COMMITTEESORAL ABSTRACTSSPONSORSPOSTER ABSTRACTSPROGRAMAUTHOR INDEXCommittees
Asian Crystallographic Association
President: Prof. Mamannamana Vijayan
Indian Institute of Science, India
Vice President: Prof. Mitchell Guss
University of Sydney, Australia
Treasurer & Secretary: Prof. Ian Williams
Hong Kong University of Science & Technology, Hong Kong

International Program Committee
Chairman: Se Won Suh
Members:
Amemiya, Yoshiyuki
Baker, Ted
Feng, Donglei
Kennedy, Brendan
Martin, Jennifer
Miki, Kunio
Murakami, Youichi
Ogawa, KeiichiroRao, Zihe
Row, T. N. Guru
Singh, T. P.
Wang, Andrew
Wang, Yu
Williams, Ian

Korea
Japan
New Zealand
China
Australia
Australia
Japan
Japan
Japan
China
India
India
TaiwanTaiwanHong Kong

Organizing Committee
Chairman: Shih-Lin Chang
Members:
Hsiao, Chwan-Deng
Jean, Yuch-Cheng
Lee, Chih-Hao
Liang, Keng S.
Lii, Kwang-Hwa
Liu, Ling-Kang
Peng, Shie-Ming
Sheu, Hwo-Shuenn
Wang, Andrew
Wang,Yu
Yu, Shu-Cheng
Yuan, Hanna S.

National Tsing Hua University
Academia Sinica
National Synchrotron Radiation
Research Center
National Tsing Hua University
National Synchrotron Radiation
Research Center
National Central University
Academia Sinica
National Taiwan University
National Synchrotron Radiation
Research Center
Academia Sinica
National Taiwan University
National Cheng Kung University
Academia Sinica

IUCr Scientific Freedom Policy Statement
The Organizing Committee of the AsCA 2007 shall observe the basic policy of
non-discrimination and affirms the right and freedom of scientists to associate ininternational scientific activity without regard to such factors as citizenship,
religion, creed, political stance, ethnic origin, race, colour, language, age or gender,in accordance with the Statutes of the International Council for Science.
At AsCA 2007 no barriers will exist which would prevent the participation of
bona fide scientists.

General Information
Registration and Reception
The Registration Desk is located on the 1F.
Opening Time: November 4,
13:30~18:00
November 5~7, 8:00~18:00
A name badge is required for all sessions.
Exhibition
The exhibitions are displayed on the 1F and 2F during theOpening Time: November 5~6, 8:30~18:00
November 7,
8:30~12:00
Internet Access
Computers will be set up on 2F for attendees to access to the Internet. For every
attendee’s convenience, please limit Internet your access to 10 minutes, so thatevery attendee has the opportunity to use the Internet service. Free wirelessInternet is available, but the speed is limited.
Luncheon & Coffee BreakLuncheon from November 5 to 7 will be served on the 2F (Yueshiang Restaurant)
and on the B1 (Social Room) from 12:15 to 13:30.
280 seats are available at the 2F and 120 seats are available at the B1.
Vegetarian Service will be provided on the B1.
Coffee and tea are served during tea time on the 1F and 2F.
Shuttle Service
Free Shuttle Buses from and to the venues of two evening events, Dinner Buffet
and Banquet, are provided.
Pre-event
Shuttles are available at the main entrance of the Howard International Houseon the 1F from 18:30 to 19:00.
Shuttles leave as soon as they are full.
The last shuttle leaves at 19:00.
Post-event
Please follow the staff in blue uniform handing “AsCA 2007” sign.
Shuttles leave as soon as they are full.
Shuttles do not serve any other stops except for Howard International House.
The last shuttle leaves 30 minutes after the end of the event.

Information for Authors and Presenters
Oral Presentations
A set of notebook PC and LCD projector will be ready in each hall/room. Eachroom has AsCA staffs in blue uniform. All presenters are kindly requested to cometo the speaker ready room 30 minutes prior to your session and please hand yourfile or notebook to our site staffs.
What do Oral Codes stand for?
For example, “O1A05-M1”
O
is initial of Oral.
1
is Session number from 1 to 6.
Aindicate the room.
“A”: Convention Hall, “B”: Conference Room, “C”: Room 103
05
means the presentation date.
M
indicate the time.
“M”: Morning, “A”: Afternoon
1is the presentation sequence.
Poster Presentations
Poster presentations are held in the corridors on the 2F to 4F in the Howard
International House from 13:30 on Nov. 5 to 15:30 on Nov. 6.
All posters are scheduled to be displayed for 2 days.
Authors are kindly requested to set up posters between 10:30 and 13:30 on Nov. 5
and to remove them between 15:30 and 17:00 on Nov. 6.
What do Poster Codes stand for?
For example, “P05-116”
P
is initial of Poster.
05
indicates that the author of poster should have to present in person on
November 5 from 13:30~15:30
116
the serial number of poster, which you can easily find your display
board by following the number.
Poster Board Size
95cm(Width)X120cm(Height)

AsCA’07 Program Timetable
Nov.

4

5

SundayMonday08:00

Registration from 08:00

08:30

Opening 08:30 – 09:00 (A)

09:00

Plenary 1 (20th Anniversary) 09:00 – 10:00
Dr. Zhong Lin Wang (A)Coffee Break 10:00 – 10:15

10:00
10:15

-

Oral Session 1 10:15 – 12:15
MS-16/17: New methods for structural biology (A)MS-12: Crystallography of pharmaceuticals and natural products (B)MS-04: Advances in small angle X-ray and neutron scattering (C)

12:15

Lunch 12:15 – 13:30

13:30

Poster – 1 13:30 – 15:30
Corridor 2F, 3F, 4F

Registration
15:30

Break 15:30 – 16:00

13:30 – 18:00

16:00

Oral Session 2 16:00 – 18:30
MS-15: Macromolecular assemblies: proteins and nucleic acids (A)MS-09: Science of inorganic materials (B)MS-05: Electronic structure and bonding by X-ray diffraction and othertechniques (C)

18:00

-

18:30
19:30

Welcome Mixer
Rayonix& Marresearch

Dinner Buffet

18:30 – 21:00

Bruker – AXS

2F, Howard International House

19:30 – 21:30
Hall 201, NTU Internaitonal Convention Center

21:00

-

(A): Convention Hall, (B): Conference Room, (C): Room 103

6

7

Tuesday

Wednesday--

Plenary 2 & 3 09:00 – 10:00

Plenary 4 & 5 09:00 – 10:00

Dr. Jill Trewhella (A)Dr. Osamu Nureki (A)Dr. Krishan Lal (B)Dr. Kwang-Hwa Lii (B)

Nov.
08:00
08:30
09:00

Coffee Break 10:00 – 10:15

10:00
10:15

Oral session 3 10:15 – 12:15

Oral session 5 10:15 – 12:15

MS-13: Membrane proteins - methods and structures MS-18a: Cool structures in protein crystallography I (A)(A)

MS-10: Science of organic materials (B)MS-06: Scattering studies of novel electronic and ma MS-01: Neutron sources, instrumentation, andgnetic systems (B)applications (C)MS-02: Synchrotron, instrumentation, time-resolved
technique, and remote access (C)
12:15
13:30

Lunch 12:15 – 13:30
Poster – 2 13:30 – 15:30

Oral session 6 13:30 – 15:30

Corridor 2F, 3F, 4F

MS-18a: Cool structures in protein crystallography II (A)MS-11: Dynamic aspects of molecular and solid state
crystals (B)MS-03: Advances in powder X-ray and neutron
diffraction (C)Break 15:30 – 16:00

15:30
16:00

Oral session 4 16:00 – 18:30

Plenary 6 (20th Anniversary) 16:00 – 17:00

MS-14: Proteins related to disease/drug discovery (A)Dr. Yigong Shi (A)MS-07: Crystal engineering and supramolecular
17:00

chemistry (B)Closing ceremony (A) 17:00

MS-08: Nano technology: structure, surface, and in

Farewell Party 17:30 – 19:30

terface (C)2F, Howard International House
18:30

-

19:30

BanquetRigaku19:30 – 21:30
3F, Grand Formosa Regent Hotel(A): Convention Hall, (B): Conference Room, (C): Room 103-

November 05, Monday
Plenary 1 (09:00 – 10:00) (Convention Hall)
Chair: Sydney Hall

10:15 PL05-001 OXIDE NANOSTRUCTURES – FROM GROWTH TO
NANOGENERATORS AND TO NANOPIEZOTRONICS
Zhong Lin Wang

Oral Session 1 (10:15-12:15) (Convention Hall)
MS-16/17: New methods for structural biology
Chair/Co-chair: Isao Tanaka, Zhi-Jie Liu

10:15 O1A05-M1 THE EFFECT OF AMINO ACIDS AND AMINO ACIDDERIVATIVES ON PROTEIN CRYSTALLIZATION
L. Ito, T. Kobayashi, K. Shiraki, T. Narukawa, A. Oosuka and H.
Yamaguchi
10:40 O1A05-M2 (NZ)CH...O CONTACTS ASSISTED CRYSTALLIZATION
Neil Shaw, Zhongyun Cheng, Bi-Cheng Wang, Zihe Rao and Zhi-Jie Liu
11:05 O1A05-M3 PHASING WITH IN-HOUSE SOFTER X-RAY RADIATION
Cheng Yang, James W. Pflugrath, Joseph D. Ferrara
11:30 O1A05-M4 LONG WAVELENGTH PHASING: CURRENT AND FUTURE
CHALLENGES
B.C. Wang, John Rose, Lirong Chen, John Ruble, James Tucker Swindell
II, Zeng-Qing Albert Fu, Jim Fait, Zhongmin Jin, Andrew Horward andJohn Chrzas
11:55 O1A05-M5 PSAP: PROTEIN STRUCTURE ANALYSIS PACKAGE
K. Sekar, B.Balamurugan, M.N.A.Md.Roshan, B.Shaahul Hameed,
K.Sumathi, R.Senthil Kumar, A.Udayakumar, K.H.Venkatesh Babu,
M.Kalaivani, G.Sowmiya, P.Sivasankari, S.Saravanan, C.Vasuki Ranjani,
K.Gopalakrishnan, K.N.Selvakumar, M.Jaikumar, T.Brindha and Daliah
MichaelOral Session 1 (10:15-12:15) (Conference Room)MS-12: Crystallography of pharmaceuticals and natural products
Chair/Co-chair: Ian D. Williams, H. K. Fun

10:15 O1B05-M1 CONTROL OF POLYMORPHIC TRANSITION INDUCING
PREFERENTIAL ENRICHMENT BY MODIFYING
MOLECULAR STRUCTURES OR ADDING SEED CRYSTALS
Rui Tamura
10:45 O1B05-M2 POLYMORPHISM CASE STUDIES IN THE ARTEMISININ
FAMILY OF ANTI-MALARIAL DRUGS: INVOLVEMENT OF
MOLECULAR SHEET MOTIFS
Fanny L-Y. Shek, Herman H-Y. Sung, Richard K. Haynes and Ian D.
Williams
11:05 O1B05-M3 DETERMINATION OF ABSOLUTE CONFIGURATION FOR
SOME NATURAL PRODUCTS FROM TRADITIONAL CHINESE
MEDICINE
Herman H-Y. Sung, Nancy Y. Ip and Ian D. Williams
11:25 O1B05-M4 DISTINGUISHING BETWEEN NATURAL PRODUCTS AND
NATURAL PRODUCT ARTIFACTS USING SINGLE CRYSTAL
X-RAY STRUCTURE DETERMINATION: A CASE STUDY ON
MACLURAXANTHONE, A COMPOUND CONTAINING A
CHROMENE RING
Suchada Chantrapromma, Nawong Boonnak, and Hoong-Kun Fun
11:45 O1B05-M5 PROTEIN MEASUREMENTS ON A LABORATORY POWDER
X-RAY DIFFRACTOMETER
D. Beckers, S. Prugovečki, T. Degen, A. Stefanovic

Oral Session 1 (10:15-12:15) (Room 103)
MS-04: Advances in small angle X-ray and neutron scattering
Chair/Co-chair: Yoshiyuki Amemiya, Moonhor Ree

10:15 O1C05-M1 QUANTITATIVE GISAXS ANALYSIS OF LAMELLAR
STRUCTURES SELF-ASSEMBLED IN BRUSH POLYMER THIN
FILMS
Moonhor Ree, Jinhwan Yoon, Kyeong Sik Jin, Kyuyoung Heo, Sangwoo
Jin, Jehan Kim, Kwang-Woo Kim, Tae Joo Shin
10:35 O1C05-M2 MESO AND NANO-SCALE STRUCTURAL FORMATION OF
POLYETHYLENE THIN FILMS EVALUATED BYSYNCHROTRON GRAZING-INCIDENCE SMALL-ANGLE AND
WIDE-ANGLE X-RAY SCATTERING MEASUREMENTS
Sono SASAKI, Hiroyasu MASUNAGA, Hiroo TAJIRI, Katsuaki
INOUE, Hiroshi OKUDA, Atsushi TAKAHARA, Masaki TAKATA
10:55 O1C05-M3 STRUCTURAL CHANGES IN THE MECHANICALDEFORMATION PROCESS OF SPECIFICALLY-ORIENTED
POLYETHYLENE SAMPLES AS VIEWED FROM THE
SIMULTANEOUS MEASUREMENTS OF SYNCHROTRONSAXS-WAXD AND RAMAN SPECTRA
Kohji TASHIRO, Shinichi TAKEDA, Makoto HANESAKA, Hiroyasu
MASUNAGA, Sono SASAKI and Masaki TAKATA
11:15 O1C05-M4 STRAIN-INDUCED CRYSTALLIZATION OF REINFORCED
NATURAL RUBBER AS STUDIED BY SYNCHROTRON X-RAY
SCATTERING
Hyun Hoon Song, Min Kwan Kang, Hye-Jin Jeon, Gwanghoon Kwag
and Hyungkyu Choi
11:35 O1C05-M5 ANOMALOUS SMALL ANGLE X-RAY SCATTERING FOR THE
DISTRIBUTION AND AGGREGATION OF THE GOLDNANOPARTICLES IN A PS-b-P4VP DIBLOCK COPOLYMER
U-Ser Jeng, Ying-Huang Lai, Ching-Mao Huang, and Kung-Hwa Wei,
Chiu-Hun Su, and Hwo-Shuenn Sheu
11:55 O1C05-M4 CORE-SHELL MICELLAR STRUCTURES OF NOVELTERTIARY AMINE METHACRYLATE-BASED BLOCKCOPOLYMERS STUDIED BY SMALL ANGLE X-RAY
SCATTERING AND DYNAMIC LIGHT SCATTERING
Yusuf Ozcan, U-Ser Jeng, Vural Butun, Ying-Huang Lai, Chiu-Hun Su,
Keng S. Liang, Semra IdeOral Session 2 (16:00-18:30) (Convention Hall)
MS-15: Macromolecular assemblies: proteins and nucleic acids
Chair/Co-chair: Atsushi Nakagawa, Mike Lawrence

16:00 O2A05-A1 STRUCTURE, ASSEMBLY AND ACTION OF DODECAMERIC
DPS, A STRESS RELATED FAMILY OF PROTEINS
Siddhartha Roy, Ramachandran Saraswathi, Surbhi Gupta, K.Sekar,
Dipankar Chatterji and M.Vijayan
16:25 O2A05-A2 STRUCTURL AND FUNCTIONAL STUDY OF C. ELEGANS
CELL-DEATH RELATED NUCLEASE 4 (CRN-4)
Yu-Yuan Hsiao and Hanna S. Yuan
16:45 O2A05-A3 CONFORMATIONAL CHANGE IN BIFUNCTIONALREPLICATION INITIATOR PROTEIN RepE
Akira Nakamura, Chieko Wada and Kunio Miki
17:05 O2A05-A4 STRUCTURE OF AN IgNAR-AMA1 COMPLEX
Victor Streltsov, Kylie Henderson, Andrew Coley, Adrian Batchelor,
Robin Anders, Michael Foley, Stewart Nuttall
17:25 O2A05-A5 STRUCTURAL AND FUNCTIONAL INSIGHTS INTO DOM34, A
KEY COMPONENT OF NO-GO mRNA DECAY
Hyung Ho Lee and Se Won Suh
17:45 O2A05-A6 THE CRYSTAL STRUCTURE OF A VIRUS-LIKE PARTICLE
FROM HYPERTHERMOPHILLIC ARCAHEON PYROCOCCUSFURIOSUS PROVIDE INSIGHT INTO THE EVOLUTION OF
VIRUSES
Fusamichi Akita, Khoon Tee Chong, Hideaki Tanaka, Eiki Yamashita,
Naoyuki Miyazaki, Yuichiro Nakaishi, Kazunori Namba, Mamoru
Suzuki, Tomitake Tsukihara and Atsushi Nakagawa
18:10 O2A05-A7 HIGHER RESOLUTION STRUCTURE OF GIANTHEMOGLOBIN FROM OLIGOBRACHIA MASHIKOI
Nobutaka Numoto, Taro Nakagawa, Akiko Kita, Yuichi Sasayama,
Yoshihiro Fukumori and Kunio Miki

Oral Session 2 (16:00-18:30) (Conference Room)MS-09: Science of inorganic materials
Chair/Co-chair: Yukio Noda, Je-Geun Park

16:00 O2B05-A1 VISUALIZATION OF RATTILING IN PrOs4Sb12 BY SINGLECRYSTAL NEUTRON DIFFRACTION
Koji Kaneko, Naoto Metoki, Hiroyuki Kimura, Yukio Noda, Tatsuma D.
Matsuda and Masafumi Kohgi
16:30 O2B05-A2 SINGLE CRYSTAL NEUTRON DIFFRACTIONINVESTIGATIONS OF TYPE I CLATHRATES – POTENTIAL
THERMOELECTRIC MATERIAL
Mogens Christensen, Bo B. Iversen.
16:50 O2B05-A3 X-RAY SCATTERING STUDY OF RB4
Ki Bong Lee, S. Ji, C. Song, J. Koo, Y. J. Park, J. Y, Kim and B. K. Cho
17:20 O2B05-A4 HYDROGEN BONDING PHASE TRANSITIONS IN SOMEORGANIC CRYSTALS
Hoong-Kun Fun, Beck-Sim Lee and Suchada Chantrapromma
17:40 O2B05-A5 DIFFRACTION STUDIES OF RELATION BETWEEN HELICITYOF CYCLOID MAGNETISM AND FERROELECTRIC
POLARIZATION IN MULTIFERROIC MANGANESE OXIDES
Taka-hisa Arima, Hajime Sagayama, Nobuyuki Abe, Koji Taniguchi,
Hiroyuki Ohsumi, Masato Matsuura, Kazuma Hirota, Daisuke Okuyama,
Yuichi Yamasaki, and Yoshinori Tokura
18:10 O2B05-A6 ANOMALOUS STRUCTURAL PHASE TRANSITION ABOVELIQUID NITROGEN TEMPERATURE IN THE MULTIFERROICPEROVSKITE Dy(Mn0.5Fe0.5)O3
Fu-Kuo Chiang , Fei-Ting Huang, and Ming-Wen Chu

Oral Session 2 (16:00-18:30) (Room 103)
MS-05: Electronic structure and bonding by X-ray diffraction and othertechniques
Chair/Co-chair: Yu Wang, T. N. Guru Row

16:00 O2C05-A1 SINGLE CRYSTAL STRUCUTURE ANALYSIS OF
PHOTO-EXCITED STATES OF HALOGEN-BRIDGEDDICOPPER(I) COMPLEXES
Yoshiki Ozawa, Shingo Yoshida, Nobuyuki Kitayama, Minoru Mitsumi,
Koshiro Toriumi, Kiyoshi Tsuge, Hiromi Araki, and Yoichi Sasaki
16:30 O2C05-A2 INVESTIGATION OF THE PHOTOEXCITEDCHARGE-TRANSFER STATE OF [AuBr(PPh3)2] BY THE
MULTIPLE-EXPOSURE IP METHODManabu Hoshino, Hidehiro Uekusa, Shintaro Sonoda, Takuhiro Otsuka,
Youkoh Kaizu, Yoshiki Ozawa, Koshiro Toriumi
17:00 O2C05-A3 X-RAY ATOMIC ORBITAL ANALYSIS AND ITS APPLICATIONTO RARE-EARTH CRYSTALS
Kiyoaki Tanaka, Ryoko Makita, Shiro Funahashi, Takashi Komori,
Terutoshi Sakakura
17:30 O2C05-A4 STRUCTURES OF POLYPYRIDINE MONONUCLEAR IR(III)COMPLEXES IN THE CLOSED-SHELL SINGLET AND
TRIPLET STATES
Naokazu Yoshikawa, Shinichi Yamabe, Nobuko Kanehisa, Yasushi Kai,
Hiroshi Takashima, and Keiichi Tsukahara
18:00 O2C05-A5 APEX II ULTRA - PRECISION AND ACCURACY
Michael Ruf, Martin Adam

November 06, Tuesday
Plenary 2 (09:00 – 10:00) (Convention Hall)
Chair: Sine Larsen

10:15 PL06-002 BIOMOLECULAR SIGNALLING AND REGULATION; A
SOLUTION SCATTERING VIEW
Jill Trewhella
Plenary 3 (09:00 – 10:00) (Conference Room)
Chair: Shih-Lin Chang

10:15 PL06-003 CHALLENGES IN CHARACTERIZATION OF SINGLECRYSTALS, THIN LAYERS AND DEVICES BY HIGHRESOLUTION X-RAY DIFFRACTION AND REFLECTIONTECHNIQUES
Krishan Lal
Oral Session 3 (10:15-12:15) (Convention Hall)
MS-13: Membrane proteins - methods and structures
Chair/Co-chair: Satoshi Murakami, Che Alex Ma

10:15 O3A06-M1 FLUORESCENCE-DETECTION SIZE EXCLUSIONCHROMATOGRAPHY FOR PRECRYSTALLIZATIONSCREENING OF INTEGRAL MEMBRANE PROTEINS
Toshimitsu Kawate, Atsuko Yamashita, Jaysankar Jasti, Michael
Rosconi, Paul Shaffer, Alexander Sobolevsky, Tanja Homrichhausen and
Eric Gouaux
10:40 O3A06-M2 ION BINDING AND SELECTIVITY OF THE ROTOR OF THE
V-TYPE NA+-ATPASE FROM ENTEROCOCCUS HIRAE
Takeshi Murata, Ichiro Yamato, Yoshimi Kakinuma, Mikako Shirouzu,
John E. Walker, Shigeyuki Yokoyama and So Iwata
11:05 O3A06-M3 NEW STRUCTURAL ASPECTS OF BOVINE HEARTCYTOCHROME C OXIDASE
H. Aoyama, T. Tsukihara and S. Yoshikawa
11:30 O3A06-M4 STRUCTURE OF THE CYTOCHROME b6f COMPLEX:QUINONE ANALOGUE INHIBITORS AS LIGANDS OF HEME
cn
Eiki Yamashita, Huamin Zhang,William A. Cramer

11:50 O3A06-M5 X-RAY STRUCTURE of EmrE SUPPORTS DUAL TOPOLOGY
MODEL
Yen-Ju Chen, Owen Pornillos, Samantha Lieu, Che Ma, Andy P. Chen,
Geoffrey Chang

Oral Session 3 (10:15-12:15) (Conference Room)
MS-06: Scattering studies of novel electronic and magnetic systems
Chair/Co-chair: Donglai Feng, Yong-Qiang Cai

10:15 O3B06-M1 MOMENTUM DEPENDENT CHARGE EXCITATIONS IN
CORRELATED ELECTRON SYSTEMS STUDIED BYRESONANT INELASTIC X-RAY SCATTERING
Kenji Ishii
10:40 O3B06-M2 SPIN, CHARGE, AND ORBITAL ORDERING OF
TRANSITION-METAL OXIDES
Di-Jing Huang

11:05 O3B06-M3 WIGNER CRYSTALLIZATION IN A MOLECULARCONDUCTOR, (DI-DCNQI)2Ag
Hiroshi Sawa, Toru Kakiuchi, Yusuke Wakabayashi, and Kazushi
Kanoda11:25 O3B06-M4 Q-DEPENDENT DIELECTRIC FUCTION STUDIES USINGINELASTIC X-RAY SCATTERING
N. Hiraoka, H. Ishii, I. Jarrige, and Y. Q. Cai,
11:45 O3B06-M5 CRYSTAL AND MAGNETIC STRUCTURE OF ORGANICCONDUCTOR β'-ET2ICl2 BY USING NEUTRONS
Yukio Noda, Masashi Watanabe, Atsushi Matsunaga, Satoshi Komiyama,
HiromiTaniguchi, Atshushi Kawamoto and Yoshiya Uwatoko
12:00 O3B06-M6 LATTICE DISTORTION AND FERROMAGNETISM IN BaRuO3
Chao-hung Du, K. J. Tseng, Y. Y. Lo, Mau-Tsu Tang

Oral Session 3 (10:15-12:15) (Room 103)
MS-02: Synchrotron, instrumentation, time-resolved technique, and remote
accessChair/Co-chair: Soichi Wakatsuki, Julian Adams

10:15 O3C06-M1 THE AUSTRALIAN SYNCHROTRON
Julian Adams
10:45 O3C06-M2 AUTOMATION AT SER-CAT: TOWARDS SIGNAL BASEDDATA COLLECTIONJohn P. Rose, John Chrzas, James Fait, Zeng-Qing Albert Fu, Andrew
Howard, John Gonczy, Zhongmin Jin and B. C. Wang
11:15 O3C06-M3 100-PS TIME-RESOLVED X-RAY EXPERIMENTS WITH DAILYSINGLE BUNCH MODE: CURRENT STATUS OF BEAM LINE
NW14A AT THE PHOTON FACTORY ADVANCED RING
Shin-ichi Adachi
11:45 O3C06-M4 DEVELOPMENT AND APPLICATION OF THE “PINPOINT
STRUCTURE MEASUREMENT SYSTEM”
Sub-Micron Beam and Time-Resolved Measurement at SPring-8’s
BL40XU
Shigeru Kimura, Nobuhiro Yasuda, Yoshimitsu Fukuyama, Jungeun
Kim, Yoshihito Tanaka, Koshiro Toriumi, Yutaka Moritomo, Yoshihiro
Kuroiwa, Kenichi Kato and Masaki Takata

Oral Session 4 (16:00-18:30) (Convention Hall)
MS-14: Proteins related to disease/drug discovery
Chair/Co-chair: Jennifer Martin, Andrew Wang

16:00 O4A06-A1 ALANINE RACEMASE AS A TEMPLATE FOR DRUGDISCOVERY IN TUBERCULOSIS
Kurt Krause , Mike Benedik, James Briggs, Milya Davlieva , Harold
Kohn , Joe Longtin, Daniel Milligan , Ulrich Strych
16:30 O4A06-A2 STRUCTURES OF ALL FOUR PHOSPHODIESTERASE-4
SUBFAMILIES PROVIDE INSIGHT INTO SUBFAMILYINHIBITOR SELECTIVITY
Jiwen Cai, Huanchen Wang, Ming-Sheng Peng, Yi Chen, Jie Geng,
Howard Robinson, Miles Houslay & Hengming Ke
17:00 O4A06-A3 STRUCTURAL BASIS FOR RECRUITMENT OF TANDEM
HOTDOG DOMAINS IN ACYL-COA THIOESTERASE 7 AND
ITS ROLE IN INFLAMMATION
Jade K. Forwood, Anil S. Thakur, Gregor Guncar, Mary Marfori, Dmitri
Mouradov, Stuart Kellie, David A. Hume, Thomas Huber, Jennifer L.
Martin, Bostjan Kobe
17:30 O4A06-A4 THROUGH-PUT PROTEIN STRUCTURE DETERMINATION
AND RATIONAL STRUCTURE-BASED DRUG DESIGN USINGFRAGMENT-BASED APPROACH
Tej P. Singh, Sanjit Kumar, Pradeep Sharma, Rafia Mir, Ishfaq A.
Sheikh, Amit K. Singh, R. Prem Kumar, Mau Sinha, Nagendra Singh,
Punit Kaur, A. Srinivasan and S. Sharma
17:50 O4A06-A5 STRUCTURAL BASIS FOR GLUTAMATE RACEMASEINHIBITION
Kook-Han Kim, Young-Jong Bong, Joon Kyu Park, Key-Jung Shin,
Kwang Yeon Hwang and Eunice EunKyeong Kim
18:10 O4A06-A6 CRYSTAL STRUCTURE OF ABT-737 IN COMPLEX WITH
Bcl-xLPeter E. Czabotar, Erinna F. Lee, Brian J. Smith, Kurt Deshayes, Kerry
Zobel, W. Douglas Fairlie, Peter M. Colman

Oral Session 4 (16:00-18:30) (Conference Room)MS-07: Crystal Engineering and Supramolecular Chemistry
Chair/Co-chair: Ashwini Nangia, Jun Harada

