake Tsukihara........................................... 42, 72, 209

Philippe Scouflaire ....................................................... 186

Min Tang ....................................................................... 47

J. Suda ......................................................................... 187

Kohji Tashiro .................................................................. 50

Terutoshi Sakakura ...................................................... 189

Isao Takahashi ........................ 52, 159, 170, 190, 194, 199

Hidenori Sagehashi ...................................................... 191

M.B. Tang ...................................................................... 59

Setsuo Sato .......................................................... 191, 211

Mei‐Bo Tang ................................................... 62, 156, 261

Hiroshi Suzuki ...................................................... 192, 251

Hideaki Tanaka .............................................................. 72

Vasu Sriranga ............................................................... 195

Shunichi Takeda............................................................. 74

Fanny L‐Y. Shek ............................................................ 200

N. Takeshita ................................................................... 75

Yu. Stetsko ................................................................... 204

Y. Tomioka ..................................................................... 75

B.‐Y. Shew ............................................................ 204, 222

Kouji Taniguchi .............................................................. 76

Mamoru Suzuki ........................................................... 209

Nobuo Tanaka ............................................................... 82

Tadeusz Skarzynski ...................................................... 210

Kenji Tsuda .................................................................... 83

Teguh Yulius Surya Panca Putra ................................... 211

Tomitake Tshukihara ..................................................... 92

Shigeru Sugiyama ........................................................ 212

Maxim Titushin ........................................................... 101

Craig Sterling ............................................................... 214

Kunikazu Takeshita ...................................................... 105

Dyah Sulistyanintyas .................................................... 217

Sunao Takahashi .......................................................... 105

Yu. P. Stetsko ................................................................ 222

Takashi Tanaka ............................................................ 105

Wenjing Shen .............................................................. 224

Kuang‐Lei Tsai...............................................106, 121, 134

Maria Selmer ............................................................... 226

Ya‐Jun Tang.................................................................. 108

T.P.Srinivasan ............................................................... 227

Minh Hai Ta ................................................................. 111

Hyun Hoon Song .......................................................... 234

Zhenting Tang.............................................................. 117

Woon Bo Shim ............................................................. 234

Akio Takénaka ............................................................. 131

Wen‐Hua Sun............................................................... 240

Atsushi Takahashi ........................................................ 131

Chuan‐Fu Sun .............................................................. 242

Haruo Tanaka .............................................................. 131

Leonid Sazanov ............................................................ 247

Masaru Tsunoda .......................................................... 131

Haiwei Song ................................................................. 248

Jinzhi Tan ............................................................. 132, 152

Arputharaj David Stephen ........................................... 249

Jia‐Yin Tsai ................................................................... 133

Joachim Stoeckigt ........................................................ 249

Osamu Tsuruta ............................................................ 134

Yuna Sun ...................................................................... 251

Michael Thomson ....................................................... 136

Congting Sun ............................................................... 258

Tung‐Yi Tsai .................................................................. 145

Walter Schelle ............................................................. 261

Toshiji Tada .................................................................. 147
Lin Tang ....................................................................... 149
Changlin Tian .............................................................. 150

Ｔ

Katsuhide Terada .................................. 154, 161, 177, 193
Hikaru Terauchi ............................ 159, 170, 190, 194, 199

James Tsai ...................................................................... 18

Hirohisa Tanaka ........................................................... 159

Jared Taylor ................................................................... 19

Masashi Taniguchi ....................................................... 159

Ming‐Liang Tong ............................................................ 20

Norimitsu Tohnai ................................................. 160, 197

Mau‐Tsu Tang ................................................................ 25

Takumi Tajima ............................................................. 164

M.J. Turner .................................................................... 32

Henry H‐Y. Tong ........................................................... 179- 276 -

AsCA’09

Index

Kiyoaki Tanaka ..................................................... 179, 189

Ｗ

Yasuyuki Takenaka ............................................... 179, 189
Koichi Tanaka ............................................................... 181
Kota Takano ......................................................... 188, 243

Brian West ..................................................................... 18

Miwako Takahashi ....................................... 188, 243, 246

Weiru Wang .................................................................. 18

Akihisa Tokuda............................................................. 190

Hongli Wang .................................................................. 22

Shuki Torii ............................................ 191, 211, 217, 218

Meimei Wu ................................................................... 22

Kazuyuki Toyota ........................................................... 192

Ian D. Williams ........... 22, 63, 86, 157, 179, 188, 195, 200

YasuhideTomioka ......................................................... 200

Yu Wang ............................................................. 25, 36, 87

Yoshinori Tokura .......................................................... 200

Soichi.Wakatsuki ...................................... 28, 73, 104, 215

M.‐T. Tang ............................................................ 204, 222

Dong Wang.................................................................... 29

Kazufumi Takano ......................................................... 212

J. Wiesmann .......................................................... 40, 213

Thomas C. Terwilliger .................................................. 232

Jiawei Wang .................................................................. 41