16:00 O4B06-A1 MOLECULAR BRICKS, PENS, GRIDS AND SPHEROIDS FROMDIHETEROAROMATIC HOSTS
Roger Bishop, Solhe F. Alshahateet, Jason Ashmore, Donald C. Craig
and Marcia L. Scudder
16:30 O4B06-A2 ROLE OF MIXED HALOGENS (F, Br) TOWARDS CRYSTALPACKING AND INTERMOLECULAR INTERACTIONS IN
SUBSTITUTED BENZANILIDES
Susanta K. Nayak, T. N. Guru Row
16:50 O4B06-A3 SYNTHESIS, STRUCTURES AND MAGNETIC PROPERTIES OFA SERIES OF CYANO-BRIDGED HETEROMETALLICCOMPLEXES
Shao-Jun Wang, Long Jiang, Wei-Xiong Zhang and Tong-Bu Lu
17:20 O4B06-A4 WATER CLUSTERS, ISOSTRUCTURALITY AND
POLYMORPHISM IN HYDROXY DERIVATIVE OFHALOBENZENE CRYSTAL STRUCTURES
Binoy Saha
17:40 O4B06-A5 ENGINEERING OF LUMINESCENT PROPERTIES IN MIXEDLANTHANIDE CARBOXYLATE COORDINATION POLYMERSYuFong Yen, Samadara Thushari, Alvin Siu, Kam-Sing Wong and Ian D.
Williams
18:10 O4B06-A6 SUPRAMOLECULAR ASSEMBLIES OF MONONUCLEAR AND
POLYMERIC COBALT(ii) AND NI(II) DICARBOXYLICCOMPLEXES
Tanwawan Duangthongyou, Sutatip Siripaisarnpipat , Chris Adams

Oral Session 4 (16:00-18:30) (Room 103)
MS-08: Nano technology: structure, surface, and interface
Chair/Co-chair: Shie-Ming Peng, Isao Takahashi

16:00 O4C06-A1 QUENCHED DISORDER EFFECTS IN TOPOLOGICALLYORDERED NANOPORES ON THE SMECTIC PHASE
TRANSITION OF 8CB
R. Guegan, D. Morineau, R. Lefort, A. Moreac, and M. Guendouz
16:20 O4C06-A2 AN ELECTRON DIFFRACTION METHOD FOR DETERMINING
THE CHIRALITY OF CARBON NANOTUBES
Lu-Chang Qin, Hakan Deniz, Jie Tang
16:40 O4C06-A3 RHEED SURFACE POLE FIGURE -- A NEW IN-SITU
TECHNIQUE FOR POLYCRYSTALLINE AND
NANOSTRUCTURED SURFACE TEXTURE ANALYSISFu Tang, Toh-Ming Lu and Gwo-Ching Wang
17:00 O4C06-A4 QUANTUM OSCILLATIONS AND BEATS IN X-RAY
REFLECTION DURING FILM GROWTH
Y.-R. Lee, A. Gray, J. Tischler, P. Czoschke, H. Hong, S.-L. Chang, andT.-C. Chiang
17:20 O4C06-A5 CHARACTERIZATION OF NANOMETER SCALE GRAINSIZED Pt ON Si AND PtSi/Si STRUCTURES DEPOSITED BY
HIGH RATE MAGNETRON SPUTTERING
V.Uma and R.Chandramani Ramu
17:40 O4C06-A6 SYNTHESIS, STUDIES AND LUMINESCENT PROPERTIES OFTERBIUM OXIDE DOPED LaMn0.9Zn0.1O3+d
NANOPEROVSKITE BY SOL-GEL METHODA A Alemi, E Karimpour Nahari and H Shokri
18:00 O4C06-A7 STUDIES OF THE NANOSTRUCTURE OF NATURALVEGETABLE FIBERS
Nguyen Van Tri

November 07, Wednesday
Plenary 4 (09:00 – 10:00) (Convention Hall)
Chair: Andrew H. Wang

10:15 PL07-004 STRUCTURAL INSIGHTS INTO THE GATING CONTROL IN
BACTERIAL TRANSPORTERS
Osamu Nureki
Plenary 5 (09:00 – 10:00) (Conference Room)
Chair: Masaki Takata

10:15 PL07-005 SYNTHESIS, CRYSTAL STRUCTURES AND PROPERTIES OFMETAL SILICATES
Kwang-Hwa Lii

Oral Session 5 (10:15-12:15) (Convention Hall)
MS-18a: Cool structures in protein crystallography I
Chair/Co-chair: Kunio Miki, T. P. Singh

10:15 O5A07-M1 CRYSTAL STRUCTURES OF THE COMPLEXES OF C-LOBE
OF LACTOFERRIN WITH NON-STEROIDALANTI-INFLAMMATORY DRUGS (NSAIDS) REVEAL THE
BINDING PATTERN BETWEEN C-LOBE AND NSAIDS WHICH
SUGGESTS A NEW THERAPY FOR MANAGEMENT OFNSAID-INDUCED GASTROPATHY
Sujata Sharma, Rafia Mir, Mau Sinha, Nagendra Singh, and Tej P.
Singh
10:40 O5A07-M2 CRYSTAL STRUCTURES OF NATIVEBACTERIOPHAGE-ASSOCIATED HYALURONATE LYASE
AND ITS COMPLXES WITH LACTOSE AND ASCORBIC ACID
P. Mishra, V. Bhakuni, A. S. Ethayathulla, R. Prem Kumar, N. Singh, S.
Sharma, P. Kaur, A. Srinivasan and T. P. Singh
11:05 O5A07-M3 STRUCTURAL AND MUTATIONAL STUDIES OF
ANTHOCYANIN MALONYLTRANSFERASES ESTABLISH THE
FEATURES OF BAHD ENZYME CATALYSIS
Hideaki Unno, Fumiko Ichimaida, Hirokazu Suzuki, Seiji Takahashi,
Yoshikazu Tanaka, Atsushi Saito, Tokuzo Nishino, Toru Nakayama andMasami Kusunoki

11:30 O5A07-M4 CRYSTAL STRUCTURE OF
N-ACETYLGLUCOSAMINE-PHOSPHATE MUTASE, A
MEMBER OF THE ALPHA-D-PHOSPHOHEXOMUTASESUPERFAMILY
Yuichi Nishitani, Daisuke Maruyama, Tsuyoshi Nonaka, Akiko Kita,
Takaaki A. Fukami, Toshiyuki Mio, Hisafumi Yamada-Okabe, Toshiko
Yamada-Okabe and Kunio Miki
11:55 O5A07-M5 SUBSTRATE SPECIFICITY OF PHOSPHODIESTERASES,STRUCTURAL INSIGHT INTO VIAGRA FUNCTION, AND
STRUCTURE-BASED DESIGN OF DRUGS FOR
INFLAMMATORY DISEASES
Hengming Ke and Huanchen Wang

Oral Session 5 (10:15-11:45) (Conference Room)
MS-10: Science of Organic Materials
Chair/Co-chair: Yoshio Nogami

10:15 O5B07-M1 COMPLEMENTARY STUDIES OF ENZYME-RESISTANT
STARCH - IMPLICATIONS FOR HUMAN HEALTH
A. López-Rubio, M. J. Gidley, A. K. Shrestha, B.M. Flanagan, A. Htoon,
H. Chanvrier, S. Uthayakumaran, I.A.M. Appelqvist, A.R. Bird, D.L.
Topping, M.K. Morell and E.P. Gilbert
10:45 O5B07-M2 CRYSTAL AND MOLECULAR STRUCTURES OFORGANOPHOSPHORUS COMPOUNDS - CONFORMATION
AND BIOLOGICAL ACTIVITY OF HETEROCYCLIC
MOLECULES
Musali Krishnaiah and Jadaprolu Radha Krishna
11:15 O5B07-M3 IXS STUDY OF EXCITON PROPERTIES IN ORGANIC
MOLECULES
Ke YangOral Session 5 (10:15-12:15) (Room 103)MS-01: Neutron sources, instrumentation, and applications
Chair/Co-chair: Brendan Kennedy, Mahn Won Kim

10:15 O5C07-M1 HIGH SPEED NEUTRON DIFFRACTION AT THE OPALRESEARCH REACTOR: THE WOMBAT INSTRUMENT
A.J. Studer, M. Avdeev, M.M. Elcombe, J.R. Hester, and V.K. Peterson
10:45 O5C07-M2 WATER-REDISPERSIBLE SINGLE WALL CARBON
NANOTUBES AND 40M SANS INSTRUMENT DEVELOPMENTAT HANARO
Sung-Min Choi, Tae-Hwan Kim, Changwoo Doe , Young-Soo Han andSteven R Kline
11:15 O5C07-M3 FIRST RESULTS FROM THE NEW OPAL RESEARCH
REACTORR. A. Robinson
11:45 O5C07-M4 VERSATILE NEUTRON DIFFRACTOMETR AT J-PARC- IBARAKI MATERIALS DESIGN DIFFRACTOMETER T. Ishigaki, A. Hoshikawa, M. Yonemura, F. Shikanai, T. Morishima, T.
Kamiyama, K. Aizawa, T. Sakuma, Y. Tomota, M. Arai, M. Hayashi, K.
Ebata, Y. Takano, K. Komatsuzaki, H. Asano, Y. Takano, T. Kasao

Oral Session 6 (13:30-15:30) (Convention Hall)
MS-18b: Cool structures in protein crystallography II
Chair/Co-chair: Mitchell Guss, Hanna Yuan

13:30 O6A07-A1 TACKLING A MUNC-Y PUZZLE: STRUCTURE OF THE
MUNC18C PROTEIN
Jennifer L Martin, Shu-Hong Hu, Catherine F. Latham, Christine L. Gee,
David E. James
13:55 O6A07-A2 CRYSTAL STRUCTURE OF DSREFH, A PROTEIN ESSENTIALFOR OXIDATION OF STORED SULFUR IN THE PURPLE
SULFUR BACTERIUM ALLOCHROMATIUM VINOSUM
Dong Hae Shin
14:20 O6A07-A3 STRUCTURAL AND COMPUTATIONAL STUDIES ON TYPE II
RIPs
Alok Sharma, A.A. Jeyaprakash, M.J.Swamy and M.Vijayan
14:45 O6A07-A4 STRUCTURAL STUDIES OF THE CPX PATHWAYH
ACTIVATOR NLPE ON THE OUTER MEMBRANE OF
ESCHERICHIA COLI
Yu Hirano, Md. Motarab Hossain, Kazuki Takeda, Hajime Tokuda andKunio Miki
15:10 O6A07-A5 CRYSTAL STRUCTURE OF IL-15/IL-15RALPHA COMPLEX
Mami Chirifu, Chiharu Hayashi, Teruya Nakamura, Sachiko Toma,
Tsuyoshi Shuto, Hirofumi Kai, Yuriko Yamagata, Simon J. Davis andShinji Ikemizu

Oral Session 6 (13:30-15:30) (Conference Room)MS-11: Dynamic aspects of molecular crystals
Chair/Co-chair: Keiichiro Ogawa, Roger Bishop

13:30 O6B07-A1 IXS STUDY OF EXCITATION PROPERTIES OF ORGANIC
MOLECULAR CRYSTALS AND SIMPLE MOLECULES
Binping Xie, Ke Yang, Y. Q. Cai, N. Hiraoka, Donglai Feng
13:50 O6B07-A2 MOLECULAR DYNAMICS IN SEVERAL CHLORINECOMPOUNDS ON THE BASIS OF X-RAY THERMALPARAMETER, IR/RAMAN AND NQR DATA
L.Ramu and R.Chandramani.
14:10 O6B07-A3 VAPOR INDUCED GUEST EXCHANGE OF ORGANICINCLUSION CRYSTAL
Hidehiro Uekusa, Yasunari Ashida, Kotaro Fujii
14:30 O6B07-A4 CONCERTED STRUCTURAL CHANGE AND
PHOTOCHROMISM OF TRANS-BIINDENILIDENEDIONDERIVATIVES
Akiko Sekine, Kumiko Aruga, Hidehiro Uekusa, Katsuya Souno andKoichi Tanaka
14:50 O6B07-A5 CRYSTAL STRUCTURE ANALYSES OF CIS/TRANS
PHOTOISOMERIZATIONS
Jun Harada, Mayuko Harakawa and Keiichiro Ogawa
15:10 O6B07-A6 CRYSTALLINE STATE PHOTO ISOMERIZATION OF ANORGARNO-DIRHODIUM DITHIONITE COMPLEX
Koshiro Toriumi, Hiroshi Kanamono, Shouichi Hashimoto, Yoshiki
Ozawa, Minoru Mitsumi, Hidetaka Nakai, Yousuke Miyano, Yoshihito
Hayashi, and Kiyoshi IsobeOral Session 6 (13:30-15:30) (Room 103)
MS-03: Advances in powder X-ray and neutron diffraction
Chair/Co-chair: Takashi Kamiyama, Andrew Studer

13:30 O6C07-A1 STRUCTURE DETERMINATION FROM HIGH RESOLUTIONSYNCHROTRON POWDER DIFFRACTION DATA
Eiji Nishibori, Shinobu Aoyagi, and Makoto Sakata
14:00 O6C07-A2 STRUCTURAL STUDIES EMPLOYING HIGH ENERGY
POWDER DIFFRACTION
Peter L. Lee
14:30 O6C07-A3 EXPECTING THE UNEXPECTED. PHASE TRANSITIONS IN
MANGANESE PEROVSKITES
Brendan J Kennedy, and Zhaoming Zhang
14:50 O6C07-A4 MORPHOTROPIC PHASE BOUNDARY LIKE
CHARACTERISTIC IN A LEAD-FREE, AND
NON-FERROELECTRIC SYSTEM (1-x)NaNbO3-xCaTiO3
Saurabh Tripathi, Rajeev Ranjan, Dhananjai Pandey, Sanjay Kumar
Mishra and P.S.R. Krishna
15:10 O6C07-A5 SYNCHROTRON RADIATION X-RAY DIFFRACTION AND
SPECTROSCOPIC ELLIPSOMETRY INVESTIGATION OF Si3N4ON Si FOR SUB-50NM Si-IC APPLICATIONSZhe Chuan Feng, Li-Chi Cheng, Chu-Wan Huang, Ying-Lang Wang, and
Hwo-Shuenn Sheu
Plenary 6 (16:00 – 17:00) (Convention Hall)
Chair: Peter M. Colman

10:15 PL07-006 MECHANISM OF PROGRAMMED CELL DEATH THROUGHSTRUCTURAL BIOLOGY
Yigong Shi

Poster Sessions
November 05, Monday
P05-001

ENGINEERING MATERIALS DIFFRACTOMETER AT J-PARC
Stefanus Harjo, Atsushi Moriai, Kentaro Suzuya, Kazuya Aizawa, Kaori
Shirakihara, Yo Tomota, Koichi Akita, Masatoshi Arai, Yukio Morii

P05-002

CURRENT STATUS OF IBARAKI BIOLOGICAL CRYSTALDIFFRACTOMETER IN J-PARC
Ichiro Tanaka, Takashi Ohhara, Kazuo Kurihara, Katsuhiro Kusaka, Takaaki
Hosoya, Katsuaki Tomoyori, Nobuo Niimura, Tomoji Ozeki, Kazuya Aizawa,
Masatoshi Arai, Yukio Morii, Makoto Hayashi, Kazuhiro Ebara and Yoshiki
TakanoP05-003

PROGRESS REPORT ON SUPER HIGH RESOLUTION POWDERDIFFRACTOMETER IN J-PARC
Shuki Torii, Yasuo Kobayashi, Junichi Suzuki, Hidenori Sagehashi, Minoru
Nagai, Kenichi Oikawa, Kazuhiro Mori, Masao Yonemura, Toru Ishigaki and
Takashi Kamiyama

P05-014SHORT-RANGE ORDER PARAMETERS OF AsGeSe GLASSES
A.H. Moharram, M. A. Hefni and A.M. Abdel-Baset

P05-015

STRUCTURAL AND SPECTROSCOPIC STUDIES OF CATIONDISORDER IN SOME BI CONTAINING PYROCHLORES
Qingdi Zhou, Brendan J. Kennedy

P05-016APPLICATION OF LARGE RADIUS IMAGING PLATE CAMERA FORSYNCHROTRON POWDER X-RAY DIFFRACTION TO STRUCTURAL
PHASE TRANSITION STUDIES
Masahiko Tanaka and Yoshio Katsuya

P05-017

MORPHOTROPIC PHASE BOUNDARY IN (1-x)BiFeO3-xPbTiO3 :PHASE COEXISTENCE REGION AND UNUSUALLY LARGETETRAGONALITY
Shuvrajyoti Bhattacharjee, Saurabh Tripathi and Dhananjai Pandey

P05-018

DISORDER OF Pb ATOM IN CUBIC PHASE OF PEROVSKITE-TYPE
SOLID SOLUTIONS PZT AND PZN-PT
Yoshihiro Terado, Chikako Moriyoshi, Yoshihiro Kuroiwa, Yasuhisa Yamamura
and Makoto Iwata

P05-019

X-RAY STRESS ANALYSIS FOR FIBER TEXTURES BASED ON
SYMMETRY IN RECIPROCAL LATTICE SPACERyouichi Yokoyama, and Jimpei Harada
P05-020

GENERALIZED METHOD OF STRUCTURE ANALYSIS FOR MICROIMPERFECT CRYSTALS USING SR.
Ken-ichiro Yamamoto, Yoshio Nogami, Naoshi Ikeda, Takayoshi Ito, Toru
Matsuura, Taku Tsuneta, Satoshi Tanda

P05-021

SYNTHESIS, REACTIVITY AND 3-D STRUCTURAL DETERMINATIONBY POWDER DIFFRACTION ON MOLYBDOPTERIN COMPLEX
Jey Jau Lee, Hwo-Shuenn Sheu,Keng S. Liang , Baidyanath Ghosh and Parag
Sinchan Roy

P05-022SOLVING ZEOLITE STRUCTURES FROM POWDER DATA USINGDENSITY BUILDING FUNCTIONS AND HISTOGRAM MATCHING
Chris Gilmore and Douglas Dorset

P05-023

BIO-MEMBRANE STRUCTURE PROBED BY THE LAMELLAR X-RAY
DIFFRACTION AND THE SMALL ANGLE X-RAY SCATTERING AT
NSRRC
Ming-Tao Lee, Yu-Shan Huang, U-Ser Jeng, Ying-Huang Lai, and Ya-Sen Sun

P05-024

ANOMALOUS X-RAY SCATTERING AND ABSORPTIONSPECTROSCOPY INVESTIGATE THE MORPHOLOGY OF FePt
MONOLAYER NANOPARTICLE ON SURFACE MODIFIEDSUBSTRATES WITH AU OVERLAYER
Tzu-Wen Huang, Kuan-Li Yu, Yen-Fa Liao and Chih-Hao Lee

P05-025

SPINODAL CRYSTALLIZATION KINETICS ON SUPERCOOLEDLIQUID OF POLY(TRIMETHYLENE TEREPHTHALATE)
Wei-Tsung Chuang, Hwo-Shuenn Sheu,U-Ser Jeng, Po-Da HongP05-026

AN INSTRUMENT FOR TIME RESOLVED AND ANOMALOUS
SIMULTANEOUS SMALL AND WIDE ANGLE X-RAY SCATTERING(SWAXS) AT THE NSRRC
Chiu-Hun Su, Ying-Huang Lai, Ya-Sen Sun, U-Ser Jeng, Jhih-Min Lin,
Tsang-Lang Lin, Yu-Shan Huang, Hwo-Sheunn Sheu, Wei-Tsung Chuang,
Chia-Hung Hsu, Ming-Tao Lee, Keng S. Liang

P05-027

SOLUTION SAXS AND NMR ON DOMAIN ORIENTATION AND
BINDING OF THE COMPONENTS OF THE HUMAN BCKD COMPLEX
Chi-Fon Chang, Yu-Shan Huang, U-Ser Jeng

P05-028

EXPERIMENTAL ELECTRON DENSITIES AND MOLECULAR
INTERACTIONS: INTER-MOLECULAR HYDROGEN BONDING
Azadeh Matin, Thanh Ha Nguyen, Jane Hanrahan and David Hibbs

P05-029

EXPERIMENTAL ELECTRON DENSITIES AND MOLECULAR
INTERACTIONS: INTER-MOLECULAR Π-STACKINGINTERACTIONS
Thanh Ha Nguyen and David Hibbs

P05-030

Yb-DOPING EFFECT AND TEMPERATURE DEPENDENCE IN CoSb3
SKUTTERUDITE STRUCTURE
Atsuko Ohno, Satoshi Sasaki, Eiji Nishibori, Shinobu Aoyagi, Makoto Sakata and
Bo Brummerstedt Iversen

P05-031

SITE PREFERENCE AND DOPING EFFECT IN(Hg,Pb)(Ba,Sr)2Ca2Cu3O8+δ SUPERCONDUCTORS
Satoshi Sasaki and Kouji Yamawaki

P05-032

CLOSE CL···CL CONTACT: IS IT ATTRACTIVE OR REPULSIVE?
Daisuke Hashizume

P05-033

THEORETICAL CALCULATION OF XMCD SPECTRA AT K-EDGE Ni
AND Fe SPINEL FERITE
Koichi Ohkubo, Takeshi Toyoda

P05-034

ELECTRONIC STRUCTURE OF MERCURIC IODIDE USINGCOMPTON SCATTERING TECHNIQUE
M. Sharma, Gulzar Ahmed and B. L. Ahuja

P05-035

CHARGE DENSITY DISTRIBUTION AND BOND
CHARACTERIZATION ON COMPLEX MN(H2O)2NI(CN)4⋅3H2O
Lai-Chin Wu, I-Jui Hsu, Gene-Hsiang Lee, Yu Wang

P05-036

CHEMICAL BONDING AND INTERMOLECULAR INTERACTIONS OFA NICKEL(II) COMPLEX
Yu-Chun Chuang, Yu Wang, Gene-Hsiang Lee, Ben-Jie Liaw, Chen-Wei Liu

P05-037

MIXED LIGAND COPPER(I) COMPLEXES OF
TRIPHENYLPHOSPHINE AND PHENYLTHAIOUREA
Ruthairat Nimthong, Chaveng Pakawatchai, Yupa Thunyasirikul and Saowanit
Saithong

P05-038

INVESTIGATION OF ELECTRON DENSITY DISTRIBUTION IN
ANATASE (TiO2) WITH- AND WITHOUT UV-IRRADIATION
Ken-ichi Ito and Hiroki Okudera

P05-039

CHARGE DENSITY STUDIES ON HETEROBIMETALLIC
PHOSPHIDO-BRIDGED Mo AND W COMPLEXES
Chi-Rung Lee, I-Jui Hsu, Hsiu-Mei Lin and Shin-Guang Shyu

P05-040

EXPERIMENTAL CHARGE DENSITY STUDY ON A Fe(II) COMPLEXAT HIGH SPIN AND LOW SPIN STATES
Chou-Fu Sheu, Che-Hsiu Shih, Szu-Miao Chen, Yu-Chun Chuang, Gene-Hsiang
Lee, Yu-Shan Huang, Kuan-Li Yu, Yu Wang

P05-083

PRELIMINARY STRUCTURAL REFINEMENTS AND A NEWSYNTHETIC ROUTE TO δ-Bi2O3-RELATED PHASES IN THE Bi-W-O,
Bi-Mo-O, Bi-Ta-O AND Bi-Nb-O SYSTEMS
Neeraj Sharma, Rene Macquart and Chris D. Ling

P05-084

INSIGHT INTO THE STABILITY OF TETRAGONAL AND
RHOMBOHEDRAL PHASES IN DOUBLE PEROVSKITES
P. J. Saines, J. Spencer and B. J. Kennedy

P05-085

A STUDY OF STRONTIUM, ALUMINIUM AND INDIUM TUNGSTEN
BRONZESM. S. Rahman and A. Hussain

P05-086

CRYSTAL STRUCTURE AND HABIT OF CaIrO3
Masahiko Sugahara, Akira Yoshiasa, Takafumi Hashimoto, Syunsuke Sakai,
Akihiko Nakatsuka, Maki Okube and Akira Yoneda

P05-087

SYNCHROTRON POWDER DIFFRACTION STUDY ON GAMMAAl2O3
Seiichi Matsuda, Takashi Ida, Kazuhiro Asai and Hisashi Hibino

P05-088

STRUCTURE DETERMINATION OF HYBRID STRUCTURES FOUND
IN BaTiO3 CRYSTAL
Y. Yoshimura, K. Sone, H. Sumiyoshi, T. Kondo, A. Kojima, K. Tozaki

P05-089

DIFFRACTION AND XAFS STUDY OF AgI UNDER HIGH PRESSURE
AND HIGH TEMPERATURE
Akira Yoshiasa, Hiroshi Arima, Hiroshi Fukui, Osamu Ohtaka, Maki Okube, andYoshinori Katayama

P05-090

CAGE SUBSTRUCTURES AND SITE OCCUPANCIES IN CLATHRATECOMPOUNDS,La3Pd20T6 (T = Si And Ge)
Y. Matsushita, A. Satoa, H. Kobayashi, A. Dönni, H. Kitazawa, F. Izumi, Y.
Nemoto, T. Goto, M. Kaneko, S. Sasaki, and N. Kishimoto

P05-091

MODULATED STRUCTURES IN THE AMOB2O5 FAMILY FROMVARIABLE TEMPERATURE X-RAY POWDER DIFFRACTION DATA
Siegbert Schmid

P05-092

RXMS STUDY ON A MAGNETIC HELIX OF BaTiCoFe10O19
Maki Okube, Seiji Ohsawa, Takeshi Toyoda, Takeharu Mori, Satoshi Sasaki

P05-093

SODIUM ARRANGEMENT IN NAXMO2 P2 STRUCTURE AS A
FUNCTION OF TEMPERATURE, TRANSITION METAL TYPE, AND
SODIUM STOICHIOMETRY
Angélique Jarry, Maxim Avdeev

P05-094

UNUSUAL SITE PREFERENCE OF BORON IN SYNTHETIC
MgAl2-xBxO4 SPINEL (x = 0.11 and 0.13) UNDER HIGH PRESSURE
Shunsuke Sakai,Akira Yoshiasa, Takafumi Hashimoto, Akihiko Nakatsuka,
Kazumasa Sugiyama, Maki Okube, and Eiji Ito

P05-095

PHOTOISOMERIZATION OF RUTHENIUM DIMETHYL SULFOXIDECOMPLEXES AND THEIR CRYSTAL STRUCTURES
Yuji Karakane, Hidehiro Uekusa

P05-096

CRYSTALLOGRAPHIC STUDY ON DEHYDRATION BEHAVIOR OF
CHABAZITE
Akihiko Nakatsuka, Hironao Okada, Keiko Fujiwara, Noriaki Nakayama andTadato Mizota

P05-097

TEMPERATURE DEPENDENCE OF CRYSTAL STRUCTURE OFPYROPE GARNET
Mami Shimokawa, Akihiko Nakatsuka, Makio Ohkawa and Noriaki Nakayama

P05-098

EVOLUTION OF CORUNDUM STRUCTURE AT HIGHTEMPERATURES
S. Kondo, K. Tateishi, H. Hibino and N. Ishizawa

P05-099

PHASE TRANSITION OF Gd3RuO7
K. Okada, S. Kondo, T. Suwa and N. Ishizawa

P05-100

ANOMALOUS STRUCTURAL PHASE TRANSITION ABOVE LIQUIDNITROGEN TEMPERATURE IN THE MULTIFERROIC PEROVSKITE
Dy(Mn0.5Fe0.5)O3
Fu-Kuo Chiang , Fei-Ting Huang, and Ming-Wen Chu

P05-101

SYNTHESIS AND STRUCTURE OF FERROMAGNETIC RUTILE
Takashi Mochiku, Kazuhiro Yamaki, Natsumi Shimizu, Akinori Hoshikawa,
Hiroki Fujii, Katsura Yamada, Shinji Itoh, Itsuhiro Kakeya, Kazuo Kadowaki and
Kazuto Hirata

P05-102

TEMPERATURE AND PRESSURE INDUCED TRANSITIONS OFPEROVSKITES ABX3 TO OTHER STRUCTURE TYPES
Maxim Avdeev, Sergey Yakovlev

P05-103

SYNTHESIS AND CHARACTERIZATION OF SERIESHETERMETALLIC COORDINATION POLYMER MaxMb1-x(tda)H2O(Ma, Mb=Zn, Co AND Ni, 0<x<1 )Ming-Cheng Wu and Chi-Shen Lee

P05-104

SYNTHESIS AND CHARACTERIZATION OF NEW QUATERNARYSELENIDE In1.91Pb4Bi4.09Se13
Ming-Fang Wang and Chi-Shen Lee

P05-105

MAGNETIC PROPERTIES OF DINUCLEAR ONE-DIMENSIONALCOMPLEXES WITH TRIAZOLE BASED LIGANDS
S. M. Chen, C. F. Sheu, Y. S. Wen, and Y. Wang

P05-106

INVESTIGATION OF THE ELECTRONIC STRUCTURE OF
LANTHANIDE ZIRCONATES
Richard Clements, Brendan Kennedy, Chris Ling, Anton Stampfl

P05-107

STRUCTURAL PHASE TRANSITION ACCOMPANIED BYMETAL-INSULATOR TRANSITION IN HOLLANDITE VANADATE
Masahiko Isobe, Shigenori Koishi and Yutaka Ueda

P05-108

PSEUDO-MEROHEDRAL TWINNING : HOW TO TREAT A SIX-FOLD
TWIN
Martin Adam, Anita Coetzee, Leo Straver and Rob Hooft

P05-109

THE CRYSTAL STRUCTURE OF GUEST-REMOVEDMELANOPHLOGITE
Akihiro Ida, Kuniaki Kihara and Shuhei Fujinami

P05-110Structure REFINEMENT OF THE SAMPLE OBTAINED BY NASA’S
STARDUST MISSION
Kazumasa Ohsumi, Kenji Hagiya, Takashi Mikouchi and Michael Zolensky

P05-111

CRYSTAL STRUCTURE AND PHOTO-EXCITATION ENERGYMIGRATION IN CRYSTALS OF DOUBLE-COMPLEX SALTS
M[Ru(bpy)3][CrxAl1-x(ox)3] (M+ = Na+, Li+; 0≦x≦1)
Satoshi Ishii, Tomoko Nakaguchi, Takuhiro Otsuka and Youkoh Kaizu

P05-112STRUCTURE AND MAGNETIC PROPERTY OF CYANIDE BRIDGE
MOLECULAR SQUARE AND MOLECULAR SQUARE CHAIN
Chin-Lin Yang, Yu Wang

P05-113

LIGHT AND THERMAL INDUCED META-STABLE STATESTRUCTURE OF SPIN CROSSOVER COMPOUND {Fe(abpt)2[N(CN)2]2}
C. F. Sheu, S. Pillet, S. M. Chen, Y. C. Lin, I. J. Hsu, G. H. Lee, Y. H. Liu, C.
Lecomte, Y. Wang

P05-114

STRUCTURAL STUDIES OF BIOLOGICALLY IMPORTANT
HETEROCYCLIC COMPOUNDSPeriyasamy Murugan, Munusamy Thirumavalavan, Tian-Huey Lu, Kuo Chu
Hwang

P05-115

HYDROGEN BONDING INTERACTIONS AND SHEET-LIKE
STRUCTURES IN NICOTINAMIDE COMPLEXES
S. Athimoolam and S. Natarajan

P05-116

PYRIDOXINIUM NITRATE AND TRICHLOROACETATE
S. Athimoolam and S. Natarajan

P05-117

SYNTHESIS, GROWTH AND CHARACTERIZATION OF NEW
ORGANIC NONLINEAR OPTICAL CHALCONE DERIVATIVESSINGLE CRYSTALS
P. S. Patil , S. M. Dharmaprakash , G. Bhagavannarayana and Hoong-Kun Fun

P05-118

CRYSTAL STRUCTURES OF MONO- AND DI-SUBSTITUTEDFERROCENE DERIVATIVES
Naotake Nakamura, Kazuya Hiro and Takeshi Takamatsu

P05-119

SUPRAMOLECULAR HYDROGEN-BONDING NETWORKS IN
ADENINIUM SALTS
Balasubramanian Sridhar and Krishnan Ravikumar

P05-120

CRYSTAL OF 6-[BIS(2-CHLOROETHYL)AMINO]-12-OXO-DIBENZO[d,g] [1,3,2]DIOXAPHOSPHOCIN 6-OXIDE
Jadaprolu Radha Krishna, Musali Krishnaiah, Vedavati G. Puranik

P05-121

CRYSTAL STRUCTURE OF 4-(4-CHLORO-PHENYL)-5-PHENYLISOXAZOLE
A.K.Balaji, J.Radha Krishna, M.Krishnaiah, Than Zaw Oo, Thetmar Win and Pho
Kaung

P05-122

MOLECULAR RECOGNITION OF 2-PHENOXYBUTANOIC ACID BYCHIRAL AROMATIC AMINES
Ryoma Aoki, Yukio Takahashi and Isao Fujii

P05-123

STRUCTURE DETERMINATION OF PENTACENE DERIVATIVE BY
SYNCHROTRON POWDER DIFFRACTION DATA
Hwo-Shuenn Sheu, Wei-Ju Shih, Wei-Tsung Chuang, and Yu-Tai Tao

P05-124

PREPARATION, PROPETIES, AND STRUCTURAL STUDIES OF[MCl(diphosphine)]2 (M = Rh, Ir; diphosphine = BINAP)
Tsuneaki Yamagata, Aika Iseki, Kazunori Hoshida, Hiromitsu Nagata, KazuhideTani, and Kazushi Mashima

P05-125

HIGH RESOLUTION CRYSTAL STRUCTURE OF A BLUECOMMERININ PIGMENT
Naohiro Matsugaki, Masaaki Shiono, and Kosaku Takeda

P05-126

SOLID-STATE PHOTODIMERIZATION OF 6-METHYLCOUMARIN
AND IT’S INCLUSION COMPLEXES, INVESTIGATED BY Ab INITIOPOWDER CRYSTAL STRUCTURE ANALYSIS
Kotaro Fujii, Hidehiro Uekusa, Shunsuke Tanigawa, Shinji Toyota, Fumio Toda

P05-127

GUEST EXCHANGE MECHANISM OF ORGANIC INCLUSIONCRYSTAL INVESTIGATED BY POWDER X-RAY DIFFRACTIONANALYSIS
Yasunari Ashida, Hidehiro Uekusa, Natsuki Amanokura, and Masami Kaneko

P05-128

HYDROGEN BONDING DYNAMICS OF THE STRUCTURE
4,5-DIMETHYL-N-(2-METHYL PHENYL)-2-{[(1E)-3,4,5-TRIMETHOXYPHENYLMETHYLENE] AMINO} THIOPHENE-3-CARBOXAMIDE
Vasu,a K. A. Nirmala,b Deepak Chopra,c S. Mohand and J. Saravanan

P05-129

THE PHICIAL PROPERTIES OF S DOPANT IN InP UNDERHIGH-PRESSURE BY ADX AND RAMAN METHDOS
Yen-Ting Liu, Chih-Ming Lin and Hwo-Shuenn Sheu

P05-130

DIMERIZATION IS IMPORTANT FOR THE GTPASE ACTIVITY OF
CHLOROPLAST TRANSLOCON COMPONENTS ATTOC33 AND
PSTOC159
Yi-Hung Yeh, Muppuru M. Kesavulu, Hsou-min Li, Shu-Zon Wu, Yuh-Ju Sun,
Emadeldin H. E. Konozy and Chwan-Deng Hsiao

P05-131

EFFECTS OF TERMINAL SUBSTITUENTS AND SEED CRYSTALS ON
THE MODE OF POLYMORPHIC TRANSITION INDUCING
PREFERENTIAL ENRICHMENT
Masahiro Horiguchi, Shinichiro Okuhara, Eiji Shimano, Daisuke Fujimoto,
Hiroki Takahashi, Hirohito Tsue, and Rui Tamura

P05-132

STRUCTURE-ASSISTED DISCOVERY OF HELICOBACTER PYLORISHIKIMATE KINASE (HPSK) INHIBITORS
Wen-Chi Cheng, Yen-Fu Chen, Jinn-Moon Yang and Wen-Ching Wang

P05-133

AB INITIO STRUCTURAL DEFERMINATION OF PHARMACEUTICAL
COCRYSTAL FROM POWDER X-RAY DIFFRACTION DATA
Chihiro Itoga, Kotaro Fujii, Hidehiro Uekusa, Noriyuki Takata, Koji Shiraki

P05-134PROBING INTER MOLECULAR INTERACTIONS IN
FUNCTIONALISED THIOPHENES
K.A.Nirmala, Vasu

P05-135

MOLECULAR RECOGNITION OF SYNEPHRINE BY CHIRALORGANIC ACIDSTaira Kimino, Yukio Takahashi, and Isao Fujii

P05-136

CRYSTAL STRUCTURE OF
2-PHENYL-2,3-DIHYDRO-4H-CHROMEN-4-ONE
Nongnaphat Khosavithitkul, Kenneth J. Haller

P05-137

CRYSTAL STRUCTURE OF ‘N-(4-METHOXYPHENYL)2-{[(1E)-(4-METHYLPHENYL)
METHYLENE]AMINO}-4,5,6,7-TETRAHYDRO-THIENO[2,3-C]PYRIDI
NE-3-CARBOXAMIDE’
G. N. Anilkumar, M. K. Kokila , Puttaraja, S. Mohan and J. Saravanan

P05-138

CRYSTAL STRUCTURE OF ‘N-(4-METHOXYPHENYL)2-{[(1E)-(4-METHYLPHENYL)
METHYLENE]AMINO}-4,5,6,7-TETRAHYDRO-THIENO[2,3-C]PYRIDI
NE-3-CARBOXAMIDE’
G. N. Anilkumar , M. K. Kokila, Puttaraja , S. Mohan and J. Saravanan

P05-139

CRYSTAL CHEMISTRY OF CYCLODEXTRINS AND THEIRINCLUSION COMPOUNDS WITH BIOLOGICALLY-ACTIVE GUESTS
Mino R CairaP05-140

CRYSTAL STRUCTURE OF‘2-AMINO-N-(2-METHOXYPHENYL)-5,6,7,8-TETRAHYDRO-4H-CYCLOHEPTA[B]THIOPHENE-3-CARBOXAMIDE’
K. Chandra Kumar , M. K. Kokila, Puttaraja, S. Mohan and J. Saravanan

P05-141

HIGH RESOLUTION, HIGH THROUGHPUT X-RAY POWDERDIFFRACTION EXPERIMENTS AND DATA ANALYSIS
A. Stefanovic, D. Beckers, T. Degen, S. Prugovečki

P05-169

RNA DEGRADATION BY ESCHERICHIA COLI POLYNUCLEOTIDEPHOSPHORYLASE
Zhonghao Shi, Wei-Jen Yang, Kin-Fu Chak and Hanna S. Yuan

P05-170

UNDERSTANDING OF D-STAGGER IN COLLAGEN FIBERS BASEDON THE 7/2-HELICAL STRUCTURE AND AMINO ACID SEQUENCE
Koichi Masakiyo, Tatsuya Kawaguchi and Kenji Okuyama

P05-171

X-RAY CRYSTAL STRUCTURE ANALYSIS OF HEMOGLOBIN FROMDOMESTIC PIGEON (COLUMBA LIVIA) AT 1.44Å RESOLUTION
P.Charles, K.Neelagandan, S.Sundaresan, Jürgen J. Müller ,Udo Heinemannand M.N.Ponnuswamy

P05-172

SMALL-ANGLE X-RAY SCATTERING EXPERIMENTS TO
DETERMINE THE STRUCTURAL TRANSITIONS IN THE INSULIN
RECEPTOR ECTODOMAIN UPON INSULIN BINDING
Andrew E. Whitten, Jill Trewhella, Colin W. Ward and Michael C. Lawrence

P05-173

CRYSTAL STRUCTURE OF THE HUMAN FOXO3A-DBD/DNACOMPLEX SUGGESTS THE EFFECTS OF POST-TRANSLATIONALMODIFICATION
Kuang-Lei Tsai, Yuh-Ju Sun, Cheng-Yang Huang, Jer-Yen Yang, Mien-Chie
Hung and Chwan-Deng Hsiao

P05-174

CRYSTAL STRUCTURE OF HUMAN TUDOR-SN AND IMPLICATIONOF ITS ROLES IN RNA INTERFERENCE
Chia-Lung Li and Hanna S. Yuan

P05-175

CRYSTAL STRUCTURE OF DNAC REPLICATIVE DNA HELICASEREVEALS THE MECHANISM OF HEXAMERIZATION AND POSSIBLE
PROTEIN-PROTEIN INTERACTIONS NETWORKCheng-Yang Huang, Kuang-Lei Tsai, Wei-Ti Chen, Chwan-Deng Hsiao

P05-176

PYROCOCCUS HORIKOSHII ARGINYL-TRNA SYNTHETASELACKING ADDITIONAL N-TERMINAL DOMAIN WITH
AMINOACYLATION ACTIVITY
Emiko Uchikawa, Shun-ichi Sekine, Shigeyuki Yokoyama, and Michiko Konno

P05-177

CRYSTAL STRUCTURE OF 5-METHYLTHIORIBOSE 1-PHOSPHATEISOMERASE PRODUCT COMPLEX FROM BACILLUS SUBTILIS:IMPLICATIONS FOR CATALYTIC MECHANISMHaruka Tamura, Yohtaro Saito, Hiroki Ashida, Tsuyoshi Inoue, Yasushi Kai,
Akiho Yokota, and Hiroyoshi Matsumura

P05-178

STRUCTURAL DIFFERENCE BETWEEN RICE AND RED ALGARUBISCO COMPLEXED WITH SULFATE
Yasuhiro Komura, Hiroyoshi Matsumura, Hiroyuki Ishida, Hiroki Ashida, Eiichi
Mizohata, Tsuyoshi Inoue, Amane Makino, Tadahiko Mae, Akiho Yokota,
Yasushi Kai

P05-179

CRYSTAL STRUCTURE OF IcaR, A REPRESSOR OF THE TetR FAMILYIMPLICATED IN BIOFILM FORMATION IN STAPHYLOCOCCUS
EPIDERMIDIS
Wen-Yih Jeng, Tzu-Ping Ko, Rey-Ting Guo, Chien-Liang Liu, Chia-I Liu,
Hui-Lin Shr and Andrew H.-J. Wang

P05-180

STRUCTURAL BASIS FOR THE DISTINCTIVE SUBCHLOROPLAST
LOCATION OF THREE MAIZE LEAF FERREDOXIN:NADPHOXIDOREDUCTASES
N. Muraki, G. T. Hanke, T. Shiba, T. Hase, and G. Kurisu

P05-181

PREPARATION, CRYSTALLIZATION AND PRELIMINARYCRYSTALLOGRAPHIC ANALYSIS OF OLD YELLOW ENZYME FROMTRYPANOSOMA CRUZ
Naoki Okamoto, Shigeru Sugiyama, Keiji Tokuoka, Nahoko Uchiyama, Yousuke
Okano, Hiroyoshi Matsumura, Yasushi Kai, Koji Inaka, Yoshihiro Urade andTsuyoshi Inoue

P05-182

CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF THE
CERAMIDASE FROM PSEUDOMONAS AERUGINOSA
Hiroyuki Okano,Koji Kambayashi, Nozomu Okino, Hatsumi Monjusyo,
Yoshimitsu Kakuta Makoto Ito and Tsuyoshi Inoue

P05-183

WHY DO NITRILASES NEED TO FORM HELICES TO BE ACTIVE?
Trevor Sewell, Serah Kimani and Muhammed Sayed

P05-184

THE PRESENT STATUS OF ACCURATE STRUCTURE REFINEMENTS
FOR MACRO MOLECULES BY THE MAXIMUM ENTROPY METHOD
Makoto Sakata, Eiji Nishibori, , TakahiroNakamura, Masanori Arimoto, Shinobu
Aoyagi, Hideo Ago, Masashi Miyano and Toshikazu Ebiszaki

P05-185

CRYSTALLIZATION OF THE COLD-ADAPTED ARABINANASE FROMPENICILLIUM CRYSOGENUM
Kyoko Ikoma, Yuri Sogabe, Asako Yamaguchi, Tetsuko Nakaniwa, Takayoshi
Kinoshita, Tatsuji Sakamoto, Hideshi Ihara and Toshiji Tada

P05-186

RIETVELD ANALYSIS SOFTWARE FOR J-PARC
Ryoko Oishi, Masao Yonemura, Shuki Torii, Akinori Hoshikawa, Toru Ishigaki,
Yuichiro Nishimaki, Takahiro Morishima and Takashi Kamiyama

P05-187

VISUALISING AND QUANTIFYING INTERMOLECULAR
INTERACTIONS WITH HIRSHFELD SURFACES AND
CRYSTALEXPLORER
Joshua J. McKinnon, Mark A. Spackman, and Dylan Jayatilaka

P05-188

THE EFFECT OF AMINO ACIDS AND AMINO ACID DERIVATIVES ON
PROTEIN CRYSTALLIZATION
L. Ito, T. Kobayashi, K. Shiraki, T. Narukawa, A. Oosuka and H. Yamaguchi

P05-189

COMPUTATIONAL METHODOLOGY TO ANALYZE VARIOUS
DEFECTS IN CUBIC CRYSTALS
S. T. Nakagawa

P05-190

DDLM: A NEW DICTIONARY LANGUAGE SUBMITTED TO COMCIFSFOR APPROVAL
Nick Spadaccini, John Westbrook, and Syd Hall

P05-191

MULTIPLE STRATEGIES IN HIGH-THROUGHPUT CLONING,
EXPRESSION AND PRODUCTION OF RECOMBINANT PROTEINSFOR STRUCTURAL PROTEOMICS
Hao Xu, Jin-Yi Zhu, Mervin Zhao, Quentin Florence, James Tucker Swindell
II, Bret Dillard, Dayong Zhou, Angela Yang, John Rose, and Bi-Cheng Wang

November 06, Tuesday
P06-004

PERFORMANCE OF THE HIGH-THROUGHPUT PROTEIN
CRYSTALLOGRAPHY BEAMLINE BL13B1 AT THE NSRRC
Chun-Hsiung Chao, Yuch-Chen Jean, Yu-Shan Huang, Chien-Chang Tseng,
Cheng-Hung Chiang, Chun-Jung Chen, Shih-Chun Chung, Ching-Shiang Hwang,
King-Long Tsang and Chien-Te Chen

P06-005

STANDARD OPERATION SYSTEM FOR STRUCTURAL BIOLOGYBEAMLINES AT SPRING-8
Go Ueno, Kazuya Hasegawa, Nobuo Okazaki, Kunio Hirata, Takashi Kumasaka
and Masaki Yamamoto

P06-006

HOMELABS VS. SYNCHROTRONS: THE FACTS WILL SURPRISE YOU
Joseph D. Ferrara, Cheng Yang

P06-007

NEXT GENERATION X-RAY DETECTOR FOR IN-HOUSE XRD SYSTEM
Takeyoshi Taguchi, Christian Broennimann and Eric F. Eikenberry

P06-008

STRUCTURAL BIOLOGY BEAMLINES AT SPring-8
Masaki Yamamoto, Go Ueno, Takaaki Hikima, Atsushi Nisawa, Kunio Hirata,
Tetsuya Shimizu, Nobutaka Shimizu, Masahide Kawamoto, Kazuya Hasegawa,
Hisanobu Sakai, Seiki Baba, Nobuo Okazaki, Aik Hong Teh, Takashi Kumasaka

P06-009

STATISTICAL PROPERTIES OF X-RAY INTENSITY MEASURED WITH
A COUNTING SYSTEM WITH FINITE DEAD-TIME
Takashi Ida, Akihisa Oya, Hisashi Hibino

P06-010MAIL-IN DATA COLLECTION AT SPRING-8 STRUCTURAL BIOLOGYBEAMLINES
Seiki Baba, Kazuya Hasegawa, Go Ueno, Nobuo Okazaki, Hisanobu Sakai,
Hironori Murakami, Takashi Kumasaka and Masaki Yamamoto

P06-011

HIGH THROUGHPUT PROTEIN CRYSTAL EXCHANGE ROBOTS OF
THE PHOTON FACTORY BEAMLINES
Masahiko Hiraki, Shokei Watanabe, Nobuo pHonda, Yusuke Yamada, Naohiro
Matsugaki, Noriyuki Igarashi, Yurii Gaponov and Soichi Wakatsuki

P06-012UPGRADE OF THE STRUCTURAL BIOLOGY BEAMLINES AT THE
PHOTON FACTORY
Noriyuki Igarashi, Naohiro Matsugaki, Yusuke Yamada, Masahiko Hiraki andSoichi Wakatsuki

P06-013

THE SIDE LINE OF TAIWAN CONTRACT BEAMLINE BL12XU ATSPRING-8 FOR HIGH ENERGY PHOTOEMISSION
Chi-Yi Huang, Ku-Ding Tsuei, Yong Q. Cai, Cheng-Chi Chen, Yen-Fang Song andShih-Chun Chung

P06-041

RATIOS OF ELASTIC CONSTANTS OF CDTE DERIVED FROM X-RAY
THERMAL DIFFUSE SCATTERING UNDER HIGH PRESSURE
Daisuke Ohtsu, Maki Okube, Takahiro Kuribayashi, Yasuhiro Kudoh, Taiki
Nakanishi, Hiroyuki Katsuragawa, Akiko Nakao, and Satoshi Sasaki

P06-042

SITE OCCUPANCY AND MAGNETIC STRUCTURE OF BATIMNFE10O19
HEXAFERRITETaiki Nakanishi, Maki Okube, Hiroyuki Katsuragawa, Daisuke Ohtsu, Takeshi
Toyoda, Akiko Nakao, and Satoshi Sasaki

P06-043

VALENCE AND SPIN STATE OF Co IONS IN La1-XCaXCoO3
Hiroyuki Katsuragawa, Maki Okube, Takayasu Hanashima, Taiki Nakanishi,
Daisuke Ohtsu, and Satoshi Sasaki

P06-044

MIXED-VALENCE STATES OF TRANSITION-METAL ATOMS IN A
SOLID SOLUTION BETWEEN Fe3O4 AND Co3O4
Yoshihiro Yamamoto, Norio Shimizu, Maki Okube, Atsuko Ohno and Satoshi
SasakiP06-045

X-RAY SCATTERING STUDY OF YTTRIUM-DOPED HfO2 THIN FILMS
C.-H. Hsu, Z. K. Yang, K. L. Yu, M.-T. Tang, M. L. Huang, W. C. Lee, Y. J. Lee, P.
Chang, M. Hong, and J. Kwo

P06-046STUDIES ON FERROMAGNETIC CARBONS
Prabal Dasgupta

P06-047

CRYSTAL STRUCTURE AND MAGNETIC PROPERTIES OF NaFe(WO4)2
AND NaCr(WO4)2
D.Sangaa, L.Nyam-Ochir, H.Ehrenberg, D.Mikhailova, H.Fuess

P06-048

THE METHOD OF DETERMINATION OF STRUCTURAL IN
STRETCHED POLYMERSAida Martirosyan

P06-049

CRYSTAL ENGENEERING OF NEW 4,4’-BIPYRIDINES AND RELATEDCOMPOUNDS
Olexii V. Gutov, Eduard B. Rusanov, Alexander N. Chernega, Mark I. Povolotskii

P06-050

COCRYSTALS OF OXALIC ACID WITH DERIVATIVES OF TRICYCLICQUINAZOLONE-4
Akmal Tojiboev, Kambarali Turgunov, Bahodir Tashkhodjaev

P06-051

CRYSTAL STRUCTURES OF TWO ALIPHATIC AMIDASES AMIE AND
AMIF FROM HELICOBACTER PYLORI REVEAL A CONSERVEDCATALYTIC TRIAD
Wen-Ching Wang, Chiu-Lien Hung, Cheng-Yu Chen, and Yu-Wen HuaP06-052

POLYTYPE TRANSFORMATION DURING NITROGEN DOPING OF SiC
CRYSTALS
Jinli Chen and Zhe Chuan Feng

P06-053

FoRMATION OF LARGE LANTHANIDE CLUSTER HAVING CHIRAL
LIGANDS AND THEIR MOLECULAR ASSEMBLY IN THE
CRYSTALLINE STATE
Chizuko Kabuto , Kenji Omata , Kuninobu Kabuto , and Yoichi Sasaki

P06-054HOST FRAMEWORK OF INCLUSION CRYSTAL OF
1,1,2,2-TETRAKIS(4-CARBOXYPHENYL) ETHANE
Michiko Iriyama, Natsumi Sakuma, Hidehiro Uekusa, Natsuki Amanokura,
Masami Kaneko

P06-055

CRYSTAL STRUCTURE ANALYSIS OF
1,1,2,2-TETRAKIS(3-METHYL-4-HYDROXYPHENYL)ETHANEINCLUSION CRYSTALS
Kazuyuki Toyota, Hidehiro Uekusa, Natuki Amanokura, and Masami Kaneko

P06-056

STRUCTURAL DIVERSITY OF [M(SCN)2] FRAGMENTS WITH
N,N’-BISPYRIDINE-TYPE LIGANDS, 4-BPD (4-BPD =1,4-BIS(4-PYRIDYL)-2,3-DIAZA-1,3-BUTADIENE)
Chih-Chieh Wang, Wei-Zeng Lin, Yu-Ruei Guo, Wei-Ting Huang, Shuen-Jie Dai,
Mei-Ju Ke, Gene-Hsiang Lee

P06-057

STRUCTURAL DIVERSITY OF [M(SCN)2] FRAGMENTS WITH BPHD
(BPHD = 2,5-Bis(4-pyridyl)-3,4-diaza-2,4-hexadiene)
Chih-Chieh Wang, Yi-Tzu Lin, Yu-Hsuan Lee, Gene-Hsiang Lee

P06-058

CRYSTAL STRUCTURE AND VIBRATIONAL SPECTRA OF
m-OXO-BIS[TETRA(p-METHOXYPHENYL)PORPHYRINATOIRON(III)]
Ratchadaporn Puntharod, Bayden Wood, Don McNaughton, and Kenneth J. Haller

P06-059[H2en]2+ CATION DISORDER IN A NETWORK OF VANADIUMPOLYBORATE CLUSTERS
Aungkana Chatkon, Kenneth J. Haller, and Ian D. Williams

P06-060

A THREE-DIMENSIONAL SUPRAMOLECULAR STRUCTURE OF ZINCVANADATE: Zn(2-EtIm)2(VO3)2
Orrasa In-noi, Samroeng Krachodnok, Kenneth J. Haller, Herman H.-Y. Sung,
Fanny L.-Y. Shek and Ian D. Williams

P06-061

LAYERED AND NETWORK STRUCTURES OF HYBRID ZINCVANADATES CONTAINING BRIDGING AZOLE LIGANDS
Samroeng Krachodnok, Kenneth J. Haller, Herman H-Y. Sung, Fanny L-Y. Shek
and Ian D. Williams

P06-062

OPEN COPPER TARTRATE BIPYRIDINE 3D FRAMEWORKS WITH
VARYING WALL CHIRALITIESPokka K-C. Pang, Herman H-Y. Sung and Ian D. Williams

P06-063

FLUX SYNTHESIS OF NEW TARTRATOBORATE POLYMERS ANDCYCLIC OLIGOMERSAlex S-F. Au-Yeung, Herman H-Y. Sung and Ian D. Williams

P06-064

CRYSTAL STRUCTURE OF COMPLEX BIMETALLIC SALTS OF
NICKEL(II): [Ni(ter)2(H2O)4][Ni(4-CNpy)2(H2O)4].H2O AND [Ni(H2O)6][Ni(ter)(4-CNpy)(H2O)4].(ter)Sanchay J. Bora and Birinchi K. Das

P06-065

A NOVEL 3D INTERPENETRATING FRAMEWORK CONTAINING 1D
LADDERS COORDINATION POLYMERS WITH MIXED ORGANICLIGANDS: [Ni2(H2O)2(BDC)2(bpp)2]
Chia-Her Lin and Tai-Hsing Tsao

P06-066

HYDROTHERMAL SYNTHESIS OF METAL HYDROXIDEIMIDAZOLIDE 3D FRAMEWORK POLYMERSFion T-Y. Yeong, Fanny L-Y. Shek, Herman H-Y. Sung and Ian D. Williams

P06-067

dSNAP: NEW SOFTWARE FOR ANALYSING THE RESULTS OFCAMBRIDGE DATA BASE SEARCHES
Chris Gilmore, Gordon Barr, Wei Dong, Andrew Parkin, Duncan Sneddon, Chick
WilsonP06-068

AN OBSERVATION ON THE WETTING PHENOMENON OF GALLIUM
NANO DROPLETS BY X-RAY DIFFRACTION
Masanori Tanaka, Takehiro Noda, Osami Sakata, Hikaru Terauchi, and Isao
Takahashi

P06-069

BEAM COMPRESSION AND LATTICE-CONSTANT VARIATIONS IN
CURVED X-RAY CAVITY
S.-Y. Chen, Y.-Y. Chang, Y.-J. Liu, M.-T. Tang, Yu. P. Stetsko, H.-H. Wu, Y.-R. Lee,
M. Yabashi, B.-Y. Shew, and S.-L. Chang

P06-070

DETERMINATION OF LATTICE PARAMETERS OF FeSi2/Si QUANTUM
DOT NANO-STRUCTURES BY X-RAY BRAGG-SURFACE DIFFRACTION
Yi-Wei Tsai, Chia-Hung Chu , Wen-Ching Sun, and Shih-Lin Chang

P06-071

CRYSTALLINE LAMELLAE IN THIN FILM OF BIODEGRADABLEPOLYMER POLY(HYDROXYBUTYRATE) STUDIED BY SURFACE
X-RAY DIFFRACTION
Shota Mukoyama, Kazuhiro Yamasaki, Hikaru Terauchi, Harumi Sato, Yukihiro
Ozaki, Isao Noda, and Isao Takahashi

P06-072

CORE-SHELL COMPOSITION AND ITS INFLUENCES ON THE
PROPERTIES OF MATERIALSVo Vong , Luu Tien Hung and Michael Hietschold

P06-073GLASS TRANSITION TEMPERATURE OF ULTRATHIN POLYMERUNDER ULTRASLOW HEATING: AN X-RAY REFLECTIVITY STUDY ON
POLYSTYRENE FILMS SUPPORTED ON Si
Chun-Ming Yang, Hikaru Terauchi, and Isao Takahashi

P06-074

CRYSTAL STRUCTURE OF β-LACTOGLOBULIN AND VITAMIN DCOMPLEX. IDENTIFICATION OF A SECOND BINDING SITE FOR
VITAMIN D: A THERMAL INDEPENDENT SITE.
Hong -Hsiang Guan, Ming -Chi Yang, Ming -Yih Liu, Jinn -Moon Yang,Wen-Liang Chen, Simon JT Mao and Chun- Jung Chen