Reji Thomas ................................................................. 249

Fritz Winkler ................................................................. 42

Takenori Takeda ........................................................... 251

Peter A. Wood ............................................................... 48

Jung‐Yu Tung ................................................................ 252

G.G. Warr ...................................................................... 49
Kathleen Wood ............................................................. 51
Martin Weik .................................................................. 53

Ｕ

X.J. Wang ....................................................................... 59

Tamami Uejima.............................................................. 73

Yingxia Wang ................................................................. 66

Satoru Unzai .................................................................. 74

Gang Wang .................................................................... 68

S. Uchida........................................................................ 75

Wanyan Wang ............................................................... 68

Go Ueno .............................................................. 105, 209

Wenjun Wang ............................................................... 68

Hidehiro Uekusa ........... 154, 161, 177, 181, 192, 193, 251

Chun‐Ming Wu .............................................................. 71

Mari Uenishi ................................................................ 159

Shuichi Wakimoto ......................................................... 76

Yoshiki Ueno ................................................................ 170

Bayden R. Wood ............................................................ 91

Kazuya Uta ................................................................... 178

Meitian Wang................................................... 93, 95, 141

Mai Uenaka ................................................................. 194

Lai‐Xi Wang ................................................................... 96

Matthew Weyland ........................................................ 60

Peng Wang .................................................................... 96

Yoshihito Uozaki .......................................................... 194

Chung Wang .................................................................. 98
Jinfeng Wang ............................................................... 101

Ｖ

Jundong Wang ............................................................ 107
Yi‐Ting Wang ................................................ 113, 137, 146

Ramanathan Vaidhyanathan ......................................... 19

Colin W. Ward ............................................................. 114

Jagadese J. Vittal ..................................... 60, 90, 235, 247

Leslie K. Williams ........................................................ 116

Eugene Vysotski........................................................... 101

Stephen G. Withers ..................................................... 116

Clemens Vonrhein ....................................................... 132

Andrew H.‐J. Wang ................................ 118, 130, 145,174

R. Vinayakumar ........................................................... 168

Bing Wang ................................................................... 136

Surendra Babu .V.H.H .................................................. 169

Liping Wang ................................................................ 136
Shawn Williams........................................................... 136
Jon D. Wright ............................................................... 137
Kai‐Tuo Wang .............................................................. 137
Xiao‐Jun Wang ............................................................ 137
John W. White ............................................................. 138- 277 -

AsCA’09

Index
Dongfeng Xue ...................................................... 258, 259

Jian Wu ........................................................................ 139
Kam Bo Wong .............................................................. 139
Xiaoai Wu .................................................................... 140

Ｙ

Hui Wang ..................................................................... 147
Haipeng Wang ............................................................. 150
Lin Wang ...................................................................... 150

Yaw‐Wen Yang ............................................................... 25

Qiye Wen ..................................................................... 162

Keqiong Ye..................................................................... 30

Daniel Wacker ............................................................. 182

Gung‐Chian Yin.............................................................. 39

Lawrence W‐Y. Wong ................................................... 195

Eiki yamashita ............................................ 42, 72, 92, 209

S.‐C. Weng ................................................................... 204

Kuan‐Li Yu...................................................................... 49

Michael Willis .............................................................. 214

Shouke Yan .................................................................... 52

Albert Weixlbaumer .................................................... 226

Cheng Yang.................................................................... 55

Eileen White ................................................................ 229

X.X. Yang........................................................................ 59

Tao Wang ..................................................................... 245

Xin‐Xin Yang ........................................... 62, 156, 163, 261

Ulrike Wedemeyer....................................................... 245

Masatomo Yashima ....................................................... 64

Ning Wang ................................................................... 253

Chun‐Chuen Yang .......................................................... 71

Weiwu Wang ............................................................... 253

Min Yao ......................................................................... 72

Hsin‐Mao Wu............................................................... 254

Masato Yoshimura..................................................72, 209

Wen‐Ching Wang ......................................................... 254

Shin‐Mei Yeh ................................................................. 74

Linhong Weng...................................................... 254, 255

Jie Yin ...................................................................... 89, 96

Dong Wu...................................................................... 256

Shinya Yoshikawa .................................................. 92, 209

Hsin‐Yi Wu ................................................................... 257

Liuqing Yang .................................................................. 95

Shu‐Zon Wu ................................................................. 261

Kai‐Wun Yeh .................................................................. 98

Luet‐Lok Wong............................................................. 263

Takashi Yamane ............................................ 100, 126, 260
Masahiro Yoshida ........................................................ 102
Yusuke Yamada.................................................... 104, 215

Ｘ

Hirokatsu Yumoto ....................................................... 105
Masaki Yamamoto............................................... 105, 209