P06-075

NANOSTRUCTURED FILMS CONSTITUTED OF TiO2 AND SnO2
PREPARED BY MEANS OF SPRAY PYROLYSIS
Pham-Van Nho, Pham-Hoang Ngan, Tran-Kim Cuong

P06-076

STRUCTURAL STUDY OF ARSENATE INCORPORATION INTOCALCIUM PHOSPHATE HYDROXYAPATITE
Winya Dungkaew, Weenawan Somphon, Kenneth J. Haller

P06-077

STRUCTURAL STUDY OF COPPER INCORPORATION INTOCALCIUM PHOSPHATE HYDROXYAPATITE
Oratai Saisa-ard, Winya Dungkaew, Weenawan Somphon and Kenneth J. Haller

P06-078

CHROMIUM AND CADMIUM IMMOBILIZATION BY PORTLAND
CEMENT SOLIDIFICATION
Weenawan Somphon, Samroeng Krachodnok, Angkana Kiatpichitpong

P06-079

NANOCRYSTALLINE COPPER SULPHIDE: SYNTHESIS AND ITS
CHARACTERIZATION
N.Vasumathi, B.B.Nayak and B.S.Acharya

P06-080

X-RAY DIFFRACTION STUDY ON THERMAL BEHAVIORS OF SHAPE
MEMORY ALLOY Au50.5Cd49.5
Michinori Yoshikawa, Genki Kikuma, Takuya Ohba, Hikaru Terauchi, and Isao
Takahashi

P06-081

OBSERVATION ON TRANSITIONs in SURfACE REGION OF COCOA
BUTTER BY X-RAY DIFFRACTION
Yusuke-Hayashi, Yoshihito-Uozaki, Hikaru-Terauchi, and Isao-Takahashi

P06-082

COMPARATIVE STUDY ON THE I-V CHARACTERISICS OF METALSTRING COMPLEXES EXPERIMENT VS THEORY
Liang-Yan Hsu, Bih-Yaw Jin, Chun-Hsien Chen. Shie-Ming Peng

P06-142

CRYSTAL STRUCTURES OF THE CYTOSOLIC DOMAIN OF THE Mg2+
TRANSPORTER MgtE
Yoshiki Tanaka , Motoyuki Hattori , Shuya Fukai , Ryuichiro Ishitani and Osamu
Nureki

P06-143

CRYSTAL STRUCTURE OF THE MgtE Mg2+ TRANSPORTER
Motoyuki Hattori, Yoshiki Tanaka, Shuya Fukai , Ryuichiro Ishitani and Osamu
Nureki

P06-144

STRUCTURAL BASIS OF PROSTACYCLIN BIOSYNTHESISYi-Ching Li, Chia-Wang Chiang, Hui-Chun Yeh, Frank G. Whitby, Lee-Ho Wang,
and Nei-Li Chan

P06-145

STRUCTURAL STUDIES OF THE HUMAN PROSTACYCLIN SYNTHASE
Chia-Wang Chiang, Hui-Chun Yeh, Lee-Ho Wang, and Nei-Li Chan

P06-146

HIGHLY AMPHIPHILIC INTERFACE IN THE COMPLEX FORMED
BETWEEN DPPIV (CD26) AND ADENOSINE DEAMINASE
Wolfram Saenger, Wilhelm A. Weihofen, Jiango Liu, Werner Reutter, Hua Fan

P06-147

CRYSTAL STRUCTURE OF BOVINE LACTOPEROXIDASE AT 2.3 Å
RESOLUTION
Amit Kumar Singh, Nagendra Singh, Sujata Sharma, Mau Sinha, Punit Kaur, A.
Srinivasan and T. P. Singh

P06-148

CRYSTAL STRUCTURE OF CAMEL PEPTIDOGLYCAN RECOGNITIONPROTEINS AT 3.0 Å RESOLUTION
Pradeep Sharma, Nagendra Singh, Sujata Sharma and T.P.Singh

P06-149

CRYSTAL STRUCTURE OF THE COMPLEX OF SHEEP SIGNALINGGLYCOPROTEIN WITH 2-METHYL-2,4-PENTANEDIOL AT 1.65Ǻ
RESOLUTION
Mau Sinha, Pradeep Sharma, Nagendra Singh, Sujata Sharma, Punit Kaur and Tej
P. Singh

P06-150

CRYSTAL STRUCTURES OF COMPLEXES OF C-LOBE OF BOVINELACTOFERRIN WITH VARIOUS SACCHARIDES AT HIGHRESOLUTIONS REVEAL A COMMON BINDING SURFACE IN THE
C-LOBE
Rafia Mir, Mau Sinha, Nagendra Singh, Vikram Gopalakrishnapillai, Sujata
Sharma, Punit Kaur and Tej.P.Singh

P06-151

CRYSTAL STRUCTURE OF GOAT LACTOPEROXIDASE AT 2.4ǺRESOLUTION
Nagendra Singh, Amit Kumar Singh, Sujata Sharma, Asha Bhushan, Punit Kaurand Tej P. Singh

P06-152

CRYSTAL STRUCTURE OF A COMPLEX OF PHOSPHOLIPASE A2( PLA2 ) WITH A NEW GRAMINE DERIVATIVE AT 2.2 Å RESOLUTION
Sanjit Kumar, Nagendra Singh, Sujata Sharma, Tej.Pal.Singh

P06-153

CRYSTAL STRUCTURES OF THREE ACTIVE SITE MUTANTS OF
BOVINE PANCREATIC PHOSPHOLIPASE A2
Shankar Prasad Kanaujia and Kanagaraj Sekar

P06-154

CRYSTAL STRUCTURE OF BOVINE C-LOBE WITH RIBOSE AT 2.5 Å
RESOLUTION
G. Vikram, R. Mir, M. Sinha, N.Singh, S. Sharma, P. Kaur and T.P. Singh

P06-155

FRAGMENT-BASED INHIBITION OF PROTEINASE K: CRYSTALSTRUCTURE OF A COMPLEX OF PROTEINASE K WITH BORONICACID AT 0.83 Å RESOLUTION
R. Jain, N. Singh, M. Perbandt, C. Betzel, S. Sharma, P. Kaur, A. Srinivasan,
T.P. Singh\

P06-156

CRYSTAL STRUCTURE OF BUFFALO LACTOPEROXIDASE AT 2.8Å
RESOLUTION
Ishfaq Ahmed Sheikh, Nagendra Singh, Sujata Sharma, Asha bhushan and T.P.
Singh

P06-157

CRYSTAL STRUCTURE OF MAMMARY SECRETORY GLYCOPROTEINFROM BUFFALO AND ITS COMPLEXES WITH OLIGO-SACCHARIDES
Punit Kaur, A.K. Singh, Rishi Jain, N. Singh, S, Sharma and T.P. Singh

P06-158

X-RAY CRYSTAL STRUCTURE ANALYSIS OF ERK1/IODOTUBERCIDINCOMPLEXIkuyo Yoshida, Takayoshi Kinoshita, Masaki Gouda, Mamoru Matsubara, Hiroshi
Ishiguro, Toshiji Tada

P06-159

CRYSTAL STRUCTURE OF HUMAN LYN KINASE DOMAIN
Nao Miyano, Takayoshi Kinoshita, Koichi Yokota, Hiroshi Ishiguro and Toshiji
Tada

P06-160

PROTEOMIC ANALYSIS OF MANGANESE REGULATION OFNEISSERIA GONORRHOEAE
Hsing-Ju Wu, Kuan-Tin Pan, He-Hsuan Hsiao, Chen-Wen Yao, Alastair G.
McEwan, Michael P. Jennings and Andrew H-J. Wang

P06-161

MOLECULAR BASIS FOR RECOGNITION OF A SELECTIVE
NUCLEOSIDE INHIBITOR BY PLASMODIUM FALCIPARUM
S-ADENOSYL-L-HOMOCYSTEINE HYDROLASE
Yoshio Kusakabe, Nobutada Tanaka, Ken-ichi Aoki, Masayuki Nakanishi, Yukio
Kitade,d and Kazuo T. Nakamura

P06-162

CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSISS-ADENOSYL-L-HOMOCYSTEINE HYDROLASE
Nobutada Tanaka, Yoshio Kusakabe, Masayuki Nakanishi, Koichi Maruyama,
Takayuki Ezaki,e Yukio Kitade,b,c,d and Kazuo T. Nakamura

P06-163

ELUCIDATION OF A CATALYTIC-CRITICAL HYDROGEN BOND
NETWORK IN THE ACTIVE SITE OF ANIMAL GLUTAMINYLCYCLASES SUGGESTS AN ESSENTIAL PROTON TRANSFER PROCESSDURING CATALYSIS
Kai-Fa Huang, Yu-Ruei Wang, En-Cheng Chang, Tsung-Lin Chou, and Andrew
H.-J. Wang

P06-164

STRUCTURAL COMPARISON STUDIES FOR 2H PHOSPHOESTERASE
SUPERFAMILY PROTEINS
Yasumitsu Sakamoto, Nobutada Tanaka, Tomomi Ichimiya, Tadashi Kurihara, andKazuo T. Nakamura

P06-165

CRYSTAL STRUCTURE OF PARASPORIN-2, AN ANTI-TUMOR TOXINFROM BACILLUS THURINGIENSIS
Toshihiko Akiba,a Yuichi Abe,b Sakae Kitada,b Yoshitomo Kusaka,b Akio Ito,bTokio Ichimatsu,c Hideki Katayama,c Tetsuyuki Akao,c Kazuhiko Higuchi,c Eiichi
Mizuki,c Michio Ohba,d Ryuta Kanai a and Kazuaki Harata

P06-166

CRYSTAL STRUCTURE OF THE HRDC DOMAIN OF HUMAN WERNERSYNDROME PROTEIN, WRN.
Ken Kitano, Nozomi Yoshihara and Toshio Hakoshima

P06-167

CRYSTAL STRUCTURE OF FUSOBACTERIUM ADHESIN A (FADA):IMPLICATIONS FOR ORAL DISEASES AND PRETERM BIRTH
Stanley Nithianantham, Minghua Xu, Mitsunori Yamada, Hongqi Liu, JonathanRoss, Mark Durham, Hameem Kawsar, Menachem Shoham and Yiping W. Han

P06-168

STRUCTURE-BASED DESIGN OF INHIBITORS OF HUMAN MTH1
PROTEIN I
Teruya Nakamura, Miyuki Inazato, Sinji Ikemizu, Yusaku Nakabeppu, and Yuriko
Yamagata

P06-192

CRYSTAL STRUCTURES OF D-AMINO ACID AMIDASE FROMOCHROBACTRUM ANTHROPI SV3 AND A-AMINO-E-CAPROLACTAMRACEMASE FROM ACHROMOBACTER OBAE
Seiji Okazaki, Atsuo Suzuki, Tsunehiro Mizushima, Hidenobu Komeda, Yasuhisa
Asano, Takashi Yamane

P06-193

XC5848, AN ORFAN PROTEIN FROM XANTHOMONAS CAMPESTRIS,ADOPTS A NOVEL VARIANT OF SM-LIKE MOTIF
Ko-Hsin Chin, Andrew H.-J. Wang, & Shan-Ho Chou

P06-194

THE CRYSTAL STRUCTURE OF XC1258 FROM XANTHOMONAS
CAMPESTRIS: A PUTATIVE PROCARYOTIC NIT PROTEIN WITH AN
ARSENIC ADDUCT IN THE ACTIVE SITE
Ko-Hsin Chin, Andrew H.-J. Wang, & Shan-Ho Chou

P06-195

KINETIC AND STRUCTURAL PROPERTIES OF TRIOSEPHOSPHATEISOMERASE FROM HELICOBACTER PYLORIChen-Hsi Chu, Yi-Ju Lai, and Yuh-Ju Sun

P06-196

CARBOHYDRATE-BINDING OF THE STARCH BINDING DOMAIN OFRHIZOPUS ORYZAE GLUCOAMYLASE IN COMPLEX WITH
β-CYCLODEXTRIN AND MALTOHEPTAOSE
Jung-Yu Tung , Yen-Yi Liu, Wei-I Chou, Fang-Yu Chang, Dah-Tsyr Chang and
Yuh-Ju Sun

P06-197

ATP-DRIVEN MOTIONS OF 70-KDA HEAT SHOCK PROTEINS(HSP70S): INSIGHTS INTO STRUCTURAL DYNAMICS OF THE HSP70
POWER STROKE
Yi-Wei Chang, Chung Wang, and Chwan-Deng Hsiao

P06-198

CRYSTAL STRUCTURE OF PHOSPHORIBOSYLPYROPHOSPHATE
BOUND NICOTINATE PHOSPHORIBOSYLTRANSFERASE FROMPYROCOCCUS FURIOSUS
KyuBeen Sohn, Yilan Fang, Rosalind Kim, Sung-Hou Kim and Dong Hae Shin

P06-199

STABILIZATION OF COLLAGEN TRIPLE-HELIX BY ARG IN THE Y
POSITION
Tatsuya Morimoto, Mitsuru Haga, Chizuru Hongo, Keiichi Noguchi, Kenji
Okuyama and Toshiki Tanaka

P06-200

THE STRUCTURAL ANALYSIS OF THE COLLAGEN-MODEL PEPTIDE,(Pro-Pro-Gly)4-Hyp-Asp-Gly-(Pro-Pro-Gly)4 CRYSTAL
Tatsuya Kawaguchi, Masaki Shimura, Chizuru Hongo, Keiichi Noguchi, Kenji
Okuyama, Kazunori Mizuno and Hans Peter Bachinger

P06-201

CRYSTAL STRUCTURE OF 3D8 scFv ANTI-DNA ANTIBODY, ITS SINGLE
DOMAINS, AND THE COMPLEX WITH A SMALL MOLECULE
Suk-Yeol Park, Young-Rim Kim, Yong-Sung Kim, Myung-Hee Kwon, Jeong-Sun
Kim

P06-202

CRYSTAL STRUCTURE OF YDJA FROM ESCHERICHIA COLI
Ji-Woo Choi, Ji-Eun Lee, Che-Hun Jung, and Jeong-Sun Kim

P06-203

CRYSTAL STRUCTURE OF ybfF FROM ESCHERICHIA COLI
Nishi Kosuke, Suk-Youl Park, Sang-Hak Lee, Ji-Woo Choi, Nguyen To Uyen,
Ji-Eun Lee, Che-Hun Jung, and Jeong-Sun Kim

P06-204

STRUCTURE AND FUNCTIONAL STUDY OF RICE BIFUCTIONAL
ALPHA-AMYLASE/SUBTILISIN INHIBITOR FROM Oryza sativa
Wen-Yan Peng, Yi-Hung Lin, Yen-Chieh Huang, Hong-Hsiang Guan, Ying-Cheng
Hsieh, Ming-Yih Liu,Tschining Chang, and Chun-Jung Chen

P06-205

X-RAY 3D STRUCTURE AND FUNCTION STUDY OF RICELECTIN-LIKE COMPLEX
Chin-Wen Wu, Yen-Chieh Huang, Hong-Hsiang Guan, Yin-Cheng Hsieh, Chia-Hao
Shin, Tschining Chang, Yi-Hung Lin and Chun-Jung Chen

P06-206

COMPLEX STRUCTURE OF XYLANASE WITH
XYLO-OLIGOSACCHARIDES FROM TRICHODERMA HARZIANUM
ETS323 : STRUCTURAL EVIDENCE FOR GLYCOSYL TRANSFERASE
REACTION
En-Hung Liu, Kun-Che Chang, Yuan-Lung Chiang, Ying-Cheng Hsieh,
Chaur-Tsuen Lo, Yi-Hung Lin,Yen-Chieh Huang, Hong-Hsiang Guan, Kuo-Cheng
Peng, Chun-Jung Chen

P06-207

CRYSTAL STRUCTURE AND FUNCTIONAL STUDY OF THE
BOWMAN-BIRK INHIBITOR FROM RICE BRAN IN TERNARYCOMPLEX WITH BOVINE TRYPSIN
Hsin-Tai Li, Yi-Hung Lin, Yen-Chieh Huang, Ying-Cheng Hsieh, Hong-Hsiang
Guan, Tschining Chang, Andrew H.-J. Wang and Chun-Jung Chen

P06-208

CRYSTAL STRUCTURE STUDY OF WILD TYPE AND MUTATEDBACILLUS CEREUS NCTU2 CHITINASE
Yin-Cheng Hsieh, Chueh-Yuan Kuo , Huei-Ju Tasi , Yi-Hsin Pan , Yaw-Kuen Li ,and Chun-Jung Chen

P06-209

CRYSTALLOGRAPHIC STUDIES OF THE C-TERMINAL DOMAIN OF
DNA GYRASE
Tung-Ju Hsieh, Hsun-Tang Chang, Te-Sheng Lin, Shu-Yun Haung, Lynn Farh, and
Nei-Li Chan

P06-210

STRUCTURAL AND FUNCTIONAL STUDIES OF THE
6-PHOSPHOGLUCONATE DEHYDROGENASE ASSOCIATED WITH
PATHOGENESIS OF KLEBSIELLA PNEUMONIAE
Ying-Yin Chen , Tzu-Ping Ko, Li-ping Lo, Chun-Hung Lin, Andrew H-J Wang

P06-211

CRYSTALLIZATION AND STRUCTURAL ELUCIDATION OF
PLASMODIUM VIVAX DIHYDROFOLATE
REDUCTASE-THYMIDYLATE SYNTHASE
Puttapol Khongsuk, Ubolsree Leartsakulpanich, Yongyuth Yuthavong and
Palangpon Kongsaeree

P06-212

THE CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF PLANTS
NADPH OXIDASE
Takashi Oda, Kokoro Hayashi, Chojiro Kojima, Hiroshi Hashimoto, Tsutomu
Kawasaki, Ko Shimamoto, Mamoru Sato, and Toshiyuki Shimizu

P06-213HIGHER SIGNAL, LOWER NOISE: HOW TO GET THE BEST DATAFROM YOUR CRYSTALSMartin Adam, Anita Coetzee, Bram Schierbeek, Cary Bauer and Rob Hooft

P06-214

CRYSTALLOGRAPHIC CHARACTERIZATION OF THE RADIXIN FERM
DOMAIN BOUND TO CYTOPLASMIC TAIL OF ADHESION MOLECULE
CD44
Tomoyuki Mori, Ken Kitano, Shin-ichi Terawaki, Ryoko Maesaki and Toshio
Hakoshima

P06-215

CRYSTALLOGRAPHIC STUDIES OF A LECTIN FROM THE
OCTOCORAL
Akiko Kita, Mitsuru Jimbo, Yukio Morimoto, Ryuichi Sakai, Hisao Kamiya, andKunio Miki

P06-216

CRYSTALLIZATION AND STRUCTURAL ELUCIDATION OF
PLASMODIUM VIVAX DIHYDROFOLATE
REDUCTASE-THYMIDYLATE SYNTHASE
Puttapol Khongsuk, Ubolsree Leartsakulpanich, Yongyuth Yuthavong and
Palangpon Kongsaeree

P06-217

NOVEL DNA-BINDING FOLD AND DNA-RECOGNITION MODEDISCOVERED IN PABI FAMILY OF RESTRICTION ENZYMES
Ken-ichi Miyazono, Miki Watanabe, Jan Kosinski, Ken Ishikawa, Masayuki Kamo,
Tatsuya Sawasaki, Koji Nagata, Janusz M. Bujnicki, Yaeta Endo, Ichizo Kobayashi,& Masaru Tanokura

P06-218

SINGLE MUTATIONS LEAD TO SIGNIFICANT INCREASE IN
SUBSTRATE SPECIFICITY AND ACTIVITY: STRUCTURAL, ENZYMEKINETICS AND MOLECULAR MODELING STUDIES FOR CYSTEINEPROTEASE FROM A TROPICAL PLANT
Raka Ghosh, Chandana Chakrabarti, Sampa Biswas and J.K. Dattagupta

P06-219

SYNTHESIS AND CHARACTERIZATION OF CuMPt6 (M= 3D
ELEMENTS) TERNARY ALLOYS
Ejaz Ahmed , Miwako Takahashi , Hiroshi Iwasaki and Ken-ichi Ohshima

P06-220

X-RAY STRUCTURE OF THE SKP1-FBS1 GLYCOPROTEIN COMPLEX
Tsunehiro Mizushima, Yukiko Yoshida, Taichi Kumanomidou, Yuko Hasegawa,Atsuo Suzuki, Takashi Yamane and Keiji Tanaka

P06-221

X-RAY MULTIPLE-WAVE DIFFRACTION ANOMALOUS FINESTRUCTURE
S.-C. Weng, Y.-R. Lee, Yu. P. Stetsko, W.-H. Sun, Y.-L. Soo and S.-L. Chang

P06-222

DYNAMICAL CALCULATION FOR TWENTY-FOUR BEAM X-RAY
DIFFRACTION IN A TWO-PLATE CRYSTAL CAVITY OF SILICON
M.-S. Chiu, Yu. P. Stetsko, and S.-L. Chang

P06-223

STRUCTURAL FEATURES OF PSYCHROPHILIC MALATEDEHYDROGENASE ADAPTING TO THE EXTREME ENVIRONMENT
Yasuo Hata, Tomomi Fujii, Tadao Oikawa and Kenji Soda

P06-224

GROWTH RING OF TEETH- A MICRO X-RAY DIFFRACTION STUDYHejing Wang, Jian Zhou, Nan Zheng and Tingjing Xu

P06-225

STRUCTURES OF SOME CRYSTAL SOLVATES OF
N-(3-ETHYLTHIO-1,2,4-THIADIAZOL-5-YL-AMINOCARBONYLMETHYL) CYTIZINE
U.S.Mahmudov, T.F.Ibragimov, K.K.Turgunov, B.Tashkhodjaev.

P06-226

STRUCTURAL EVIDENCE THAT AN a-PROTEOBACTERIA IS THE
OLDEST SURVIVING SPECIESWilliam L. Duax, Robert Huether, Qilong Mao, Vladimir Pletnev, Timothy Umland
and Charles M. Weeks

P06-227

STRUCTURAL STUDY FOR THE ENZYME MECHANISM OF
EUKARYOTIC GLUTAMINE SYNTHETASE FROM ZEA MAYS
Takeshi Ozaki, Hideaki Unno, Toshiharu Hase, Masami Kusunoki

P06-228

CRYSTAL SOLVATES OF N-(3-METHYLTHIO-1,2,4-THIADIAZOL-5YL-AMINOCARBONYLMETHYL)CYTISINE
Kambarali Turgunov, Utkur Makhmudov, Temur Ibragimov, Bakhodir Tashkodjaev

P06-229

SYNTHESIS OF NANOCRYSTALLINE (Co,Ni)Al2O4 SPINEL POWDERBY QUASICRYSTALLINE PRECURSOR
T.P. Yadav, N.K. Mukhopadhyay, R.S. Tiwari and O.N. Srivastava

P06-230

PROBING LOCAL STRUCTURES AROUND Co IN FERROMAGNETIC
HfO2:Co THIN FILMS USING EXAFS
Y. L. Soo, S. C. Weng, W. H. Sun, S. L. Chang, W. C. Lee, Y. S. Chang, J. Kwo, M.
Hong J. M. Ablett, C-. C. Kao, D.G. Liu, and J. F. Lee

P06-231

CRYO-CRYSTALLIZATION OF DIETHYL OXALATE AND STUDIES ON
INTERMOLECULAR INTERACTION
T. Vijay, S. J. Prathap and T. N. Guru Row

P06-232

CRYO-CRYSTALLIZATION OF DIETHYL OXALATE AND STUDIES ON
INTERMOLECULAR INTERACTION
T. Vijay, S. J. Prathap and T. N. Guru Row

P06-233CRYSALISPro’s ADVANCED STRATEGY MODULE FOR CHARGEDENSITY EXPERIMENTS
Dr. Jiwen Cai

P06-234

NON-CONVENTIONAL SCATTERING STUDIES OF MATERIALS USINGA LABORATORY IMAGE PLATE DIFFRACTOMETER
Lynne H. Thomas, Sylvia E. McLain, Andrew Parkin, and Chick C. Wilson

P06-235

CLASSIFYING MOLECULAR GEOMETRIES: APPLICATION OF
FACTOR ANALYSIS TO CLUSTER FORMATION IN dSNAP
Duncan Sneddon, Christopher J. Gilmore, Gordon Barr, Wei Dong, Andrew Parkin,
and Chick C. Wilson

O1A05-M1

THE EFFECT OF AMINO ACIDS AND AMINO ACID DERIVATIVESON PROTEIN CRYSTALLIZATION
L. Ito1, T. Kobayashi1, K. Shiraki2, T. Narukawa1, A. Oosuka1 and H. Yamaguchi1
1

Sch of Sci and Tech, Univ of Kwansei Gakuin, 2-1 Gakuen, Sanda, Hyogo 669-1337,

2

Inst of Appl Phys, Univ of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573

Protein crystallography is an indispensable technique for biological, biotechnological,
and pharmaceutical researches. The structure determination by X-ray crystallography has
been dramatically developed by progress in sample preparation, data collection andcomputation. To obtain high quality single crystals, however, still remains as the great
problem. The difficulty depends on the many parameters that influence protein crystallization,
including protein concentration, pH, ionic strength and precipitant concentration. Recently,
many researchers adopt the sparse-matrix including different mother liquors that cover many
chemical factors, in order to determine the primary crystallization conditions. Single crystals
suitable for X-ray diffraction experiment are not always obtained by the procedure. Suchscreening procedures are not effective enough.
Prevention of protein aggregation plays a key role in the formation of single crystals in
the aggregation-prone solution condition. Guanidine and urea are well known as aggregation
suppressors that weaken the hydrophobic intermolecular interaction of proteins. Suchdenaturants are contained in a commercially available additive-screen kit, but decrease thestability of the native state. Recently, amino acids and amino acid derivatives, which are
non-denaturating reagents, such as arginine have been used for additives to decrease theaggregation during a refolding process and a heat treatment process. In this study, weinvestigated the effect of amino acids and amino acids derivatives on protein crystallization.
As a result, protein crystals were obtained in expanded concentration range of the
known precipitant in the presence of some kind of these reagents. Especially, crystals wereobtained from many conditions including precipitants that crystal did not appear in theabsence of the reagents. For example, in the presence of arginine, HEWL crystals wereobtained from ammonium sulfate solution. It is considered that the basic additive and aminoacid derivatives promote the crystallization of positively charged HEWL. These results showthat these reagents are very effective for crystallization and promote success ratio of it andsuggests a new strategy to improve the performance of the protein crystallization by additionof amino acids.

O1A05-M2(NZ)CH...O CONTACTS ASSISTED CRYSTALLIZATION
Neil Shawa, Zhongyun Chenga, Bi-Cheng Wangb, Zihe Raoa and Zhi-Jie LiuaaNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences,

Beijing, 100101, ChinabSoutheast Collaboratory for Structural Genomics, Department of Biochemistry and Molecular

Biology, University of Georgia, GA 30602, USA

The successful crystallization and structure determination of a ParB nuclease bycreating new designer (NZ)CH…O bonds. 44 new cohesive (NZ) CH…O contacts (3.2 – 3.7Å) were synthesized by the addition of 2 methyl groups to the side chain amine nitrogen (NZ)
of 9 lysine residues of the nuclease. The engineered contacts dramatically altered the
crystallization properties of the nuclease, resulting in crystals that diffracted to 1.2 Å
resolution. The structure of the ParB nuclease protein determined in this study provides new
insights and direction for deciphering the events of DNA segregation at the atomic level. In
addition, the generality of the engineering makes it an attractive tool for tackling
crystallization problems for a broad range of protein targets.

O1A05-M3

PHASING WITH IN-HOUSE SOFTER X-RAY RADIATION
Cheng Yang, James W. Pflugrath, Joseph D. Ferrara
Rigaku Americas Corporation, The Woodlands, Texas 77381, USA

The phase problem in macromolecular crystallography has been mitigated dramaticallyin recent 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 in2006 reveals the number of structures solved by SAD phasing exceeds those solved by MAD
for the 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 sulfur 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 sulfur 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 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 from sulfur
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 structurewith a single data set.
This in-house phasing approach we describe has been given the label “know before yougo” 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.

O1A05-M4

LONG WAVELENGTH PHASING: CURRENT AND FUTURE
CHALLENGES
John P. Rose1,2, John Chrzas1,2, James Fait1,2, Zeng-Qing Albert Fu1,2, Andrew Howard2,3,John Gonczy1,2, Zhongmin Jin1,2 and B. C. Wang1,21Dept. of Biochemistry and Molecular Biology, The University of Georgia, Athens, GA, USA,

2

SER-CAT, Advanced Photon Source, Argonne National Laboratory, USA. Biological, Chemical, and3

Physical Sciences Department, Illinois Institute of Technology, Chicago, IL, USA

With the highly optimized X-ray flux and beam quality now available at 3rd generationsynchrotron sources, future improvements in overall throughput must now be directed to
improving the flow and logistics of conducting crystallographic experiments and dataacquisition themselves.
At SER-CAT, beamline setup, sample handling, sample alignment, data collection
strategy, data collection, data reduction, structure solution and data archive have all been
automated or are in the process of being automated.
Building on these technologies a newdata collection paradigm we term Signal Based Data Collection (SBDC) is being developed
aimed at increasing the success rate of structure determination and overall beamline efficiency.
The SBDC approach monitors the anomalous scattering signal present in the data (SAS or
MAD), as it is being collected, to ensure that an interpretable electron map (i.e. the structure)
can be produced. This approach differs from traditional data collection in that there is direct
feedback from the data reduction and structure determination process to the data collection
process.
The project is a partnership between structural biologists at the University of Georgia
and the excellent technical staff at SER-CAT; it builds on the methodology and technology
developed at both institutions over the past seven years, which if successful, could in a very
real sense change the way that synchrotron X-ray diffraction data is collected, increase theproductivity and cost-effectiveness of beamline operation, resulting in more and better science
being produced.
Details of the implementation of various aspects of the SBDC approach will bepresented.
Work is supported in part with funds from SER-CAT, the Georgia Research Alliance,
the National Institutes of Health (GM62407) and the University of Georgia Research
Foundation.

O1A05-M5

PSAP: PROTEIN STRUCTURE ANALYSIS PACKAGE
K. Sekara,b, B.Balamurugana, M.N.A.Md.Roshana, B.Shaahul Hameeda, K.Sumathia, R.Senthil
Kumara, A.Udayakumara, K.H.Venkatesh Babua, M.Kalaivania, G.Sowmiyaa, P.Sivasankaria,
S.Saravanana, C.Vasuki Ranjania, K.Gopalakrishnana, K.N.Selvakumara, M.Jaikumara,
T.Brindhaa and Daliah MichaelaaBioinformatics Centre and bSupercomputer Education and Research Centre, Indian Institute of

Science, Bangalore 560 012, INDIAIn the post genomic era, understanding essential knowledge hidden in a protein
molecule is of considerable interest in unraveling its structural and functional behavior. In
particular, identifying and visualizing various structural features is an essential component forstructural biologists and practicing bioinformaticians to better understand the protein
molecule. To this end, a computing engine, Protein Structure Analysis Package (PSAP), isdeveloped to identify, calculate and display various structural features of thethree-dimensional protein structures. For visualization, the free molecular graphics programs,
RasMol and Jmol are deployed in the computing engine. Further, the proposed computing
engine is interfaced with the up-to-date local copy of the Protein Data Bank. The users needto provide the PDB-identification code or upload the three-dimensional atomic coordinatesfrom the client machine. The atomic coordinates are being updated every week and hence
the users can access all the structures available in the Protein Data Bank. The computing
engine is free and is accessible online over the World Wide Web at the URL
http://iris.physics.iisc.ernet.in/psap/.
PSAP : Protein Structure Analysis Package
B.Balamurugan, M.N.A.Md.Roshan, B.Shaahul Hameed, K.Sumathi, R.Senthil Kumar,
A.Udayakumar, K.H.Venkatesh Babu, M.Kalaivani, G.Sowmiya, P.Sivasankari, S.Saravanan,
C.Vasuki Ranjani, K.Gopalakrishnan, K.N.Selvakumar, M.Jaikumar, T.Brindha, Daliah
Michael and K.Sekar
J. APPL. CRYST. (2007). (IN PRESS).

O1B05-M1

CONTROL OF POLYMORPHIC TRANSITION INDUCING
PREFERENTIAL ENRICHMENT BY MODIFYING MOLECULARSTRUCTURES OR ADDING SEED CRYSTALS
Rui Tamura
Graduate School of Human and Environmental Studies, Kyoto University, Kyoto 606-8501, Japan

Preferential Enrichment is an unusually symmetry-breaking enantiomeric resolution
phenomenon that is ascribed to an event of a complexity system [1]. We have shown that
Preferential Enrichment is initiated by the solvent-assisted solid-to-solid transformation of ametastable polymorphic form into a thermodynamically stable one occurring during
crystallization from the supersaturated EtOH solution of a certain kind of racemic mixed
crystals (i.e., solid solutions or pseudoracemates) composed of the two enantiomers, followedby partial crystal-disintegration inside the crystal lattice to release the excess enantiomer
existing in the initially-formed crystal into solution (Figure 1) [1,2]. Accordingly, Preferential
Enrichment is strongly affected by the surrounding conditions, such as additives (seedcrystals), solvent, concentration, and temperature, as well as the molecular structure.
Here we report (i) the modes of polymorphic transition relevant to the occurrence ofPreferential Enrichment and (ii) two complimentary strategies for the induction of Preferential
Enrichment by controlling the mode polymorphic transition; one is the slight modification of
the molecular structure so as to prevent the undesired polymorphic transition, and the other isthe use of the appropriate seed crystals to induce the desired “epitaxial transition” [1,3].
Me
SO 3 Me N
MeX

γ-p o lym o rp hic form
R

R

O

O R

O

α 1 -p oly m orp h ic form
S

S

S

OH

H
N

S

S

R

S

S

R

R

R

polym o rph ic
tran sition

S

S
S

S
S

S
S

R

S

S
S

R

R

S

R

S
S

S
S

R

S

S

S
S

R

R

S
R

H
N

N

S

S

O
S O
O

X

R
S

O

O
X

R
O
H
O
S O
O

O

R
S

Ph

S

p artial crystal disin teg ratio n& disso lu tio n into solu tion

F igure 1

Reference:[1] Top. Curr. Chem. 2007, 269, 53-82.
[2] (a) J. Am. Chem. Soc. 2002, 124, 13139-13153. (b) Cryst. Growth Des. 2003, 3, 973-979. (c) Enantiomeric
Separation: Fundamentals and Practical Methods; Toda, F. Ed, Kluwer Academic Publishers, Dortrecht, 2004,
pp. 135-163.
[3] (a) Chem. Eur. J. 2006, 12, 3515-3527. (b) Cryst. Growth Des., in press.

O1B05-M2

POLYMORPHISM CASE STUDIES IN THE ARTEMISININ FAMILY OF
ANTI-MALARIAL DRUGS: INVOLVEMENT OF MOLECULAR SHEETMOTIFS
Fanny L-Y. Shek, Herman H-Y. Sung, Richard K. Haynes and Ian D. Williams
Department of Chemistry, Hong Kong University of Science and Technology,
Clear Water Bay, Kowloon, Hong Kong, China.

Email: fanny@ust.hk

Atremisinin, a polycyclic peroxide natural product, is the component known as 'Qing
Hao Su' in Traditional Chinese Medicine derived from Artemisia annua. Its' derivatives has
been used as anti-malarial agents for a number of years. The parent compound and several
related members of its family have been found to display polymorphism, of which someforms have been prepared by us through hydrothermal or sub-hydrothermal crystallization.
Recently a highly effective new dervative Artemisone has been developed (R.K. Haynes et al,
Angew. Chemie, 2006, 45, 2082) and here we report its low temperature polymorphic phasetransition. This involves rotation of one molecular sheet with respect to adjacent ones,
taking a monoclinic Z' = 2 to a triclinic Z' = 4 arrangement, details below. Preserved
molecular sheet motifs have also been observed in a family of 11-azaartemisinins in whicharylsulphonate groups are substituted at the nitrogen. (R.K. Haynes et al, ChemMedChem,
2007, in press) The 4-chlorophenyl and bromophenyl derivatives are isostructural P21, withmolecular sheets which are in register, the 4-tolyl derivative is also P21 but with a doubled
cell due to offset of alternate sheets along the b-axis, whilst the 4-nitrophenyl analog is
orthorhombic P212121 with adjacent sheets rotated by 180o, which has the effect of cancelling
molecular dipoles. The relevance of such partially conserved structures to pharmaceuticalpolymorph searching and engineering will be discussed. We thank the HKSAR Research
Grants Council and Bayer Corporation for financial support.
Artemisone
100K
Triclinic P1
a = 11.1078
b= 12.385
c = 15.280
α= 90.03
β = 108.63
γ = 90.15
V = 1986.2

298K
Monoclinic P21
11.18712.501
15.39890108.5390
2041.9A3

O1B05-M3

DETERMINATION OF ABSOLUTE CONFIGURATION FOR SOME
NATURAL PRODUCTS FROM TRADITIONAL CHINESE MEDICINE
Herman H-Y. Sung, Nancy Y. Ip and Ian D. Williams
Department of Chemistry and Biotechnology Research Institute, Hong Kong University of Science andTechnology, Clear Water Bay, Kowloon, Hong Kong, China.
Email: hermans@ust.hk

The determination of natural product structures continues to be dominated bymulti-nuclear high field nmr spectroscopy in conjunction with high resolution mass
spectrometry. However these are either indirect or inconclusive techniques and it may be
hoped that the use of X-ray structure determination will become more prevalent in this field.
The use of copper X-radiation from in-house diffractometers is also essential in determining
the absolute configurations of the compounds involved. We herein present benchmark
results of such determinations on a number of standard natural product compounds withvarying degrees of oxygen and nitrogen content and using different collection times,
temperatures and strategies with an Oxford Diffraction Xcalibur instrument employing a
Copper Enhance Ultra source. The determinacy of the Flack parameter for high oxygen
content compounds such as sucrose is compared to those from a variety of new compounds
isolated from herbs used in Traditional Chinese Medicine. Examples include the diterpenoid
compounds
ent-isopimar-8(14),15-dien-19-oic
acid,
and
5-alpha-hydroxy-ent-rosa-15-en-18-oic acid, (below) isolated from the whole herb of
Sagittaria pygmaea (Liu X.T. et al, Planta Medica, 2007, 73, 84)
We thank the HKSAR Research Grants Council for financial support.

O1B05-M4

DISTINGUISHING BETWEEN NATURAL PRODUCTS AND NATURALPRODUCT ARTIFACTS USING SINGLE CRYSTAL X-RAY
STRUCTURE DETERMINATION: A CASE STUDY ON
MACLURAXANTHONE, A COMPOUND CONTAINING A CHROMENE
RINGSuchada Chantrapromma,a Nawong Boonnak,a and Hoong-Kun Funba

Department of Chemistry, Faculty of Science, Prince of Songkla University, Hat-Yai,

Songkhla 90112, Thailand.
b

X-ray Crystallography Unit, School of Physics, Universiti Sains Malaysia, 11800 USM,

Penang,Malaysia.

Natural products are frequently tested for their potentials to be used as drugs, so thecorrect differentiation between natural products and natural product artifacts is extremely
important so as not to make the wrong conclusions during the testing of these compounds forpotential drug application. The distinguishing between natural products and natural productartifacts is of paramount importance and interest to researchers in natural products,
pharmacology and chemistry. Besides offering the complete approach to 3-D structural
analysis, single crystal X-ray structure determination also has the simple ability todifferentiate easily between natural products and natural product artifacts. The distinguishing
between the natural products and natural product artifacts by this technique shall be presented
using as an example, a compound containing a chromene ring namely macluraxanthone (Fig.
1). This compound was isolated from Cratoxylum formosum subsp. pruniflorum (or Tui-Khonin Thai), a Thai medicinal plant. The decoction of the fresh or dried leaves from this plant has
been used in traditional medicine such as tonic, stomachic and diuretic [1].

Fig. 1 The chemical diagram and X-ray structure of macluraxanthone.

Reference:
1. G. M. Kitanov, I. Assenov, Dam The Van, Pharmazie, 43, H12 (1988).

O1B05-M5

PROTEIN MEASUREMENTS ON A LABORATORY POWDER X-RAY
DIFFRACTOMETER
D. Beckers, S. Prugovečki, T. Degen, A. Stefanovic
PANalytical B.V. , Almelo, The Netherlands

The Bragg-Brentano diffractometer has been used for decades for the investigation oforganic compounds as encountered, for example, in the pharmaceutical industry. In the lastten years, the introduction of new X-ray optical components and fast detection systems has
widened the number of attractive configurations for laboratory X-ray diffractometersconsiderably. Choosing the optimum hardware for a given set of analytical problems is moredifficult (and interesting!) than it was before.
In this presentation, we will show the capability of modern powder diffractometers toprovide reasonable high-resolution data on weakly scattering protein samples by choosing an
optimized set-up. Measurement an analysis results on different samples are shown. The data
quality was good enough for indexing, space group determination and even a Rietveld
refinement was reasonable. Although longer measurement times than on beam-lines are
required, radiation damage is much less. The possibility of high throughput screening ofproteins on X-ray powder laboratory instrumentation is also demonstrated and discussed.

O1C05-M1

QUANTITATIVE GISAXS ANALYSIS OF LAMELLAR STRUCTURES
SELF-ASSEMBLED IN BRUSH POLYMER THIN FILMS
Moonhor Ree*, Jinhwan Yoon, Kyeong Sik Jin, Kyuyoung Heo, Sangwoo Jin, Jehan Kim,
Kwang-Woo Kim, Tae Joo Shin
Pohang University of Science & Technology, Pohang Accelerator Laboratory,
Department of Chemistry, BK21 School of Molecular Science
Pohang 790-784, Republic of Korea ree@postech.edu

Lamellar stack structures are one of the most common morphological structures
observed in polymer thin films, including those of brush polymers, and are even observed inbulk polymer samples. However, no quantitative two-dimensional grazing incidence
small-angle X-ray scattering (2D GISAXS) analysis, or even transmission small-angle X-ray
and neutron scattering (TSAXS and TSANS) analysis, has been performed on such lamellar
stack structures in polymer thin films and bulk samples. Only limited, qualitative scattering
analyses have been carried out with scattering profiles extracted along the direction of thelamellar stacking. In this study, we developed a GISAXS formula for the quantitative analysisof lamellar stack structures formed in polymer thin films, and used it to characterize 2D
GISAXS patterns measured for lamellar structures in nanometer-scaled thin films of brushpolymers. The 2D GISAXS measurements and a quantitative data analysis using the derived
GISAXS formula provide, for the first time, the comprehensive structure and orientation
details of the lamellar stacks formed in the thin films of several brush polymers, details ofbrush polymers that cannot be obtained by TSAXS, TSANS and microscopic methods.
Furthermore, this study provides a molecular structure model and electron density profiles.
This study was supported by the Korea Science & Engineering Foundation (National
Research Lab for Polymer Synthesis and Physics and Center for Integrated Molecular
Systems) and by the Ministry of Education (BK21 Program). Synchrotron GIXS
measurements at the Pohang Accelerator Laboratory were supported by the Ministry of
Science & Technology and the POSCO Company.

O1C05-M2

MESO AND NANO-SCALE STRUCTURAL FORMATION OF
POLYETHYLENE THIN FILMS EVALUATED BY SYNCHROTRONGRAZING-INCIDENCE SMALL-ANGLE AND WIDE-ANGLE X-RAY
SCATTERING MEASUREMENTS
Sono SASAKI1, Hiroyasu MASUNAGA1, Hiroo TAJIRI1, Katsuaki INOUE1, Hiroshi
OKUDA2, Atsushi TAKAHARA3, Masaki TAKATA1,4
1Japan Synchrotron Radiation Research Institute (JASRI) / SPring-8, Hyogo 679-5198, Japan;

2International Innovation Center, Kyoto University, Kyoto 606-8501 Japan; 3Institute for Materials

Chemistry and Engineering, Kyushu University, Fukuoka 812-8581, Japan; 4The RIKEN Harima
Institute / SPring-8, Hyogo 679-5198, Japan.

Polymer thin films have been used for parts of components of displays, as the insulation
layer of semiconductors and as materials to coat papers for printing. To satisfy the physicalproperties of the thin films as materials, it is important to control their higher-order structuresat meso-to-nano scales. To reveal the essential structural property of the thin films, we havedeveloped
thegrazing-incidence
small-angle and wide-angle X-ray
scattering(GISWAXS)
experimental
technique at the BL40B2 in SPring-8(Hyogo, Japan). In this study, thehigher-order structures of polyethylene Figure 1. Experimental geometry of the GISWAXS(PE) thin films on Si wafers in annealing measurements.
and crystallization processes were IP: imaging plate, FP: flat panel, II:Imaging intensifier, CCD:
investigated at molecular and lamellar charge coupled device.
scalesbysynchrotron
GISWAXS
measurements.
Figure 1 shows the experimental geometry of the GISWAXS
measurements. The components of the scattering vector, q, paralleland perpendicular to the sample surface were defined as qy = (2π/λ)sin(2θf) cos(αf) and qz = (2π/λ) (sin(αi) + sin(αf)), respectively, forreflected scattering. Here, α iis the incident angle of the X-ray Figure 2. GISWAXS patterns measured
beams near the critical angle of total external reflection, αf is the for the PE thin films on a Si wafer at 393
exit angle, λ is the wavelength of the incident X-ray beams and 2θf K in a stepwise annealing process fromis the angle between the scattered beam and the plane of incidence. 298 K. The λ was 0.15nm and the αι
The subscripts s and w in Figure 1 indicate the grazing-incidence was 0.13 deg.
small-angle X-ray scattering (GISAXS) and the grazing-incidence

wide-angle X-ray scattering (GIWAXS) geometries, respectively.
Figure 2 shows GISWAXS patterns measured for the PE thin films (thickness: ca. 400nm) on a Si wafer at 393 K in a stepwise annealing process from 298 K. In-situ GIWAXS
profiles of the PE thin film detected at the certain annealing temperatures (Ta) between 373 K
and 393 K indicated that the a axis of the PE orthorhombic unit cell was relatively oriented in
the perpendicular direction to the film surface. On the other hand, the GISAXS data suggested
that crystalline lamellae were stacked with large disordering parallel to the film surface, andthe long period became longer with the Ta. The crystallization behavior of polyethylene inthin films during solvent-evaporation of a droplet of its p-xylene solution was evaluated bytime-resolved GISWAXS measurements as a technical application to the kinetic study, which
will be presented and discussed.

O1C05-M3

STRUCTURAL CHANGES IN THE MECHANICAL DEFORMATIONPROCESS OF SPECIFICALLY-ORIENTED POLYETHYLENESAMPLES AS VIEWED FROM THE SIMULTANEOUS
MEASUREMENTS OF SYNCHROTRON SAXS-WAXD AND RAMAN
SPECTRAKohji TASHIRO1, Shinichi TAKEDA1, Makoto HANESAKA1, Hiroyasu MASUNAGA2,
Sono SASAKI2 and Masaki TAKATA2, 3
1

Graduate School of Engineering, Toyota Technological Institute, Tempaku Nagoya, 468-8511, JapanJASRI / SPring-8, Hyogo 679-5198, Japan
3
The RIKEN Harima Institute / SPring-8, Hyogo, 679-5198, Japan
2

Investigation of structural changes occurring in the deformation process of polymer
solids subjected to the mechanical stress is essentially important for the design of newpolymer materials with excellent mechanical properties. In many studies, however, thesamples used were mainly unoriented and the lamellae are distributed randomly, and so thechange in lamellar orientation before and after the deformation is impossible to trace. Rather
it might be easier to trace the deformation procedure of lamellae when thespecifically-oriented sample of already-known lamellar stacking structure is utilized in themeasurement. In the present experiment the a-axially-oriented polyethylene sample,
obtained by spinning of the molten sample, was stretched along the draw axis, during which
the SAXS and WAXD patterns were measured at short intervals using the synchrotron X-ray
beam in parallel with the Raman spectral measurement for the molecular characterization.
This in-situ simultaneous measurement has been performed at the beam line 40B2 in SPring-8,Japan. Figure shows schematically the changes in the 2-dimensional patterns of WAXD and
SAXS taken in the necking process of the a-axially-oriented linear low-density polyethylene
sample. At the starting point the meridional scattering was observed in the SAXS pattern.
As the sample was drawn gradually the necking phenomenon was started and thefour-scattering patterns were observed to appear, indicating the transformation to the stacking
structure of tilted lamellae. It should be noticed that, before an occurrence of thisremarkable change in lamellar stacking structure, the “discontinuous” change of the a-axial
orientation to the c-axial orientation was found to occur in the crystal lattice. By stretching
the sample furthermore, the other type of meridional scatterings appeared in the SAXS pattern
and it changes to the four-points scattering pattern, indicating the tilted lamellae change to thefibrillar structure.
These behaviors are different each other depending on the degree of side
branching in the polyethylene samples.

SAXS

WAXD
a-axisc-axisO1C05-M4

STRAIN-INDUCED CRYSTALLIZATION OF REINFORCED
NATURAL RUBBER AS STUDIED BY SYNCHROTRON X-RAY
SCATTERING
Hyun Hoon Songa, Min Kwan Kanga, Hye-Jin Jeona, Gwanghoon Kwagb and Hyungkyu
Choiba

Department of Advanced Materials, Hannam University, S. Korea; bR&D Center, Kumho

Petrochemical Co. Ltd., S. Korea

Natural rubber is one of the most commercially utilized elastomeric polymers. Intensive
studies have been carried out to improve the mechanical and physical properties including
elasticity, abrasion resistance and resilience of natural rubber. Synthetic polybutadiene rubberof ultra high cis content has been also of particular interest in the rubber industry andintensively studied due to its properties which are superior to those of natural rubber. In
rubber industry, the natural rubber/synthetic rubber blend is practically utilized. Carbon black(CB) is another traditional filler used to increase the mechanical and physical properties inrubber industry. Carbon nanotubes (CNTs) also have been identified as an excellent
reinforcing material to modify mechanical, thermal and other properties of polymers.
In our recent work, strain-induced crystallization of natural rubber containing various
amounts of synthetic rubber, carbon nanotubes (CNTs) and carbon black (CB) was
systematically studied by synchrotron X-ray scattering. X-ray scattering intensities from theoriented rubber were decomposed into three phases; isotropic amorphous (IA), oriented
noncrystalline (ON), and crystalline (Cr) phase and each phase changes were monitored upon
stretching. In this presentation, the structure evolution of the orienting rubbers and themechanical properties, in particular, the effects of the reinforcing synthetic rubbers andinorganic fillers will be discussed.

O1C05-M5

ANOMALOUS SMALL ANGLE X-RAY SCATTERING FOR THE
DISTRIBUTION AND AGGREGATION OF THE GOLDNANOPARTICLES IN A PS-B-P4VP DIBLOCK COPOLYMER
U-Ser Jeng,a Ying-Huang Lai,a Ching-Mao Huang,b and Kung-Hwa Wei,b Chiu-Hun Su,a and
Hwo-Shuenn SheuaabNational Synchrotron Radiation Research Center, Hsinch 30049 Taiwan. Department of Materials
Science and Engineering, National Chiao Tung University, Hsinchu, Taiwan 30049

Using anomalous small angle X-ray scattering (ASAXS), we have studied the orderedstructure formed by 2-phenylethanethiol-coated gold nanoparticles (NPs) embedded in a
spherical poly(styrene-b-4-vinylpyridine) diblock copolymer (PS-b-P4VP). The SAXS image
taken for the copolymer/NPs composite illustrates a powder ring in conjunction withdiffraction spots distributed along the powder ring. From the diffraction peak positions andprofiles, an ordering spacing of 3.5 nm and an ordering size up to 100 nm are estimated. With
the X-ray energy tuned closed to the LIII-absorption edge of gold (11.919 keV), the diffraction
peaks decreases obviously when the photon energy is changed from 11.200 keV to 11.910 keV.
This result indicates clearly that the 2 nm gold nanoparticles are responsible for the highlyordered structure observed. The dissociation of the ordered gold clusters in an isothermal
annealing at 170 °C is monitored by in-situ small angle X-ray scattering. The four-hour
isothermal annealing disrupts the ordered gold clusters completely, while P4VP spheres
develop better ordering inside the composite. With ASAXS, further, we have found that the
dissociated gold NPs have relocated themselves to the surfaces of the P4VP spheres, forming
NPs shells outside the P4VP cores. We
discuss the mechanism of the structural
evolution of the gold NPs in the
copolymer/NPs composite.

Fig. 1: SAXS and TEM images for the PS-b-P4VP/gold NPs composite before and after thermal annealing,respectively.

O1C05-M6

CORE-SHELL MICELLAR STRUCTURES OF NOVEL TERTIARYAMINE METHACRYLATE-BASED BLOCK COPOLYMERS STUDIEDBY SMALL ANGLE X-RAY SCATTERING AND DYNAMICS LIGHT
SCATTERING
Yusuf Ozcan,a,b U-Ser Jeng,a,* Vural Butun,c Ying-Huang Lai,a Chiu-Hun Su,a Keng S. Liang,aSemra Ide baNational Synchrotron Radiation Research Center, Hsinch 30049 Taiwan. bDepartment of Physics

Engineering, Hacettepe University, 06800, Beytepe, Ankara, TURKEY. cFaculty of Arts and Science,
Department of Chemistry, Eskisehir Osmangazi University, Campus of Meselik, 26480, Eskisehir,
TURKEY.

We have studied the solution structure of couple novel amphiphilic block polymers,
with the same hydrophobic end of 2-(dimethylamino)ethyl methacrylate (DMA)
block-copolymerized with, respectively, two polyeleclyte ends of tertiary amine methacrylate
copolymers of 2-(diethylamino)ethyl methacrylate (DEA) and 2-(N-morpholino)ethyl
methacrylate (MEMA). The micellization of the polyelectrolyte block copolymer is controlled
by the sample concentration, temperature, and pH value. In contrast to the traditional micelles
formed by small surfactant molecules, whose inverted micelle structure is achieved by
selected solvents, the novel polyelectrolyte block copolymer of DEA n-(DMA-MEMA)m caninvert the micelle structure in aqueous solution simply by changing pH value from 6.7 to 8.
The micelle structures, including the size, shape, aggregation number, and polydispersity, arecharacterized using small angle X-ray scattering and dynamic light scattering. The result
indicates that a more stable micelle structure of DEAn-DMAm can be achieved with n:m ~~1:2 at 23 °C and pH= 7.7. At which condition, the narrowly disperse spherical micelles havea core-shell structure with a core radius of 54±5Å, a shell thickness of 28±3Å, and an
aggregation number of 105±5. Interestingly, the volume ratio 1:2 of the hydrophobic core
(DEA) to the hydrophilic shell (DMA swelled with water) is nearly the same as the ratio of
n/m, and the packing parameter p of the micelle structure is ~0.2 which satisfies the criterionof p <1/3 for stable spherical micelles of common amphiphilic molecules.
Fig. 1: Micelle formations of polyelectrolyte
block copolymers in various solution
conditions.

O2A05-A1

STRUCTURE, ASSEMBLY AND ACTION OF DODECAMERIC DPS, A
STRESS RELATED FAMILY OF PROTEINS
Siddhartha Roya, Ramachandran Saraswathia, Surbhi Guptaa, K.Sekarb, Dipankar Chatterjia
and M.VijayanaaMolecular Biophysics Unit, bBioinformatics Centre, Indian Institute of Science,

Bangalore 560012, India

DNA binding protein from stationary phase cells (Dps) is involved in protecting DNA
from oxidative damage and in sequestering ferric ions during nutritional starvation. We had
earlier determined the structure of a Dps molecule from M. smegmatis (MsDps1). Through theanalysis of this structure in comparison with the known structures of Dps from other sources,
among other things, the dodecameric molecule was established to be a distorted icosahedron(J.Mol.Biol. 339, 1103-1113, 2004). The subsequent analysis of mutants involving thedeletion of the N-terminal and C-terminal tails of the subunit demonstrated the role of the tails
in dodecameric assembly, in addition to the role of the C-terminal tail in DNA binding(J.Mol.Biol. 370, 752-767, 2007). We have now identified a second Dps (MsDps2) through asearch of the M. smegmatis genome, cloned and expressed it and determined its structure. The
dodecameric structure is stabler in MsDps2 than in MsDps1, substantially because the
N-terminal tail is more strongly involved in holding the subunits together than the tails are in
MsDps1. This N-terminal tail also appears to be involved in DNA binding. The structures of
MsDps1, its N- and C-terminal mutants and MsDps2 provide insights into the nuances of theassembly, DNA binding and ferroxidase activity of the Dps family.

O2A05-A2

STRUCTURL AND FUNCTIONAL STUDY OF C. ELEGANS
CELL-DEATH RELATED NUCLEASE 4 (CRN-4)
Yu-Yuan Hsiao a,b and Hanna S. Yuan baInstitute of Bioinformatics and Structure Biology, National Tsing Hua UniversitybInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan

Programmed cell death (apoptosis) is an essential biological process for development,
maintenance of appropriate cell number and 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 newly identified apoptotic nucleases in C. elegans involvedin the sequential DNA degradation process. CRN-4 interacts with several nucleases, including
CPS-6, NUC-1, CRN-1 and CRN-5, to form a multi-protein complex, named degradeosome,which promotes apoptotic DNA degradation. A DEDDh exonuclease domain is identified in
the CRN-4 and therefore CRN-4 likely bears 3’-5’ exonuclease activity, responsible forchromosome DNA nicking and/or exonuclease digestion.
To reveal the molecular basis for DNA fragmentation in apoptosis, we over expressedand purified recombinant CRN-4 from E. coli. We found that CRN-4 contains both DNase
and RNase activities and prefers dsDNA over ssDNA. The crystal structure of CRN-4 wasdetermined at a resolution of 2.5 Å by MAD method (data collected at BL12B1 in NSRRC).
CRN-4 folds into a dimer with an N-terminal DEDDh exonuclease domain and a C-terminal
domain with unknown function. The N-terminal catalytic domain adopts an α/β globular fold
and shares similar structure and catalytic residues to those of other members of DEDDh
exonucleases, such as 3’hExo and ε186. The C-terminal domain contains a novel mixed α/βfold with 7 basic residues exposing to the surface. We suggest that the C-terminal domain in
CRN-4 is involved in DNA binding in a way similar to the RNA-binding SAP domain of
3’hExo. The structural comparison of dimeric CRN-4 to several nucleases further reveals
that this protein likely recognizes DNA in a unique way than we had seen before in other
DEDD family of nucleases.