Hongjie Xu ..................................................................... 23

Hanna S. Yuan ...................................... 106, 113, 137, 146

Anbi Xu .......................................................................... 30

Haiyang Yu................................................................... 107

Yong Xiong ..................................................................... 58

Cai Yuan .............................................................. 107, 149

Fangfang Xu ................................................................... 78

Jiang Yu ....................................................................... 108

Liqun Xia ...................................................................... 141

Hye‐Jin Yoon ................................. 109, 111, 115, 148, 233

Min Xu ......................................................................... 142

Ji Young Yoon........................................ 111, 115, 148, 233

Wei Xie ........................................................................ 142

In Seok Yang ................................................................ 115

Xiaohui Xu ................................................................... 143

Chao‐Yu Yang ....................................................... 118, 145

Feng Xue ...................................................................... 144

Soohwan Yum ............................................................. 128

Chunyan Xu.................................................................. 149

Hideshi Yokoyama ....................................................... 134

Wei Xu ......................................................................... 225

Jer‐Yen Yang................................................................. 134

Rong Xiao..................................................................... 229

Peter N. Yaron ............................................................. 138

Zhen Xu........................................................................ 259

Sheng Ye ...................................................................... 140

Yongbin Xu ................................................... 127, 144, 150

Wupeng Yan ................................................................ 140

Jian Xu ................................................................. 196, 214

Che‐Chuan Yang .......................................................... 146

Fei Xue ................................................................. 251, 263

Koichi Yokota ............................................................... 147- 278 -

AsCA’09

Index

Tadashi Yamamoto ...................................................... 147

J.T. Zhao ......................................................................... 59

Xiaoyan Yang ............................................................... 147

Jing‐Tai Zhao................................... 62, 156, 163, 175, 261

Xiuna Yang ................................................................... 147

Yong Zhou ............................................................. 72, 242

Yue Yu .......................................................................... 147

Yu Zhao ......................................................................... 92

Wen Yang............................................................. 147, 263

Rongguang Zhang........................................... 92, 108, 256

Feng Yu ........................................................................ 149

Cong‐Zhao Zhou .................................................. 108, 121

Bo‐Young Yun ............................................................... 150

Ran Zhang ................................................................... 116

Etsuo Yonemochi ................................. 154, 161, 177, 193

Jindong Zhao ............................................................... 117

Grin Yuri....................................................................... 156

Xiaofeng Zheng ................................................... 117, 123

Osamu Yamate ............................................................ 178

Yan Zhang .................................................................... 137

Masashi Yokoyama ...................................................... 181

Guoping Zhao .............................................................. 139

Masao Yonemura......................................... 191, 206, 217

Peng Zhang.................................................................. 139

Alex S‐F. Au Yeung........................................................ 195

Zilong Zhang................................................................ 139

Atsushi Yamamoto ....................................................... 197

Cong Zhao ............................................................ 147, 151

Bing‐Ping Yang ............................................................. 198

Jianye Zang .................................................................. 150

Chunming Yang ............................................................ 199

Liang Zhang ................................................................. 151

Fion T‐Y. Yeong ............................................................. 200

Lili Zhu ......................................................................... 152

Xiuzhen Yu ................................................................... 200

Zhixue Zhu................................................................... 156

M. Yabashi ................................................................... 204

Hui Zhang ............................................................ 156, 261

Naoto YAGI .................................................................. 214

Huaiwu Zhang ............................................................. 162

Jiho Yoo ....................................................................... 223

Dunwen Zuo ................................................................ 172

Wen‐Tao Yu ................................................................. 225

Xianliang Zhou............................................................. 172

Tadashi Yamazaki ......................................................... 233

P. G. Zverev .................................................................. 187

Hsin‐Sheng Yang .......................................................... 248

Junrong Zhang ...................................... 191, 211, 217, 218

Chih‐Wei Yang ............................................................. 252

Qingdi Zhou ................................................................. 201

Yi‐Hung Yeh ................................................................. 261

Li Zhao ......................................................................... 229
Ze ZHANG .................................................................... 236
Ying‐Ying Zhang ........................................................... 239

Ｚ

Chuli Zhang ................................................................. 245
Xuejun C. Zhang .......................................................... 251

Chao Zhang.................................................................... 18

Yaming zhou ................................................................ 254

Jiazhong Zhang .............................................................. 18

Wenzheng Zhang ........................................................ 262

Kam Y.J. Zhang ............................................................... 18

Zonghao Zeng.............................................................. 262

Yong‐Liang Zhu .............................................................. 18

Weihong Zhou ......................................................262, 263

Zhentang Zhao............................................................... 23

Qi Zhao ........................................................................ 263

Liman Zhang .................................................................. 30

Yilong Zou ................................................................... 263

Lijun Zhou ...................................................................... 41
H. Zhang ........................................................................ 59- 279 -