O2C05-A3

X-RAY ATOMIC ORBITAL ANALYSIS AND ITS APPLICATION TO
RARE-EARTH CRYSTALS
Kiyoaki Tanaka,a Ryoko Makita,a Shiro Funahashi,a Takashi Komori,a,b Terutoshi SakakuraaaGraduate school of engineering Nagoya Institute of Technology, Nagoya,Japan; bToyota Industries

Cooperation ,Kariya, JapanThe 4f-electron density distribution in MB6 (M=La, Ce, Sm) has been investigatedsuccessfully by the X-ray Atomic Orbital analysis (XAO) with the program QNTAO. The
quantum mechanical and crystallographic framework of it are presented.
It is the method based on the atomic orbitals (AO) and all the atoms in the unit cell are
divided into the groups of sub-shell electrons (s/p/d/f). Each AO in the crystal field isexpressed as a linear combination of sub-shell basis functions such as dxy, dyz etc. The
starting set of AO's are calculated for a single electron in the crystal field. The expansion
coefficients are determined by the least-squares method keeping the ortho-normal relationshipbetween the AO’s. In the multi-electron system, the wave function is expressed in terms of alinear combination of the anti-symmetric Slater determinants and the system splits into atomic
terms. The d3 system in the Oh crystal field with t2g2eg1 configuration for example has ten
atomic terms but the X-ray scattering factors of them always keep the contributions of the t2g
and eg electrons 2 to 1. X-ray diffraction cannot specify the atomic terms. However thisensures on the sound quantum mechanical bases that the AO's calculated for the single
valence electron are effective. Since the electron population on each AO cannot bemeasured by spectroscopy, those measured by the X-ray diffraction is very important. Eachgroup of the electrons in the same sub-shell is treated as a pseudo-atom, which enables us to
get the electron population of each AO keeping the electro-neutrality of the unit cell and trace
the electron transfer among the AO's as shown in CeB6 at low temperature.
However the XAO analysis has two limitations. First it neglects the electron
correlations. The non-integer occupation number of each AO may reflect it. Second it isbased on the AO models and does not explain two-center electrons which appear in themolecular orbital models. Therefore it is applied best to ionic crystals especially to thesystems with highly localized d and f electrons including the compounds with anon-stoichiometric structure.
The XAO analyses for 4f-EDD have given fruitful results. In CeB6 the electrons aretransferred from Ce to B6 at low temperature but they are back donated to Ce 5d orbitals not
to 4f orbitals at 430 and 535 K accompanying the inversion of 4f energy levels, which isreflected to the obtained electron population on each AO. The 5d occupation was also foundin Lab6 and SmB6 accompanying the change of the 4f energy levels.

O2A05-A4

STRUCTURE OF AN IGNAR-AMA1 COMPLEX
Victor Streltsova, Kylie Hendersona,b,c, Andrew Coleyb,c, Adrian Batchelord, Robin Andersс,Michael Foleyb,c, Stewart Nuttallaa

CSIRO Molecular and Health Technologies, Melbourne, Australia. bCooperative Research Centre for

Diagnostics, Brisbane, Australia. cSchool of Biochemistry, La Trobe University, Melbourne, Australia.
dUniversity of Maryland School of Pharmacy, Baltimore, Maryland, USA.

Apical Membrane Antigen-1 (AMA1) is essential for invasion of erythrocytes andhepatocytes by Plasmodium parasites and is a leading malarial vaccine candidate. While
antibodies to AMA1 can prevent such invasion, extensive polymorphisms withinsurface-exposed loops may limit the ability of conventional AMA1-induced antibodies toprotect against all parasite genotypes. Using an AMA1-specific IgNAR (Immunoglobulin
New Antigen Receptors) single variable domain antibody, we performed targetedmutagenesis and selection against AMA1 from three P. falciparum strains. We present
co-crystal structures of two antibody-AMA1 complexes, which reveal the extended IgNAR
CDR3 loops penetrating deep into a hydrophobic cleft on the antigen surface, and contacting
residues conserved across parasite species. Comparison of a series of affinity-enhancing
mutations allowed dissection of their relative contributions to binding kinetics, and correlation
with inhibition of erythrocyte invasion. These findings provide insights into mechanisms of
single-domain antibody binding, and will enable design of reagents targeting otherwise
cryptic epitopes in apicomplexan parasites.

O2A05-A5

STRUCTURAL AND FUNCTIONAL INSIGHTS INTO DOM34, A KEYCOMPONENT OF NO-GO MRNA DECAY
Hyung Ho Lee and Se Won Suh
Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-747,
Korea

In Saccharomyces cerevisiae, the two proteins Dom34 and Hbs1 play key roles in a
newly identified mRNA-surveillance pathway called no-go decay, by which mRNAs withtranslational stalls are endonucleolytically cleaved and subsequently degraded. However, theidentity of the endoribonuclease is unknown. Homologs of the yeast Dom34, called Pelota,
are broadly conserved in eukaryotes and archaea. Dom34/Pelota is related to the translation
termination factor eRF1.
To gain insights into the structure and function of Dom34/Pelota, we have determinedthe crystal structure of a representative member of the Dom34/Pelota family and investigated
the ribonuclease activity of Dom34. Dom34/Pelota consists of three domains of similar sizes,
with domain 1 being structurally dissimilar from domain 1 of eRF1 but resembling theRNA-binding Sm fold. The yeast Dom34 shows an endoribonuclease activity when we
assayed with defined RNA substrates containing a stem-loop, suggesting that it could be
responsible for the endonucleolytic cleavage of the stalled mRNA in no-go decay.

O2A05-A6

THE CRYSTAL STRUCTURE OF A VIRUS-LIKE PARTICLE FROM
HYPERTHERMOPHILLIC ARCAHEON PYROCOCCUS FURIOSUS
PROVIDE INSIGHT INTO THE EVOLUTION OF VIRUSES
Fusamichi Akita, Khoon Tee Chong, Hideaki Tanaka, Eiki Yamashita, Naoyuki Miyazaki,
Yuichiro Nakaishi, Kazunori Namba, Mamoru Suzuki, Tomitake Tsukihara and Atsushi
Nakagawa
Institute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan.

Pyrococcus furiosus is a hyperthermophilic archaeal microorganism found near
deep-sea thermal vents and its optimal growth temperature of 100 °C. Recently, a 38.8 kDa
protein from P. furiosus DSM 3638 was isolated and characterized1. Electron microscopy
revealed that this protein aggregated as spheres of approximately 30 nm in diameter, which
we designated P. furiosus virus-like particles (PfVs).
X-ray crystallographic analysis at 3.6 Å resolution revealed that each PfV consisted of
180 copies of the 38.8-kDa protein and retained T=3 icosahedral symmetry, as is often thecase in spherical viruses2. The total molecular mass of each particle was approximately 7
MDa. Although crystals diffracted to higher than 3.2 Å resolution, only 10 or fewer images
could be collected from a single crystal because of radiation damage. All diffraction
experiments on PfV crystals were performed using the beamline BL44XU, which is designed
for biological macromolecular assembly crystallography, at SPring-8. The crystals belonged
to the space group P41212, with cell dimensions of a = b =631.5, c = 351.3 Å. The crystal
contained half a particle in the asymmetric unit. Initial phase calculations were performed bymultiple isomorphous replacement with anomalous scattering using heavy atom clusters(SiW12, Ta6Br14), and the initial phase was calculated at 10 Å resolution. To enhance theresolution, we used conventional heavy atom compounds such as LuCl6. The 4.5 Å resolution
electron density map calculated by multiple isomorphous replacement with anomalous
scattering using the cluster compounds LuCl6 and Ta6Br12 was then improved by density
modification, including solvent flattening, histogram mapping, and NCS averaging. An
electron density map at 4-Å resolution, obtained by multiple isomorphous replacement withanomalous scattering of the heavy atom clusters SiW12 and Ta6Br14 was used as a starting
model, and the resolution was extended to 3.6 Å.
An examination of capsid structures suggested strong evolutionary links among PfV,
tailed double-stranded DNA bacteriophages, and herpes viruses. The similar
three-dimensional structures of the various coat proteins indicate that these viral capsids
might have originated and evolved from a common ancestor. The structure of PfV provides apreviously undescribed example of viral relationships across the three domains of life
(Eukarya, Bacteria, and Archaea).

O2A05-A7

HIGHER RESOLUTION STRUCTURE OF GIANT HEMOGLOBINFROM OLIGOBRACHIA MASHIKOI
Nobutaka Numoto,a,b,* Taro Nakagawa,c Akiko Kita,a,d Yuichi Sasayama,e Yoshihiro
Fukumoric and Kunio Mikia,bacGraduate School of Science, Kyoto University; bRIKEN SPring-8 Center at Harima Institution;

Graduate School of Natural Science and Technology, Kanazawa University; dResearch Reactor

Institute, Kyoto University; eInstitute of Nature and Environmental Technology, Kanazawa University,
Japan.
*

Present address; Graduate School of Natural Science and Technology, Kanazawa University.

Siboglinid polychaetes live in sulfide rich seabed and have no mouth or gut.
These
animals obtain their nutrition mainly from their symbiont which is thought to bechemoautotrophic sulfur-oxidizing bacteria.
One of the siboglinid polychaetes,
pogonophoran beard worm has 400 kDa extracellular giant hemoglobin (Hb) which cantransports oxygen and sulfide simultaneously. The symbiotic bacteria are supplied withsulfide by the giant Hb and afford host organic materials. The crystal structures of vascularand coelomic 400 kDa Hb of siboglinid polychaetes have given the insights into themechanisms of their unique properties of oxygen binding or functions of sulfide binding, butboth structures were solved with oxygenated forms at moderate resolutions.
We have
determined the crystal structure of 400 kDa Hb in partially ferric met state from a siboglinid
polychaete Oligobrachia mashikoi at 1.95 Å resolution. The electron densities at higher
resolution confirm the existence of an isomer of the B1 subunit.
The structure showed
completely lacks of electron density around distal heme pockets at the A2, B1 and B2
subunits, whereas clear peaks were observed at the A1 subunits.
Because the color of thecrystals were brown and absorption spectrum from the dissolved crystals were characteristicof that of met state, it was suggested that the obtained structure was in unliganded met forms
at three fourth subunits of the 24mer assembly and only the A1 subunits were in oxygenatedforms.
Remarkable structural changes at the AB loop regions in all subunits were seen in
the partially unliganded structure. These movements cause quaternary rearrangements ofthe dimer and the dodecamer structures, which are the common subassembly of the giant Hbs,
suggesting that the ligand induced structural changes of Oligobrachia giant Hb is quite
different from other well-studied Hbs.
We have also determined the structure of metal-binding state of Oligobrachia Hbbeyond 1.7 Å resolution.
These structures reveal that the bound metals stabilize theoxygenated form of the giant Hb.

O2B05-A1

VISUALIZATION OF RATTILING IN PrOs4Sb12 BY SINGLE CRYSTALNEUTRON DIFFRACTION
Koji Kaneko,a Naoto Metoki,a,b Hiroyuki Kimura,c Yukio Noda,c Tatsuma D. Matsudaa andMasafumi KohgidaAdvanced Science Research Center, Japan Atomic Energy Agency, Tokai, Naka, Ibaraki 319-1112,

Japan; bDepartment of Physics, Tohoku University, Sendai 980-8578, Japan; cInstitute ofMultidisciplinary Research for Advanced Materials, Tohoku University, Sendai 980-8577, Japan;dDepartment of Physics, Tokyo Metropolitan University, Hachioji 192-0397, Japan;

Recently, skutterudite compound PrOs4Sb12 was reported to be the first Pr-based heavy
fermion superconductor with Tsc=1.85 K. Since the ground state is the non-magnetic singlet,
the mechanism for the formation of heavy quasiparticles and unconventional
superconductivity attracts considerable interest. The first excited triplet state close to theground state is a suggestive of the important role of orbital degree-of-freedom in PrOs4Sb12,
which is supported by the existence of field-induced antiferroquadrupolar ordered phase.
Furthermore, since Pr ion is weakly bounded in the Sb icosahedron cage with relatively large
Pr-Sb distance, the importance of “rattling”, large thermal vibration of Pr, and the possible
existence of off-center potential minima are also discussed in connection with the emergenceof superconductivity. A combination of the single crystal neutron diffraction and the analysis
with using maximum entropy method (MEM) offers an ability to unveil rattling motion of Pr
in PrOs4Sb12 without any specific model. A space-, time-averaged nuclear density distribution
reflecting a thermal vibration can be obtained by a MEM analysis. The results unveil a widely
spread anisotropic Pr distribution in the Sb cage at room temperature. The Pr density has a flat,
trapezoidal distribution in the real space, where the width reaches roughly 0.6 Å in the full
width at half maximum (FWHM). In contrast, the Pr nuclear density distribution at 8 K
becomes sharp, almost isotropic and gaussian-form, although the width of 0.15 Å in FWHM
is roughly twice broader than those for Os and Sb. Note that the highest density of Pr
distribution at 8 K founds at the center of the cage within an experimental accuracy. Thesefeatures are far from the simple harmonic model, namely, the present result suggests thestrong anharmonicity for the Pr potential in the Sb cage.

O2B05-A2

SINGLE CRYSTAL NEUTRON DIFFRACTION INVESTIGATIONS OF
TYPE I CLATHRATES – POTENTIAL THERMOELECTRIC
MATERIAL
Mogens Christensen1, Bo B. Iversen2.
1

Bragg Institute, ANSTO, Lucas Heights, Australia; 2Department of Chemistry, University of Aarhus,

Aarhus, Denmark

Inorganic clathrates with type I structure are potential thermoelectric materials. One of
the key properties is an extremely low lattice thermal conductivity. Despite the perfect
crystallinity of the type I clathrates they conduct heat like a glass. The low thermal
conductivity can be related to guest atom inclusions in a host structure. The clathrate structureis shown in Figure 1, where the cage structure is shown by polygons.
We have investigated various clathrates type I using single crystal neutron diffraction
and resonant synchrotron X-ray diffraction [1]. The guest atom siting in the host structure has
been investigated. Multi-temperature diffraction data has been measured to reveal dynamic
properties of the clathrates by modelling the atomic displacement parameters. The
investigations have revealed a important host-guest interaction in the clathrates. The hostguest coupling appears to be responsible for off-centring of the guest atom and thereby
causing disorder of the guest atom. This in turn leads to the low thermal conductivity.

Figure 1: The clathrate type I structure.
Reference:[1] M. Christensen, et al., 2006 J. Am. Chem. Soc. 128 15657-65

O2B05-A3

X-RAY SCATTERING STUDY OF RB4
Ki Bong Lee,a S. Ji,a C. Song,a J. Koo,a Y. J. Park,b J. Y. Kimc and B. K. ChocaeSSC and Department of Physics; bPohang Accelerator Laboratory, POSTECH, Pohang 790-784

Korea;cDepartment of Materials Science and Engineering, GIST, Gwangju 500-712 Korea

RB4’s manifest very rich interesting phenomena originating from spin-, orbital- andlattice orderings at low-temperature. Since resonant x-ray scattering (RXS) is sensitive tothem, it provides a unique opportunity to study them at the same time. RXS measurements
were performed on GdB4 and DyB4 single crystals.
GdB4 with isotropic Gd 4f shells shows only antiferro-type spin orderings at low
temperature while DyB4 with anisotropic Dy 4f shells shows both spin- and quadrupolarorderings. From analyses of azimuthal angle dependences of RXS signals and theirpolarizations at different x-ray energy, we were able to identify peaks corresponding tomagnetic ordering, quadrupolar ordering and structural anisotropic tensor susceptibility (ATS)scattering, which demonstrates the potential of RXS as a powerful spectroscopic probe withadditional selection rules. Moreover, a coupling between quadrupolar order and strain, which
has not been experimentally verified for decades, was directly demonstrated in DyB4 byobserving that the two order parameters are proportional to each other. The details of theexperiments and analyses will be presented.

O2B05-A4

HYDROGEN BONDING PHASE TRANSITIONS IN SOME ORGANICCRYSTALS
Hoong-Kun Fun,a Beck-Sim Leea and Suchada Chantraprommaba

X-ray Crystallography Unit, School of Physics, Universiti Sains Malaysia, 11800 USM, Penang,b

Malaysia. Department of Chemistry, Faculty of Science, Prince of Songkla University, Hat-Yai,
Songkhla 90112, Thailand.

Our study of solid state hydrogen bonding in phenol-amine adducts and benzoic
acid-amine adducts has lead us to discover a new type of phase transition(Fun-Anwar-Suchada Transition or abbreviated as FAST) which we attribute to originate
from hydrogen bonding. Some crystals of the phenol-amine adducts and benzoic acid-amine
adducts undergo a distortive reversible temperature-dependent phase transition. In thosecrystals the structural phase transition is sometimes from orthorhombic-to-monoclinic ; frommonoclinic-to-triclinic ; and from triclinic to triclinic. We have identified and clarified theprimary order parameter of these structural phase transitions and a phenomenological Landau
theory of ferroelastic phase transitions was developed which was shown to be consistent withthe experimental data on the temperature dependence of the unit cell parameters [1, 2].
As is well known, the phenomenological theory, being a macroscopic theory, cannot
describe the microscopic interactions causing the phase transition, although it certainly does
play an important role in identifying the primary order parameter and giving insight into theoverall qualitative thermodynamic behaviour of the transition.
A microscopic theory [3], formulated through a mean field calculation of thethermodynamic behaviour using a variational method, was able to explain the main featuresof the phase transition, in agreement with the Landau theory of ferroelastic phase transitions.
The essential physical mechanism proposed in the microscopic theory is that the interactionsof the hydrogen bonds with phonons induce indirect long range interactions between thehydrogen bonds. The cooperative interactions between the hydrogen bonds drive thestructural phase transition.
The experimental and theoretical aspects of FAST shall be explained in this talk.
References:
1. H. -K. Fun, A. Usman, S. Chantrapromma, J. Osman, L.-H. Ong, D. R. Tilley & Y. Ishibashi. Phasetransitions in hydrogen-bonded phenol-amine adducts: analysis by ferroelastic theory. Solid State Comm. 2003.
127, 677-682.
2. H. –K. Fun, Mohd Mustaqim Rosli, Beck-Sim Lee, Lye-Hock Ong, Suchada Chantrapromma. First ordertemperature-dependent phase transition of hexamethylenetetraminium 3,5 dinitrobenzoate hemihydrate crystal:
Landau phenomenological theory approach. Journal of Molecular Structure 2007. 837, 132-141.
3. P. -T. How, B. -S. Lee, H. -K. Fun, I. A. Razak, S. Chantrapromma. Microscopic theory of phase transitions inhydrogen-bonded phenol-amine adducts. Phys. Rev. B. 2005. 71, 174109.

O2B05-A5

DIFFRACTION STUDIES OF RELATION BETWEEN HELICITY OF
CYCLOID MAGNETISM AND FERROELECTRIC POLARIZATION IN
MULTIFERROIC MANGANESE OXIDES
Taka-hisa Arima,a,b Hajime Sagayama,a Nobuyuki Abe,a Koji Taniguchi,a Hiroyuki
Ohsumi,b,c Masato Matsuura,d Kazuma Hirota,d Daisuke Okuyama,e Yuichi Yamasaki,f andYoshinori Tokurae,faInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, Japan; bSPring-8

Center, Harima Institute, RIKEN, Japan; cJapan Synchrotron Radiation Research Institute, Japan;dInstitute of Solid State Physics, University of Tokyo, Japan; eERATO Multiferroic Project, Japan

Science and Technology Agency, Japan; fDepartment of Applied Physics, University of Tokyo, Japan

Since Kimura et al. discovered the polarization flop in TbMnO3 induced by theapplication of a magnetic field, the interplay between magnetic ordering and ferroelectric
polarization in multiferroics has become of great interest. Extensive studies havesuccessively indicated that the cycloid-type spin ordering should produce ferroelectric
polarization through the inverse effect of Dyaloshinski-Moriya (DM) interaction. If theinverse DM effect would play an essential role in the ferroelectric polarization of such cycloid
magnets, the direction of polarization should be associated with the helicity of the cycloid.
Spin-polarized neutron technique is the most powerful probe into the helicity of spiralmagnets. We have carried out a spin-polarized neutron diffraction study on TbMnO3 byusing a triple-axis neutron spectrometer PONTA at JRR-3, Japan. The experimental resultclearly demonstrates the anticipated connection between the ferroelectricity and cycloid. We
also performed an x-ray magnetic scattering study at SPring8, Japan, to reveal the spin
helicity in DyMnO3.

O2B05-A6

STRUCTURE OF SrTiO3-DOPED LaAlO3 PEROVSKITE
N. Ishizawa a, Y. Inagaki a, T. Shimada b, I. Kagomiya a, K. Kakimoto a, and H. Ohsato aab

Nagoya Institute of Technology, Nagoya, Japan. Hitachi Metals, Ltd. Japan

Recently the sintered samples of (La1−xSrx)(Al1−xTix)O3 perovskite-type solid solution
are found to have higher quality factors than that of LaAlO3, peaking Qf=165THz at x~0.2 1).
Single crystals of x=0.05 and 0.20 were grown by the floating-zone method 2), and the former
showed much improved Qf. The crystals, however, possessed very weak intensities at thereciprocal lattice points forbidden for the space group R 3 c which is commonly assumed forthe rhombohedral distortion of the ideal perovskite (Pm 3 m). The present study reveals thatthe (La1−xSrx)(Al1−xTix)O3 perovskite-type crystals (x=0.05 and 0.2) belongs to R 3 whichaccommodates two crystallographically independent octahedral sites for Al(Ti). Ti atoms are
preferentially concentrated on the larger octahedron. The ordered distribution of Ti could
explain the property that the SrTiO3-doped compounds have higher Qf than pure LaAlO3.
Discussion will be given on the reasons why the symmetry of SrTiO3-doped crystals differsfrom the pure LaAlO3 3-4), the end member of the ‘solid solution’.
Reference:
1) T. Shimada et al., J. Euro. Ceram. Soc. 26, 2017-21 (2006)
2) Y. Inagaki et al., J. European Ceram. Soc. 27, 2861-64(2007)
3) C. J. Howard et al., J. Phys.: Cond. Mat. 12 349-65 (2000).
4) H. Lehnert et al., Z. Kristallogr. 215 536-41 (2000).

O2C05-A1

SINGLE CRYSTAL STRUCUTURE ANALYSIS OF PHOTO-EXCITED
STATES OF HALOGEN-BRIDGED DICOPPER(I) COMPLEXES
Yoshiki Ozawa,a Shingo Yoshida,a Nobuyuki Kitayama,a Minoru Mitsumi,a Koshiro Toriumi,b
Kiyoshi Tsuge, bHiromi Araki, and bYoichi SasakiaGraduate School of Material Science, University of Hyogo, Hyogo, 678-1297 Japanb

Graduate School of Science, Hokkaido University, Sapporo, 060-0810 Japan.

Photo-luminescent halogen-bridged dicopper(I) complexes [Cu2X2(PPh3)2(L)]∞ (L=4,4’-bipyridine or pyrazine, X = I or Br) consist of {Cu2X2} planer units, which are bridged
by diimine (L) ligands constructing infinite 1-D chain structures [1]. The assignments ofintense emission bands of these halogen-bridged oligo-cupper(I) compounds are complicate
because weak interacted multi-copper centered (CC) transition states are often concurrent
with common Cu(I) to ligand charge transfer (MLCT) states. We have tried to observe direct
geometrical distortion of the complex by photo exited state crystallographic technique inorder to figure out these emission natures. We also have made the same experiments fordiscrete dimeric copper(I) complexes [CuI2(PPh3)2(L’)]2] (L’ = phenylpyridine, pyrazine)
having similar metal-organic frameworks which show less luminescent performance.
Single crystal X-ray diffraction experiments were performed by using the lowtemperature vacuum X-ray camera at SPring-8 BL02B1 beamline. Full intensity data of bothunder light irradiated by CW laser, (442nm or 488nm) and non-irradiated conditions werecollected by multiple-exposure IP method. Photo-difference Fourier syntheses for theirradiation show that a small portion of two Iodine atoms shift toward close to each other inthe {Cu2I2} plane. Two Cu atoms tend to shift slightly apart from each other. Results of theleast-square refinements of I and Cu atom positions based on the response ratio[2] show that
there are 1.1 % excited-state species in the crystal in which the I···I distance (3.82(2)Å) is
contracted from the ground states (4.41(1)Å). While in the case of the discrete dimer
complex [CuI2(PPh3)I(pyz)2], two iodine atoms tend to move out of the {Cu2I2} plane with
opposite direction each other. This indicates that the {Cu2I2} framework rotates around an
axis containing two Cu atoms. This variety of the motions of {Cu2I2} frameworks will beconcerned with the geometry of the frame at the ground state and solid-state luminescent
properties. Details of the relationship between optical properties and excited state moleculargeometries will be discussed.
Reference:[1] H. Araki, K. Tsuge, Y. Sasaki, S. Ishizaka and N. Kitamura, Inorg. Chem., 2005, 44, 9667-9675.
[2] Y. Ozawa, M. R. Pressprich and P. Coppens, J. Appl. Cryst., 1998, 31, 128-135.

O2C05-A2

INVESTIGATION OF THE PHOTOEXCITED CHARGE-TRANSFER
STATE OF [AuBr(PPh3)2] BY THE MULTIPLE-EXPOSURE IP METHODManabu Hoshino,1 Hidehiro Uekusa,1 Shintaro Sonoda,1 Takuhiro Otsuka,1 Youkoh Kaizu,1Yoshiki Ozawa,2 Koshiro Toriumi2
12Department of Chemistry and Materials Science, Tokyo Institute of Technology, Tokyo, Japan;
Graduate School of Material Science, University of Hyogo, Hyogo, Japan

Three-coordinated gold(I) complexes, [AuX(PPh3)2](X= Cl, Br, I), show strong uminescence, of whichapplication to the EL materials is expected. The origin ofemission is suggested to be related with molecular structuralchange by photoexcitation. However, three-dimensional
structure in the photoexcited state of these complexes is not
Scheme [AuBr(PPh3)2]
clear yet. In our previous study of [AuCl(PPh3)2],
photo-induced structural change was observed as shrinkage of all metal–ligand bonds. In thisstudy, the change of electron density distribution of [AuBr(PPh3)2] (scheme) by
photoexcitation was investigated by using the accurate diffraction method, multiple-exposure
IP method on the low-temperature vacuum X-ray camera at SPring-8 BL02B1.
Diffraction intensity data at the light-on and -off stages were collected in the same IP
frame by the multiple-exposure IP method. Difference Fourier synthesis on the Fo values oflight-off and -on stages (Fo(on) – Fo(off)) showed that charge transfer from the Br atom to the
Au atom (halide-to-metal charge-transfer; XMCT) was occurred by photoirradiation (shownin Figure). The results of DFT calculation on
triplet excited state of [AuBr(PPh3)2] alsosuggest generation of the photoexcited XMCT
state. Although the complexes have similar
structure, the difference in the character of
excited states between [AuCl(PPh3)2] (bonds
shrinkage) and [AuBr(PPh3)2] (XMCT) can
explain the emission color difference (λmax =520 nm and λmax = 460 nm, respectively).
Figure Fo(on) – Fo(off) map of [AuBr(PPh3)2]

O2C05-A3

X-RAY ATOMIC ORBITAL ANALYSIS AND ITS APPLICATION TO
RARE-EARTH CRYSTALS
Kiyoaki Tanaka,a Ryoko Makita,a Shiro Funahashi,a Takashi Komori,a,b Terutoshi SakakuraaaGraduate school of engineering Nagoya Institute of Technology, Nagoya, Japan; bToyota Industries

Cooperation, Kariya, JapanThe 4f-electron density distribution in MB6 (M=La, Ce, Sm) has been investigatedsuccessfully by the X-ray Atomic Orbital analysis (XAO) with the program QNTAO. The
quantum mechanical and crystallographic framework of it are presented.
It is the method based on the atomic orbitals (AO) and all the atoms in the unit cell are
divided into the groups of sub-shell electrons (s/p/d/f). Each AO in the crystal field isexpressed as a linear combination of sub-shell basis functions such as dxy, dyz etc. The
starting set of AO's are calculated for a single electron in the crystal field. The expansion
coefficients are determined by the least-squares method keeping the ortho-normal relationshipbetween the AO’s. In the multi-electron system, the wave function is expressed in terms of alinear combination of the anti-symmetric Slater determinants and the system splits into atomic
terms. The d3 system in the Oh crystal field with t2g2eg1 configuration for example has ten
atomic terms but the X-ray scattering factors of them always keep the contributions of the t2g
and eg electrons 2 to 1. X-ray diffraction cannot specify the atomic terms. However thisensures on the sound quantum mechanical bases that the AO's calculated for the single
valence electron are effective. Since the electron population on each AO cannot bemeasured by spectroscopy, those measured by the X-ray diffraction is very important. Eachgroup of the electrons in the same sub-shell is treated as a pseudo-atom, which enables us to
get the electron population of each AO keeping the electro-neutrality of the unit cell and trace
the electron transfer among the AO's as shown in CeB6 at low temperature.
However the XAO analysis has two limitations. First it neglects the electron
correlations. The non-integer occupation number of each AO may reflect it. Second it isbased on the AO models and does not explain two-center electrons which appear in themolecular orbital models. Therefore it is applied best to ionic crystals especially to thesystems with highly localized d and f electrons including the compounds with anon-stoichiometric structure.
The XAO analyses for 4f-EDD have given fruitful results. In CeB6 the electrons aretransferred from Ce to B6 at low temperature but they are back donated to Ce 5d orbitals not
to 4f orbitals at 430 and 535 K accompanying the inversion of 4f energy levels, which isreflected to the obtained electron population on each AO. The 5d occupation was also foundin Lab6 and SmB6 accompanying the change of the 4f energy levels.

O2C05-A4

STRUCTURES OF POLYPYRIDINE MONONUCLEAR IR(III)COMPLEXES IN THE CLOSED-SHELL SINGLET AND TRIPLETSTATES
Naokazu Yoshikawa,a Shinichi Yamabe,b Nobuko Kanehisa,c Yasushi Kai,d Hiroshi
Takashima,a and Keiichi TsukaharaaaDepartment of Chemistry, Nara Women’s University; b Department of Chemistry, Nara University of

Education y; cDivision of Electrical, Electronic and Information Engineering, Osaka
University.dDepartment of Environmental and Biotechnological Future Engineering, Fukui Universityof Technology

Structures of eight Ir3+ centered polypyridine complexes were determined by density
functional theory calculations. The crystal structure of [IrCl(bpy)(terpy)](PF6)2 was obtainedby the X-ray diffraction study, where bpy is 2, 2’- bipyridine and terpy is2,2’:6’,2”-terpyridine. The computed geometries are in good agreement with the experimental
ones. Those in the triplet biradical states were also determined to evaluate the singlet–triplet
energy differences. These differences correlate well with wavelengths of the emission spectra.
The geometric changes, free tolyl ligand → the Ir3+ complexed ligand → the ligand in the
triplet biradical, were examined. It was found that one not two large-conjugated polypyridine
ligand with spin delocalizable substituents may give efficient phosphorescence to explore the
LED device.

O2C05-A5

APEX II ULTRA - PRECISION AND ACCURACY
Michael Rufa, Martin Adamb,a

Bruker AXS Inc., 5465 East Cheryl Parkway, Madison,WI, USA,.bBruker AXS B.V, Oostsingel 209,

2612 HL Delft, The Netherlands.

The APEX II ULTRA is Bruker’s top of line crystallographic instrumentation forchemical crystallography. The system combines the most sensitive CCD detector with thebrightest Molybdenum source and the most advanced multilayer optics available in a very
compact format.
The rotating anode is so compact that it can be mounted on the goniometer, setting new
standards in ease and stability of alignment. A very small focal spot combined with the
HELIOS optics produce a small high flux beam of only 150 micrometer which can increase
integrated intensities from small crystals by a factor of 60 compared to standard sealed tube
systems. The APEX II ULTRA’s ingenious design allows for a variable beam size withconstant flux which allows changing the beam size to 360 micrometer within minutes withoutchanging expensive component.

This presentation will introduce the instrumentation and present examples of charge
density studies, data collected on very small crystals and powder diffraction experiments
focusing on aspects of precision and accuracy in crystallographic experiments.

O3A06-M1

FLUORESCENCE-DETECTION SIZE EXCLUSIONCHROMATOGRAPHY FOR PRECRYSTALLIZATION SCREENING OF
INTEGRAL MEMBRANE PROTEINS
Toshimitsu Kawatea, Atsuko Yamashitab, Jaysankar Jastia, Michael Rosconia, Paul Shaffera,
Alexander Sobolevskya, Tanja Homrichhausena and Eric Gouauxa,ca

The Vollum Institute at Oregon Health and Science University, Portland, USA ;bStructural Physiology

Research Group, RIKEN Spring-8 Center, Japan ;cHoward Hughes Medical Institute, USA.

Formation of well ordered crystals of membrane proteins is a bottleneck for structure
determination by x-ray crystallography. Nevertheless, one can increase the probability ofsuccessful crystallization by precrystallization screening, a process by which one analyzes themonodispersity and stability of the protein-detergent complex. Traditionally, this has required
microgram to milligram quantities of purified protein and a concomitant investment of timeand resources. Here we show a rapid and efficient precrystallization screening strategy inwhich the target protein is covalently fused to green fluorescent protein (GFP) and theresulting unpurified protein is analyzed by fluorescent-detection size exclusion
chromatography (FSEC). This strategy requires only nanogram quantities of unpurified
protein and allows one to evaluate localization and expression level, degree of monodispersity,and approximate molecular mass. We have applied this screening strategy to six different
integral membrane proteins and found promising target proteins for crystallization. We findthat the probability of obtaining a well-behaved protein is about one in twenty, and mostimportantly, all of such "hits" have been successfully crystallized. In this talk, I show theapplication of this precrystallization screening to integral membrane proteins derived fromprokaryotic or eukaryotic organisms.

O3A06-M2

ION BINDING AND SELECTIVITY OF THE ROTOR OF THE V-TYPE
NA+-ATPASE FROM ENTEROCOCCUS HIRAE
Takeshi Murata1,2,3, Ichiro Yamato4, Yoshimi Kakinuma5, Mikako Shirouzu3, John E. Walker6,
Shigeyuki Yokoyama3 and So Iwata1,2,3
1

Department of Cell Biology, Faculty of Medicine, Kyoto University, Japan, 2Japan Science andTechnology Agency, ERATO, Iwata Human Receptor Crystallography Project, Kyoto, Japan, 3Protein
Research Group, RIKEN Genomic Sciences Center, Yokohama, Japan, 4Department of Biological
Science and Technology, Tokyo University of Science, Noda, Japan, 5Faculty of Agriculture, Ehime
University, Matsuyama, Japan, 6Medical Research Council Dunn Human Nutrition Unit, Hills Road,
Cambridge, United Kingdom

In eukaryotic cells, vital processes such as protein trafficking, endocytosis,
neurotransmitter release and intracellular pH regulation, depend on the movement of ions
across membranes by vacuolar- or V-ATPases, multisubunit complexes related to the
F-ATPases (ATP synthetases) found in eubacteria, mitochondria and chloroplasts. Bothclasses have globular catalytic domains, V1 and F1, where ATP is hydrolysed (or synthesized),
attached by central and peripheral stalks to intrinsic membrane domains, Vo and Fo, whereions are pumped across the membrane. ATP hydrolysis generates rotation of the central stalkand an attached membrane ring of hydrophobic subunits. Ions are pumped through a pathway
in the interface between the rotating c ring and subunit a as a static membrane component,
which is linked to the outside of the V1 or F1 domain by the peripheral stalk.
V-type Na+-ATPase of Enterococcus hirae transports Na+ as well as Li+ ions rather thanprotons under physiological conditions. Here, we report ion binding/release properties of therotor ring of this enzyme. The purified K-ring in detergent bound one Na+ ion per K-monomerwith high affinity (KD(Na+) = 12 µM). The 22Na+ binding to K-ring was inhibited by Li+ (Ki =48 µM) or H+ (Ki = 3.4 µM: pH 5.5) competitively but not by K+, Tl+, Rb+, Cs+, Mg2+ or Ca2+,
suggesting that the ion binding pocket in the K-ring accommodates only Na+, Li+ or H+. The
structure of the K-ring in the presence of Li+ resolved at 2.8 Å suggested that Li+ ion is boundto the specific binding pocket surrounded by five oxygen atoms like as Na+ in the Na+ boundK-ring structure (T. Murata et al., 2005, Science, 308, 654-659) with slight different distances
between the cation and oxygens. Association and dissociation rates of the 22Na+ to and fromthe rotor ring were extremely slow (kon = 1 x 102 [M-1S-1], koff = 1 x 10-3 [S-1]) when comparedwith the rates of enzyme activity of the purified whole complex in detergent, consistent withthe model that Na+ binding/release reaction for transport of the V-ATPase is accomplished at
the interface between I-subunit and K-ring during rotation. From these results, we discuss
about ion selectivity and ion transport mechanism of the E. hirae V-ATPase.

O3A06-M3

X-RAY STRUCTURE OF BOVINE HEART CYTOCHROME COXIDASEH. Aoyamaa*, T. Tsukiharab and S. YoshikawacaGraduate School of Pharmaceutical Sciences, Osaka University, bInstitute for Protein Research,

Osaka University, cDepartment of Life Science, University of Hyogo.

The mammalian mitochondrial branched-chain-α-ketoacid dehydrogenase (BCKD)
complex, containing E1, E2, and E3 domains, catalyzes the oxidative decarboxylation of
branched-chain-α-ketoacids derived from leucine, isoleucine, and valine, hence, gives rise tobranched-chain acyl-CoAs. The transacylase subunit (E2) of BCKD complex carries three
independently folded domains linked together by flexible loops: the hbLBD (a.a. 1-84),
hbSBD (a.a. 104-152), and di-domain (hbDD) comprising residues 1–168 of E2. With
multidimensional heteronuclear NMR techniques, the structures and dynamics of the threetruncated fragments were determined, respectively. For the quaternary structure, solution
small angle X-ray scattering (SAXS) result reveals a linear-like arrangement of the
sub-complex of hbLBD linked with hbSBD (DD) by the flexible chains, based on a rigid bodyrefinement of the two individual structures of LBD and SBD determined by NMR.
Furthermore, from the changes of the SAXS profile of the E1 component of BCKD, upon thebinding of the DD sub-complex, most likely, the DD sub-complex keeps a free LBD end after
the binding to the E1 domain.

SBD
Intensity

LBD

Q (Å-1)
Fig. 1: A quaternary model and the protein envelope deduced from the SAXS data for the sub-complex DD(LBS+SBD) of BCKD, using rigid body refinement with the PDB data of each component.

O3A06-M4

STRUCTURE OF THE CYTOCHROME b6f COMPLEX: QUINONEANALOGUE INHIBITORS AS LIGANDS OF HEME cn
Eiki Yamashitaa,b, Huamin Zhanga, c, William A. CrameraaDepartment of Biological Sciences, Purdue University; cAptuit, Inc., West Lafayette, IN, USA;b

Institute for Protein Research, Osaka University, Suita, Japan

The integral-membrane cytochrome b6f complex mediates electron transfer between thephotosystem II and photosystem I reaction center complexes. The electron transfer is linked toproton translocation across the membrane. Crystal structures of the b6f complex from thethermophilic cyanobacterium, M. laminosus [1] and the green alga, C. reinhardtii [2] weresolved in 2003. In the crystal structures, a unique covalently bound heme, heme cn, was foundvery close to heme bn on the electrochemically negative side of the complex. Heme cn has no
amino acid side chain as an axial ligand, but has an axial H2O that bridges heme cn and thepropionate of heme bn. The function of heme cn is still not understood.
The native crystal grown in the presence of Cd2+ of the cytochrome b6f complex fromM. laminosus resulted in an improvement of the native structure from 3.4 Å [1] to 3.0 Å [3].
In the native structure with Cd2+, two Cd2+ binding sites are located in each monomer.
Binding sites of quinone analogue inhibitors, tridecyl-stigmatellin (TDS) and2n-nonyl-4-hydroxy-quinoline-N-oxide (NQNO), were sought to map the transfer pathway ofthe lipophilic quinone across the complex [3]. Two sites were found for the chromone ring of
the TDS quinone analogue inhibitor, one near the p-side [2Fe-2S] cluster. A second TDS site
was found on the n-side of the complex facing the quinone exchange cavity as an axial ligandof heme cn. A similar binding site as an axial ligand to heme cn was found for the n-side
quinone analogue inhibitor, NQNO. Binding of NQNO and TDS as axial ligands to heme cn
implies that this heme utilizes plastoquinone as a natural ligand, thus defining an n-side
electron transfer complex consisting of hemes bn, cn, and plastoquinone (PQ) in the reduction
pathway of the PQ pool.
Reference:[1] Kurisu et al., Science, 2003
[2] Stroebel et al., Nature, 2003
[3] Yamashita et al., JMB, 2007

O3A06-M5

X-RAY STRUCTURE OF EmrE SUPPORTS DUAL TOPOLOGY MODEL
Yen-Ju Chen, Owen Pornillos, Samantha Lieu, Che Ma, Andy P. Chen, Geoffrey Chang
Genomics Research Center of Academia Sinica, Taiwan

EmrE, a multidrug transporter from Escherichia coli, functions as a homodimer of asmall four-transmembrane protein. The membrane insertion topology of the two monomers is
controversial. Although the EmrE protein was reported to have a unique orientation in themembrane, models based on electron microscopy (EM) and now defunct x-ray structures, aswell as recent biochemical studies posit an antiparallel dimer. We have now reanalyzed our xray data on EmrE. The corrected structures in complex with a transport substrate are highly
similar to the EM structure. The first three transmembrane helices from each monomer
surround the substrate-binding chamber, whereas the fourth helices participate only in dimer
formation. Selenomethionine markers clearly indicate an antiparallel orientation for themonomers, supporting a “dual topology” model.

O3B06-M1

MOMENTUM DEPENDENT CHARGE EXCITATIONS IN
CORRELATED ELECTRON SYSTEMS STUDIED BY RESONANT
INELASTIC X-RAY SCATTERING
Kenji Ishii
Synchrotron Radiation Research Unit (SPring-8), .Japan Atomic Energy Agency, Hyogo 679-5148,
Japan

Resonant inelastic x-ray scattering (RIXS) in the hard x-ray regime is a developing
experiment technique to measure charge excitations utilizing brilliant synchrotron radiation
x-rays. It has a great advantage that the momentum dependence of electronic excitations canbe measured unlike conventional optical method. In addition, RIXS gives element-selective
excitation spectra by tuning the incident photon energy to an absorption edge of the element.
There has been much activity in recent years using this technique, especially at the transition
metal K-edge to study transition metal oxides.
We have applied RIXS technique to correlated electron systems, such as cuprates andmanganites, in order to understand their electronic structure and underlying correlation effects.
In particular, electronic structure of correlated metals is in the focus of our RIXS study,
because interesting phenomena, e.g. high-Tc superconductivity in cuprates and colossal
magneto resistance in manganites, occur in the vicinity of metal-insulator transition by carrier
doping.
Here I would like to present our recent RIXS studies on high-Tc cuprates and relatedmaterials which were performed in close collaboration with theorists. Momentum andcarrier-doping dependence of an interband excitation across the Mott gap and an intraband
excitation below the gap will be discussed.

O3B06-M2

SPIN, CHARGE, AND ORBITAL ORDERING OF
TRANSITION-METAL OXIDES INVESTIGATED BY RESONANT
SOFT X-RAY SCATTERING
Di-Jing Huang
National Synchrotron Radiation Research Center, Hsinchu, Taiwan
Department of Physics, National Tsing Hua University, Hsinchu, Taiwan

Many phase transitions of correlated-electron materials are closely related to spin,
charge, and orbital ordering. In this talk, we will present our recent studies of soft x-ray
scattering on spin, charge, and orbital ordering associated with metal-insulator transition,
multiferroicity, and dimensional crossover of antiferromagnetism in transition-metal oxides.
We will first address the long-lasting debate on the existence of charge ordering of
Fe3O4 which exhibits a classic example of phase transition known as the Verwey transition.
Such a transition was originally interpreted as a charge order-disorder transition. Despite
intensive investigations over 60 years, the existence of charge ordering in magnetite remains
controversial. Using measurements of resonant soft x-ray scattering, we report direct
experimental evidence for the existence of charge-orbital ordering in magnetite [1] and thedata corroborate the LDA+U prediction [2].
We will also cover antiferromagnetism and multiferroicity of TbMn2O5. Recent
discovery of giant magetoelectric effects offers new opportunities of multiferroic applications.
However, the lack of direct scattering evidence for the multiferroicity has limited theunderstanding of the microscopic mechanism behind such giant cross-coupling effects. We
proffer scattering evidence for multiferroicity and a new pathway for understanding the
intricate coupling between antiferromagnetism and ferroelectricity in frustrated magnets [3].
Our results set fundamental symmetry constraints on the microscopic mechanism ofmultiferroicity in frustrated magnets.
The final subject is dimensional crossover of antiferromagnetism in La0.5Sr1.5MnO4 [4].
We for the first time observed quasi-2D incommensurate AF order existing at temperatures
above the Neel temperature (TN). As the temperature cools across TN, on top of thedimensional crossover, the 2D incommensurate AF order collapses to stabilize the 3D
commensurate AF order. Our results show that the spin correlation follows the same
exponential growth in inverse temperature as those observed in quantum Heisenberg
antiferromagnets.
Reference[1] D. J. Huang et al., Phys. Rev. Lett. 96, 096401 (2006).
[2] H. T. Jeng, G. Y. Guo, and D. J. Huang, Phys. Rev. Lett. 93, 156403 (2004).
[3] J. Okamoto et al., Phys. Rev. Lett. 98, 157202 (2007).
[4] K. S. Chao et al., submitted to Phys. Rev. Lett.

O3B06-M3

WIGNER CRYSTALLIZATION IN A MOLECULAR CONDUCTOR,(DI-DCNQI)2Ag
Hiroshi Sawa a, Toru Kakiuchi a, Yusuke Wakabayashi a, and Kazushi KanodababPhoton Factory, High Energy Accelerator Research Organization (KEK), Tsukuba,
Department of Applied Physics, the University of Tokyo, Tokyo, Japan

Rarefied electron gas system at high temperature is homogeneous due to the large
kinetic energy compared to the Coulomb repulsion among electrons. At extreme lowtemperatures, the system will tend to condense and make uneven lumps, as theoretically
predicted in the early 1930's. Since these lumps carry a negative charge, they form a structure
where they try to avoid each other in the spatial positioning. We call this phenomenon the
Wigner crystallization.
A molecular conductor (DI-DCNQI)2Ag is insulating even at room temperature. Planar
DCNQI molecules are piled up at even intervals along the c direction, composing 1D columns.
Since Ag is a monovalent ion having a closed shell, they construct a quarter-filled 1D-electron
band. Below 220 K, Hiraki et al. suggested that the 4kF Wigner crystal type of charge order(CO) on DCNQI molecules arose in the low-temperature phase by NMR technique. This CO
ground state was theoretically predicted by Seo et al. It is very interesting whether (or how)the electron crystal is stable in the real solid.
Single crystal x-ray diffraction measurements usingsynchrotron radiation were performed on a large warped
imaging plate camera installed on beam lines BL-1A at
PF, KEK. According to the result of the structural
analysis, two-fold structure in ground state consists of not
only charge ordering columns but also monotonic charge
dimerized columns caused by geometrical frustration
among DCNQI columns. This charge ordered structure is
regarded as a Wigner crystal caused by inter-column
Coulomb repulsion (Fig.1)[1].
Figure.1. Three-dimensional view of
the Wigner crystal-type charge

Reference:[1] T. Kakiuchi, et al., Phys. Rev. Lett., 98 (2007) 066402.

arrangement and the molecules.
Charge-rich areas are shown by red
ellipses, forming a body-centered
tetragonal lattice drawn by the bluelines.

O3B06-M4

Q-DEPENDENT DIELECTRIC FUCTION STUDIES USINGINELASTIC X-RAY SCATTERING
N. Hiraoka, H. Ishii, I. Jarrige, and Y. Q. Cai,
National Synchrotron Radiation Research Center, Hsinchu, Taiwan, 300, R.O.C.

Inelastic x-ray scattering (IXS) probes the excited states of materials, like opticalabsorption using visible or ultraviolet photons. Optical absorption observes the excitations
at the limit of zero momentum transfer (q→0), while IXS investigates the excitations as afunction of q. (Non-resonant) IXS is a similar experiment to electron energy loss spectroscopy(EELS) in this sense, but it has advantages of (i) small effects of multiple scattering and (ii) a
wide q range, covering several Brillouin zones. However, the scattering cross-section of
non-resonant IXS is extremely small, and thus it is not a very popular method at the moment,
compared with EELS or resonant IXS (RIXS). Nevertheless, it is possible to extract important
information in understanding the electronic structures of solids using non-resonant IXS if one
combines a high-brilliance synchrotron radiation source and optimized x-ray optics. We will
discuss the following two examples.
1. Semi-metal, graphite: The graphite is semi-metal and only has a Fermi surface along theK-H line in the Brillouin zone (Fermi line). This fact is well-known but there are very few
reports that have clearly observed the semi-metallic features. The IXS spectra that wehave obtained show clear semi-metallic features, exhibiting that the energy gap repeats the
opening and closing as a function of q.
2. Strongly correlated system, NiO: NiO is still extensively studied by various
experimentalists and theorists because it is a prototype of strongly correlated systems,
which still present many challenges to theoretical modelling. The IXS spectra show
characteristic q-dependences of the intensities of dd (intratomic) excitations and chargetransfers, corresponding to the spatial extent of these excitations.

O3B06-M5

CRYSTAL AND MAGNETIC STRUCTURE OF ORGANICCONDUCTOR β'-ET2ICl2 BY USING NEUTRONS
Yukio Noda,a Masashi Watanabe,a Atsushi Matsunaga,a Satoshi Komiyama,a HiromiTaniguchi,bAtshushi Kawamotoc and Yoshiya UwatokodaInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, Sendai, Japan; b

Faculty of Science, Saitama University, Saitama, Japan; c Graduate School of Science, Hokkaido
University, Sapporo, Japan; d The Institute of Solid State Physics, The University of Tokyo, Kashiwa,
Japan

The organic conductor β'-ET2ICl2 (here ET stands for bis(ethylenedithio)tetrathiafulvalenecoherent) transforms to a magnetically ordered phase at about 22K, presumably due tothe antiferromagnetic spin ordering of π-electrons in an organic ET molecule. The
characteristics of electric conductivity is semiconducting. We have performed crystal andmagnetic structure analyses of β'-ET2ICl2 by using neutrons to reveal the magnetic structure.
Special interest is the distribution of magnetic moment, which directly reflects the distributionof π-electrons.
A four-circle diffractometer named FONDER installed at T22 beam port of Japan
Atomic Energy Agency reactor JRR3M was used. Wavelength was 1.24A and maximum 2θ
angle was 115degree. For the magnetic scattering, we also used 2.40A neutrons. We have used
several samples whose crystal sizes were about 1.2 x 1.6 x 10.1 mm3 for dutarated one and 2 x
3 x 5 mm3 for hydrogen sample. Data were taken at 12K. For the comparison, we also
performed x-ray crystal structure analyses using Mo kα1 x-rays at 12K and maximum 2θ
angle was 72degree. Crystal structure data are followings; T=12K, C20D16S16ICl2 , P-1,
a=12.777(2), b=9.555(1), c=6.584(1), α=97.53(1), β=101.35(1), γ=87.09(1), Z=2, R(F)=0.033
for x-ray, R(F)=0.020 for neutron. Hydrogen sample gave almost the same results.
We found relatively strong new reflections at (0.5 0.5 0), (0.5 -0.5 0) and very weakones at (0.5 1.5 0), (-0.5 1.5 0), (1.5 0.5 0) and (-1.5 0.5 0) at 7.6K. The intensity shows anorder parameter behavior and vanishes at TN=23K. There were no peaks at (0.5 0 0) and (00.5 0). From the information of the above extinction rule, we can conclude the antiferomagnetic spin order pattern. The result is antiparallel order along [100] and [010] direction andparallel order along [110] direction. Because we performed crystal structure analysis under
the same configuration and the same crystal, we had the scale factor. Thus the magnetic
structure factors are taken as absolute numbers. We performed Fourier transformation to obtain the magnetic moment and π-electron distribution. The size is 10.3A along [1 -1 0] and12.9A along [1 1 0], and this size of distribution is almost comparable with the unit cell size.
We believe that the imaging of π-electron in an organic conductor might be the first case.

O3B06-M6

LATTICE DISTORTION AND FERROMAGNETISM IN BaRuO3
Chao-hung Du,a*K. J. Tseng,a Y. Y. Lo, a Mau-Tsu Tang baDepartment of Physics, TamkangbNational Synchrotron Radiation Research Center, Hsinchu 300, Taiwan.

*

E-mail: chd@mail.tku.edu.tw

University, Tamsui 251, Taiwan.

Studies of perovskites have stimulated research into a wide variety of unusual transition
metal oxides, since the discovery of high TC superconductors and CMR materials. It has been
demonstrated that the interplay between the different degrees of freedom in perovskites canresult in a very reach phase diagram, including the unusual conductivity and magnetism,charge/spin stripes, or even the phase separation phenomenon. The recently discovered
layered ruthenate compounds have also been the subject of considerable study, especially forthe discovery of superconductivity in Sr2RuO4. However, the mechanism thesuperconductivity in strontium ruthenates is still not clear, for example, the correlation
between the dimensionality and the local moment. BaRuO3 is chemically related to SrRuO3,
but displays different crystallographic forms. Therefore, it can be the model for understanding
these issues. BaRuO3 has been reported to show the unusual electrical and magnetic
properties, and the pseudogap and charge-density waves (CDWs) were suggested to be thecauses. The pseudogap has been observed using optical spectra, but the existence of CDWs
was questioned because of lack of the experimental evidence. Using the x-ray in-vacuum
camera on a high quality single crystal BaRuO3, we located some weak spots at T= 30 K
along the c*-axis which doubles the c*-axis of the unit cell. Further study using x-ray
scattering, by measuring the peak profiles as a function of temperature, we observed that the
CDW satellite reflections display a step-like transition at T≈ 80 and 50 K where the former iscorrespond to the formation of CDW, and the later could be caused by the lattice distortion
which is related to a weak ferromagnetic transition as confirmed from susceptibility
measurement.

O3C06-M1

THE AUSTRALIAN SYNCHROTRON
Julian Adams
Principal Beamline Scientist
Protein Crystallography
Australian Synchrotron

The Australian Synchrotron is a new 3rd generation synchrotron source. The initialfunding covered the construction of the machine and nine beamlines.
Details of the construction, commissioning, user operations of the beamlines will bepresented.

O3C06-M2

AUTOMATION AT SER-CAT: TOWARDS SIGNAL BASED DATACOLLECTIONJohn P. Rose1,2, John Chrzas1,2, James Fait1,2, Zeng-Qing Albert Fu1,2, Andrew Howard2,3,John Gonczy1,2, Zhongmin Jin1,2 and B. C. Wang1,21Dept. of Biochemistry and Molecular Biology, The University of Georgia, Athens, GA, USA,

2

SER-CAT, Advanced Photon Source, Argonne National Laboratory, USA. Biological, Chemical, and3

Physical Sciences Department, Illinois Institute of Technology, Chicago, IL, USA

With the highly optimized X-ray flux and beam quality now available at 3rd generationsynchrotron sources, future improvements in overall throughput must now be directed to
improving the flow and logistics of conducting crystallographic experiments and dataacquisition themselves.
At SER-CAT, beamline setup, sample handling, sample alignment, data collection
strategy, data collection, data reduction, structure solution and data archive have all been
automated or are in the process of being automated.
Building on these technologies a newdata collection paradigm we term Signal Based Data Collection (SBDC) is being developed
aimed at increasing the success rate of structure determination and overall beamline efficiency.
The SBDC approach monitors the anomalous scattering signal present in the data (SAS or
MAD), as it is being collected, to ensure that an interpretable electron map (i.e. the structure)
can be produced. This approach differs from traditional data collection in that there is direct
feedback from the data reduction and structure determination process to the data collection
process.
The project is a partnership between structural biologists at the University of Georgia
and the excellent technical staff at SER-CAT; it builds on the methodology and technology
developed at both institutions over the past seven years, which if successful, could in a very
real sense change the way that synchrotron X-ray diffraction data is collected, increase theproductivity and cost-effectiveness of beamline operation, resulting in more and better science
being produced.
Details of the implementation of various aspects of the SBDC approach will bepresented.
Work is supported in part with funds from SER-CAT, the Georgia Research Alliance,
the National Institutes of Health (GM62407) and the University of Georgia Research
Foundation.

O3C06-M3

100-PS TIME-RESOLVED X-RAY EXPERIMENTS WITH DAILYSINGLE BUNCH MODE: CURRENT STATUS OF BEAM LINE NW14A
AT THE PHOTON FACTORY ADVANCED RING
Shin-ichi Adachi1,2, Shunsuke Nozawa2, Ryoko Tazaki2, Tokushi Sato3, Ayana Tomita3,
Matthieu Chollet3, Laurent Guérin1, Kouhei Ichiyanagi1, Hirohiko Ichikawa2, Masahiro
Daimon2, Hiroshi Sawa1, Hiroshi Kawata1, and Shin-ya Koshihara2,3
1

Photon Factory, KEK, Japan
Non-equilibrium Dynamics Project, ERATO, JST, Japan
3
Frontier Collaborative Research Center & Department of Materials Science, Tokyo Institute ofTechnology, Japan
2

Time-resolved X-ray experiments using synchrotron radiation sources are becoming
general and powerful tools to explore structural dynamics of condensed matters in materials
and biological science. NW14A is a newly constructed undulator beam line for 100-pstime-resolved X-ray experiments at the Photon Factory Advanced Ring, KEK [1]. This beamline was designed to conduct a wide variety of time-resolved X-ray measurements, such as
time-resolved diffraction, scattering and X-ray absorption fine structure. Its versatility isallowed by various instruments, including two undulators, three diffractometers, two pulse
laser systems and an X-ray chopper. The current status of the beam line will be presented.
Reference:[1] Nozawa et al. (2007) J. Synchrotron Rad. 14, 313-319.

O3C06-M4

DEVELOPMENT AND APPLICATION OF THE “PINPOINT
STRUCTURE MEASUREMENT SYSTEM”
SUB-MICRON BEAM AND TIME-RESOLVED MEASUREMENT AT SPring-8’s
BL40XU
Shigeru Kimuraa,f, Nobuhiro Yasudaa,f, Yoshimitsu Fukuyamaa,f, Jungeun Kima,f, Yoshihito
Tanakab,f, Koshiro Toriumic,f, Yutaka Moritomod,f, Yoshihiro Kuroiwae,f, Kenichi Katoa,b,f and
Masaki Takataa,b,fac

JASRI/SPring-8, Hyogo 679-5198, Japan; bRIKEN SPring-8 Center, Hyogo 679-5198, Japan;

University of Hyogo; ｄTsukuba University; eHiroshima University;fCREST-JST, Saitama 332-0012,

Japan

The “X-ray Pinpoint Structure Measurement” project is a part of the CREST projects(2004-2008) funded by the Japan Science and Technology Agency (JST). It is our key project
to promote the research utilization for the chemical reactions of nanomaterials and the
behavior of nano-devices in operation at SPring-8. The project’s architecture, basic design,and overall strategy were previously reported with the technical achievement status at the
AsCA06 conference. In the report, we acknowledged the importance and difficulty ofcoincidentally measuring the timing and area of a structure, simultaneously with the challengeof measuring the physical and/or chemical properties in reaction, such as optical reflectivity,
absorption, electric conductivity, dielectric property and etc. In addition, of particularimportance is gaining a higher S/N ratio of measured data. In our presentation, we will report
the progress in the application of the time-resolved diffraction experiments and its upgradingby combining with the sub-micron diffraction technique.
For photo-irradiation experiments, it has proved difficult to accurately measure thesignal from the photo-induced phase due to the quite few volume ratio of pump laser
penetration region compared to the entire crystallite. The sub-micron single crystal structure
analysis technique, performed by applying high brilliance, focused X-ray microbeam, will
overcome this limitation because the penetration depth of laser light is typically at the
micrometer order. With the 100% volume penetration of the laser light, we can eliminate
ambiguity over the volume ratio in photo-induced reaction. This technique also provides abreakthrough by enabling single crystal structure analysis from a single grain of powder
sample.
To date, we have achieved sub-micron single crystal structure analysis with a focused
X-ray microbeam and time resolved “pump and probe” experiment with 40 ps time resolution.
In our presentation, we will review the present status of the project with results of the flagshipresearch subject, the “time resolved structure analysis of crystal-amorphous phase change in
DVD optical memory material”.

O4A06-A1

ALANINE RACEMASE AS A TEMPLATE FOR DRUG DISCOVERY IN
TUBERCULOSIS
Kurt Krause a, Mike Benedikb, James Briggsc, Milya Davlieva c, Harold Kohn d, Joe Longtinc,
Daniel Milligan a, Ulrich Strych caDepartment of Biochemistry, University of Otago, bDepartment of Biology and Biochemistry,

University of Houston, cDepartment of Biology, Texas A&M University, dSchool of Pharmacy,
University of North Carolina

Tuberculosis is the leading cause of death from infectious diseases worldwide, yet few
new agents have been developed to treat it over the past two decades. As a result, academic
laboratories around the world are working to accelerate anti-tuberculosis drug development.
We present progress from an academic based structure-aided drug design program that is
focused on the design of inhibitors of alanine racemase in M. tuberculosis, Because of thebroad importance of alanine racemase as a prokaryotic drug target, its inhibitors would prove
useful in the development of antibiotics for tuberculosis, including MDR strains, as well asother for the treatment of other pathogenic bacteria.
We will present results from recent work relating to proving the essential nature ofalanine racemase in mycobacteria. We will also present data on three alanine racemase
crystal structure determinations and analyze them in terms of pharmacophore development.
We will review the creation of pharmacophore models that incorporate the results ofmolecular dynamics simulations. These pharmacophore models have been used to survey, insilico, chemical databases for racemase inhibitors. In our medicinal chemistry effort, thestructure of cycloserine and its analogs have been used as a starting platform forstructure-aided design efforts. In our drug design project we encountered first-hand the
difficulties of designing inhibitors for enzymes with restricted entryways into the active sites.
Possible ways to overcome this problem will be presented.

O4A06-A2

STRUCTURES OF ALL FOUR PHOSPHODIESTERASE-4
SUBFAMILIES PROVIDE INSIGHT INTO SUBFAMILY INHIBITOR
SELECTIVITY
Jiwen Cai1, Huanchen Wang2, Ming-Sheng Peng1, Yi Chen1, Jie Geng2, Howard Robinson3,
Miles Houslay4 & Hengming Ke2
1

Structural Biology Centre, School of Pharmaceutical Sciences, Sun Yat-Sen University, Guangzhou,

510080, China
2

Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, The

University of North Carolina, Chapel Hill, NC 27599-7260, USA.
3

Biology Department, Brookhaven National Laboratory, Upton, NY 11973-5000, USA.

4

Molecular Pharmacology Group, Wolfson Building, Division of Biochemistry and Molecular Biology,

Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, UK.

Phosphodiesterase-4 (PDE4) selective inhibitors have attracted much attention as
potential therapeutics for treatment of both depression and major inflammatory diseases, but
their practical application has been compromised by side effects. A possible cause for the side
effects is similar inhibition of current inhibitors to all PDE4 subfamilies. The development of
PDE4 subfamily-selective inhibitors has been hampered by lack of structure information.
Here we rectify this by providing the crystal structures of the catalytic domains of PDE4A,
PDE4B and PDE4D in complex with the PDE4D-selective inhibitor NVP as well as theunliganded PDE4C structure. NVP binds in the same conformation to the deep substrate
pocket and interacts with the same residues. However, detailed structural comparison reveals
significant conformation differences. While the active sites of PDE4B and PDE4D are mostly
comparable, PDE4A shows significant displacements of the residues next to the invariant
glutamine that is critical for substrate and inhibitor binding. PDE4C appears to be more distalfrom other PDE4 subfamilies with certain key residues being disordered. Our analyses
provide novel mechanistic insight into the feasibility of developing PDE4 subfamily-selective
inhibitors.
* Jiwen Cai’s current affiliation is Oxford Diffraction (Hong Kong) Ltd. Rm 1303, 13/F, Kwai
Hung Holdings Centre, 89 King’s Rd. North Point, Hong Kong.

O4A06-A3

STRUCTURAL BASIS FOR RECRUITMENT OF TANDEM HOTDOGDOMAINS IN ACYL-COA THIOESTERASE 7 AND ITS ROLE IN
INFLAMMATION
Jade K. Forwood, Anil S. Thakur, Gregor Guncar, Mary Marfori, Dmitri Mouradov, Stuart
Kellie, David A. Hume, Thomas Huber, Jennifer L. Martin, Bostjan Kobe
School of Molecular and Microbial Sciences and Institute for Molecular Bioscience, University of
Queensland, Brisbane, Australia.

As part of our program on high-throughput crystallography of macrophage proteins, wehave carried out a comprehensive structural and functional characterisation of mouseacyl-CoA thioesterase 7 (Acot7). Acots catalyse the hydrolysis of fatty acyl-CoA to free fatty
acid and coenzyme A and thereby regulate lipid metabolism and cellular signalling. Whileprokaryotic homologues possess a single thioesterase domain, mammalian Acot7 contains apair of domains in tandem. We determined the crystal structures of both the N- andC-terminal domains (1.8 and 2.5 Å resolution, respectively) of the mouse enzyme, and thestructure of the full-length enzyme using a combination of chemical crosslinking, mass
spectrometry, and molecular modelling. The novel quaternary arrangement features a trimerof hotdog fold dimers. We show that both domains of Acot7 are required for activity, that
only one of two possible active sites in the dimer is functional, and identify Asn24 andAsp213 (from N- and C-domains, respectively) as the catalytic residues through site-directedmutagenesis. We also designed an enzyme with higher activity than wild-type Acot7 by
mutating the residues in the non-functional active site. Because Acot7 shows the highest
activity towards arachidonoyl-CoA (a precursor of eicosanoids), is highly expressed inmacrophages and upregulated by pro-inflammatory factors, and its over-expression in
macrophages alters the production of prostaglandins D2 and E2, we propose a role in
inflammatory processes. Together, our results provide a foundation to relate the molecularand cellular functions of Acot7 in macrophages and other mammalian tissues.
Forwood JK, Thakur AS, Guncar G, Marfori M, Mouradov D, Meng W, Robinson J,
Huber T, Kellie S, Martin JL, Hume DA and Kobe B (2007). Structural basis for recruitmentof tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation. Proc Natl
Acad Sci USA 104: 10382-10387

O4A06-A4

THROUGH-PUT PROTEIN STRUCTURE DETERMINATION AND
RATIONAL STRUCTURE-BASED DRUG DESIGN USINGFRAGMENT-BASED APPROACH
Tej P. Singh, Sanjit Kumar, Pradeep Sharma, Rafia Mir, Ishfaq A. Sheikh, Amit K. Singh, R.
Prem Kumar, Mau Sinha, Nagendra Singh, Punit Kaur, A. Srinivasan and S. Sharma
Department of Biophysics, All India Institute of Medical Sciences,

New Delhi-110 029, India(tps_aiims@hotmail.com)

Discovering and developing new medicines is a long and expensive process. Any newcompound must not only produce the desired response with minimal side effects but also bedemonstrably better than existing therapies. The conventional methods are slow, expensive
and full of uncertainties. The conceptual breakthrough that a drug may have a specific target
at the macromolecular level has benefited the drug development process profoundly. The
recent phase in drug design has utilized the knowledge of the three-dimensional structures of
the target molecules. In order to develop potent anti-inflammatory agents, we have used threepotential macromolecular targets of the inflammatory pathway. Phospholipase A2 (PLA2),
cyclooxygenase (COX-1 and COX-2) and lipoxygenase (LOX) are the three main enzymes
that catalyze the cascade which produces pro-inflammatory compounds. From theexperimental observations at the atomic level of how inhibitors bind to these targets, specificinteractions that are important in molecular recognition were inferred. We have determinedthe crystal structures of several isoforms of native enzymes, their complexes with substrateanalogues, natural ligands, known anti-inflammatory agents and designed compounds. In
order to obtain potent drugs by keeping in mind the Lipinsky’s rule of five, we have designed
more than one ligand (fragments) to saturate the binding sites of these targets. The
structures of ternary complexes with two different ligands occupying the non-overlappingsites in the substrate binding domain have shown that the potential of fragment-based design
is enormous. Since every tight inhibitor due to its size may not be a drug, the combination ofsmaller fragments should be a better choice.

O4A06-A5

D- STRUCTURAL BASIS FOR GLUTAMATE RACEMASE INHIBITION
Kook-Han Kima, Young-Jong Bonga, Joon Kyu Parka, Key-Jung Shina, Kwang Yeon Hwangb
and Eunice EunKyeong KimaaLife Sciences Division, Korea Institute of Science and Technology, 39-1 Hawolkok-dong, Sungbuk-gu,

Seoul 136-791, Korea; b, College of Life Sciences and Biotechnology, Korea University, Seoul, Korea

Glutamic acid is a required biosynthetic building block for peptidoglycan, and the
enzyme glutamate racemase(GluR) catalyzes the inter-conversion of D- and L-glutamate
enantiomers. Therefore, GluR is considered as an attractive target for the design of new
antibacterial drugs. Here we report the crystal structures of GluR from Streptococcus
pyogenes in both inhibitor free and inhibitor bound forms. The inhibitor free GluR
crystallized in two different forms and they diffracted to 2.25 Å and 2.5 Å resolution, while
the inhibitor bound crystal diffracted to 2.5 Å resolution. GluR is composed of two domainsof α/β protein that are related by pseudo-2-fold symmetry and the active site is located at thedomain interface. The inhibitor, γ-2-naphthylmethyl-D-glutamate, which was reported
earlier as a novel potent competitive inhibitor, makes several hydrogen bonds with protein
atoms, and the naphthyl moiety is located in the hydrophobic pocket. The inhibitor binding
induces a disorder in one of the loops near the active site. In both crystal forms GluR exists
as a dimer and the interactions seen at the dimer interface are almost identical. This agrees
well with the results from gel filtration and dynamic light scattering.

O4A06-A6

CRYSTAL STRUCTURE OF ABT-737 IN COMPLEX WITH Bcl-xLPeter E. Czabotar1, Erinna F. Lee1, Brian J. Smith1, Kurt Deshayes2, Kerry Zobel2, W.
Douglas Fairlie1, Peter M. Colman1
1

The Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia; 2Genentech Inc, San

Francisco, USA

ABT-737 is a recently described compound that has commanded interest as a potential
cancer therapeutic. Discovered by Abbott laboratories, it targets pro-survival members of the
Bcl-2 family of proteins, specifically Bcl-xL, Bcl-w and Bcl-2, but does not bind to Mcl-1.
These proteins inhibit programmed cell death and are over expressed in many cancer cells
thus making them refractory to established cancer therapeutics. Inhibition of these proteins by
ABT-737, or a similarly acting compound, is seen as a promising strategy for enhanced killingof cancer cells.
We have solved the crystal structure of ABT-737 in complex with Bcl-xL. Although anumber of NMR-derived structures have been described, this is the first reported x-ray
structure for any Bcl-2 family member in complex with an organic ligand. The structure
demonstrates that ABT-737 targets a hydrophobic groove on the surface of Bcl-xL. The
biological ligands for this groove are the BH3 domains of the pro-apoptotic members of the
Bcl-2 family, for example Bim. We have performed saturation mutagenesis on the residues of
Bim that are mimicked by ABT-737. In conjunction with our structure these data provide
important insights into the design of BH3 mimetics with selective binding profiles for the
Bcl-2 family of proteins.

O4B06-A1

MOLECULAR BRICKS, PENS, GRIDS AND SPHEROIDS FROMDIHETEROAROMATIC HOSTS
Roger Bishop, Solhe F. Alshahateet, Jason Ashmore, Donald C. Craig and Marcia L. Scudder
School of Chemistry, The University of New South Wales, Sydney, Australia.

Halogenated diheteroaromatic molecules are V-shaped compounds designed to behave
as lattice inclusion hosts that lack the ability to use strong hydrogen bonding in their crystal
structures [1]. Consequently, their host-guest self-assembly employs a wide variety of weaker
intermolecular interactions. This presentation describes the varied methods by which
endo-endo facial interactions can occur between groups of such host molecules in their crystal
structures.
Novel molecular brick, pen, grid and spheroid structures are obtained. The X-ray crystal
structures of these building blocks will be compared and contrasted in crystal engineeringterms.

Reference:[1] R. Bishop, Crystal Engineering of Halogenated Heteroaromatic Clathrate Systems,
Chapter 5, pages 91-116, Frontiers in Crystal Engineering, Editors: E.R.T. Tiekink and
J.J. Vittal, J. Wiley & Sons (Chichester), 2006.

O4B06-A2

ROLE OF MIXED HALOGENS (F, Br) TOWARDS CRYSTALPACKING AND INTERMOLECULAR INTERACTIONS IN
SUBSTITUTED BENZANILIDES
Susanta K. Nayak, T. N. Guru Row*.
Solid State and Structural Chemistry Unit, Indian Institute of Science,
Bangalore-560012. India.

Crystal structures of differently substituted benzanilides (Fluoro and bromo derivatives)
have been analysed to evaluate the influence of halogen bonding, appearance of weakintermolecular interactions and hydrogen bonding on the features of crystal packing. Five
compounds(Scheme-1)
namely4-fluoro-N-(2-bromophenyl)
benzamide,
2-fluoro-N-(2-bromophenyl)
benzamide,
3-fluoro-N-(2-bromophenyl)
benzamide,
3-fluoro-N-(4-bromophenyl) benzamide and 4-fluoro-N-(4-bromophenyl) benzamide havebeen studied by single crystal x-ray diffraction and the intra- and inter-molecular interactions
have been analyzed for halogen bonding features.
Br

H

H

N

N

F

F

O

a

O
Br

b

Scheme-1
These studies clearly point out that if an intra-molecular H bond is involved with thecarbonyl moiety, the possibility of halogen…oxygen bonding is remote. This implies that theorientation and presence of lone pairs on the oxygen atom is a prerequisite for halogen
bonding. Even though several halogen…halogen contacts have been observed in thesestructures all such contacts except one contact [Br…F], are with disordered positions of
halogens. Thus a systematic study of mixed halogen (Br and F) substituted benzanilides
brings out the fact that the propensity of formation of halogen…halogen bonding is sparse inthese molecules.

O4B06-A3

SYNTHESIS, STRUCTURES AND MAGNETIC PROPERTIES OF A
SERIES OF CYANO-BRIDGED HETEROMETALLIC COMPLEXES
Shao-Jun Wang, Long Jiang, Wei-Xiong Zhang and Tong-Bu Lu
MOE Key Laboratory of Bioinorganic and Synthetic Chemistry / State Key Laboratory of
Optoelectronic Materials and Technologies / School of Chemistry and Chemical Engineering, Sun
Yat-Sen University, Guangzhou 510275, China

Cyano-bridged clusters and coordination polymers have been extensively investigatedin the field of molecular magnetism since cyano-bridge can be efficient propagation formagnetic coupling. In this report, we will present a series of cyano-bridged heterometallic
chains with different structures and magnetic properties.

O4B06-A4

FUNCTIONAL POROSITY IN SELF-ASSEMBLED MOLECULAR
FRAMEWORK
Mohamed Makha, Colin Raston
Discipline of Chemistry, School of Biomedical, Biomolecular &Chemical Sciences; The University ofWestern Australia.

Amphiphilic p-sulfonato-calix[4]arene is a renowned supramolecular tecton serving asa platform in the construction of inorganic/organic clay mimics.1 Layered materials thatmimic the structure and properties of naturally occurring clays are of interest insupramolecular chemistry and crystal engineering.2 The paper will present recent work on theuse of macrocylic calixarenes sulfonates as molecular building block in molecular assemblies
featuring functionalised pores and channels of nano dimensions. The assembly process
involves crystal engineering and is governed by supramolecular weak forces, affording newmaterials such as ionic capsules, molecular solids with extended networks and micellar
aggregates. The majority of work in the area is focused on p-sulfoanto-calix[4]arene tecton
and more recently p-sulfonato-calix[5,6,8]arenes with higher degree of freedom can be
deployed to form ionic molecular solid with remarkable stability and regular porosity.
Previous work established ionic capsules and materials with 2D and 3D porosity constructedfrom organic ions, tetra-phenylphosphonium cations and polyanionic calixarne sulfonates.3
Helical structure using this self assembly approach are also accessible with potential
applications in chiral exchange resins, size exclusion chromatography and heterogeneous
catalysis.4

Reference:
1. K. T. Holman, A. M. Pivovar, J. A. Swift, M. D.Ward, Acc. Chem. Res. 2001, (34), 107;
2. G. R. Desiraju, Crystal Engineering: The Design of Organic Solids, A. M. Beatty, K. E. Granger, A. E.
Simpson, Chem. Eur. J. 2002, (8), 3256;
3. M. Makha, C. L. Raston, A. N. Sobolev, Chem. Commun., 2006, (5), 511-513;
4. C. B. Smith, L. J. Barbour, M. Makha, C. L. Raston, A. N. Sobolev. Chem. Commun., 2006, (9), 950-952.

O4B06-A5

WATER CLUSTERS, ISOSTRUCTURALITY AND POLYMORPHISM IN
HYDROXY DERIVATIVE OF HALOBENZENE CRYSTALSTRUCTURES
Binoy Krishna Saha
Department of Chemistry, Pondicherry University, Puducherry-605014, India

Water helices surrounding the nano-column of trichlorophloroglucinol andtribromophloroglucinol hosts have different handedness, PMPMPM and PPPMMM (P =right-handed and M = left-handed) depending upon the halogen⋅⋅⋅halogen interactions.
Trichlorophloroglucinol host lattice shows zeolite like behavior.
A T6(2) tape of hydrogen bonded water molecules in boat cyclohexane conformation istrapped in the channel structure of the dibromophloroglucinol host; water escapes at 40-90 °C
to transform to the anhydrous form but is readily reabsorbed from air to regain the hydrated
structure.
Triiodophloroglucinol,
triiodoresorcinol,
triiodophenol,
triiodobenzene,
tribromobenzene and trichlorobenzene are isostructural. Triiodophloroglucinol andtriiodoresorcinol are dimorphic and their second forms are also themselves isostructural. Solidsolutions are formed between isostructural compounds.

O4B06-A6

SUPRAMOLECULAR ASSEMBLIES OF MONONUCLEAR AND
POLYMERIC COBALT(II) AND NI(II) DICARBOXYLIC COMPLEXES
Tanwawan Duangthongyou,a Sutatip Siripaisarnpipat a, Chris Adams ba

Department of Chemistry, Faculty of Science, Kasetsart University, Bangkok Thailand; b The Schoolof Chemistry, University of Bristol, Bristol BS8 1TS, UK

Self – assembly based on metal ligand coordination bonds, π-π stacking interactions andhydrogen bonds provide an efficient route to supramolecular architectures with specifictopologies. Dicarboxylic acid ligands are excellent spacers to constitute 1D, 2D and 3D
structures. The structural framework of NiII and CoII metal center, involving dicarboxylic
acids of varying chain length and N-donor ligands have been studied to understand theconformational flexibility of dicarboxylic acids, and the various modes of network that can becreated by manipulating the N–donor ligand, for example in the figure below.

View of crystal structure of [Ni(H2O)4(2,2’-bipyridine)](C6H8O4)(H2O). The
hydrogen atoms and the sovent molecules (water) have been omitted.

O4B06-A7

ENGINEERING OF LUMINESCENT PROPERTIES IN MIXEDLANTHANIDE CARBOXYLATE COORDINATION POLYMERSYuFong Yen, Samadara Thushari, Alvin Siu, Kam-Sing Wong and Ian D. Williamsa) Department of Chemistry, Western Connecticut State University, Danbury CT, U.S.A.
b) Department of Chemistry and Physics, Hong Kong University of Science and Technology, Clear
Water Bay, Kowloon, Hong Kong, China.

The engineering of luminescence as a function of composition and structure has been
carried out for several families of crystalline lanthanide coordination polymers.
Luminescence for the 1D chain polymer [Ln2(2,2-biphenate)3(H2O)2] and 3D network
polymer [Ln(trimesate)] prepared from hydrothermal synthesis is strong for Tb and Eu
homopolymers, weak for Sm and Dy, whilst Gd is non-emissive as a metal center. When the
50:50 mixed metal polymers were prepared and tested some striking results were found.
Both Gd and Tb act as sensitizers and enhance the luminescence of Eu, Sm and Dy.
Efficient energy transfer appears to be possible between metal centers in these polymers,
since typically only emission from one metal is observed. Other families such as[Ln2(L-TAR)3(H2O)2] have different properties for the mixed-lanthanide polymers, forexample both Tb and Eu emissions are clearly seen together in the Tb-Eu compound. This
polymer has a carboxylate bridge, but no bridging O atom commonly shared. The structuralfeatures affecting the emissive behaviour and energy transfer process will be summarized.
The Research Grants Council (HKSAR) is thanked for financial support of this work
(603306).

O4C06-A1

QUENCHED DISORDER EFFECTS IN TOPOLOGICALLY ORDERED
NANOPORES ON THE SMECTIC PHASE TRANSITION OF 8CB
R. Guegan,a,b D. Morineau,a R. Lefort,a A. Moreac,a and M. GuendouzcaGroupe Matière Condensée et Matériaux, Université de Rennes 1, Rennes, France, bInstitute ofIndustrial Science, University of Tokyo, Meguro-ku, Tokyo, Japan, cLaboratoire d’Optronique, ENSSAT,
Université de Rennes 1, Lannion, France

The advancement of nanotechnologies in an increasing number of fields –including
microfluidics, biotechnology, nanoelectronics, supports the growing interest of the scientificcommunity in the understanding of the peculiar properties of systems of nanometer scaledimensions. A subject of current matter concerns the effects of confinement of molecularphases in mesoporous materials. The question of the phase behavior of fluids in restricted
geometries is especially rich, leading to the occurrence of new phases or modifying the natureof the transition (order or critical scaling). Liquid crystals have been commonly used as model
systems in statistical mechanics and soft matter physics. Experiments on phase transitions inliquid crystals have provided many of the most detailed tests of the modern theories of criticalphenomena., Several studies have recently shown the effects of the quenched disorder
imposed by random porous media on the continuous smectic transition. Isotropic porous
aerogels and aerosil dispersions are the two prototype systems that induce such conditions
experimentally [1, 2].
In this contribution, we have introduced porous silicon (PS) as a way to control someconditions of confinement that provide an unique opportunity to check the effect or quencheddisorder in strongly anisotropic geometry.. PS displays a well-defined geometry with apreferential alignment (1D) of nanochannels (diameter: 100-200 Å, length: 30 m). The
confinement of 4-n-octyl-4-cyanobiphenyl (8CB) liquid crystal in PS shows interesting novel
features related to a striking behavior of the Nematic-Smectic A transition. Various
experimental techniques (neutron scattering, micro-Raman spectroscopy and spectroscopic
ellipsometry), demonstrated a preferential alignment of the molecules into the channels andthe destruction of the quasi-long range order of the Smectic A phase. The transition is
replaced by a progressive short range ordering on an extended temperature range (60K below
Tc). This result has been successfully interpreted in the theoretical context of random fields,
according to the strongly disordering nature of the inner pore surface of PS [3].
Reference:[1] T. Bellini, L. Radzihovsky, J. Toner, N. A. Clark, Science, 294 1074-1079 (2001)[2] R.L. Leheny, et al, Phys Rev E, 011708-1-13 (2003)[3] R. Guégan, D. Morineau, C. Loverdo, W. Béziel, M. Guendouz, Phys. Rev. E, 73, 011707 (2006).

O4C06-A2

AN ELECTRON DIFFRACTION METHOD FOR DETERMINING THE
CHIRALITY OF CARBON NANOTUBES
Lu-Chang Qin,a Hakan Deniz,a Jie Tang baW.M. Keck Laboratory for Atomic Imaging and Manipulation, Department of Physics and Astronomy,

University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3255, USAb

National Institute for Materials Science, Tsukuba, Ibaraki 305-0047, Japan

Email: lcqin@physics.unc.edu

The knowledge of the chirality of a carbon nanotube (defined by the chirial indices (n,m)
that specify the perimeter of the nanotube) is crucial for the understanding, predictions, andinvestigations of the structure-property relationships of the nanotube and it has been achallenging task to obtain the chirality (diameter and helicity) of carbon nanotubes, inparticular multiwalled carbon nanotubes, where the chiral indices of each and every shell are
required for a complete determination of the chirality of the nanotube.
Electron diffraction from a carbon nanotube of chiral indices (n,m) can be expressed
analytically in closed form [1]. The chiral indices (n,m) of a single-shell carbon nanotube canbe measured directly from the scattering intensities Il1 , Il2, and Il3 on the principal layer lines
l1, l2, and l3 formed by the primary graphene reflections [2-3]. An alternative relationshiprelating the chiral indices (n,m) and the principal layer line spacings D1 and D2,, is also most useful for the determination of the chirality ofcarbon nanotubes [4-6].
These relationships have enabled us to establish a systematic procedure to obtain thechiral indices of carbon nanotubes unambiguously with a high accuracy. Examples ofapplication of this method to the determination of the chirality of single-walled,doubule-walled, few-walled, and multiwalled carbon nanotubes will also be presented.
Reference:[1] L.-C. Qin, J. Mater. Res. 9, 2450 (1994).
[2] L.-C. Qin, Chem. Phys. Lett. 297, 23 (1998).
[3] Z. Liu and L.-C. Qin, Chem. Phys. Lett. 408, 75 (2005).
[4] Z. Liu, Q. Zhang, and L.-C. Qin, Appl. Phys. Lett. 86, 191903 (2005).
[5] L.-C. Qin, Rep. Prog. Phys. 69, 2761 (2006).
[6] L.-C. Qin, Phys. Chem. Chem. Phys. 9, 31 (2007).

O4C06-A3

RHEED SURFACE POLE FIGURE -- A NEW IN-SITU TECHNIQUE
FOR POLYCRYSTALLINE
AND NANOSTRUCTURED SURFACE TEXTURE ANALYSISFu Tang, Toh-Ming Lu and Gwo-Ching Wang
Dept. of Physics, Rensselaer Polytechnic Institute, 110 8th Street, Troy, New York 12180-3590

The preferred crystalline orientation, or texture, is a fundamental property ofpolycrystalline film and it directly controls many important physical properties such as optical,
magnetic, mechanical, and electrical properties of the films. Texture formation is a very
complex phenomenon. To date, the fundamental understanding of the atomistic mechanisms
on the texture evolution still remains as a challenging subject. We demonstrated that it ispossible to construct a reflection high-energy electron diffraction (RHEED) pole figure of apolycrystalline film by recording multiple RHEED patterns as we rotate the substrate aroundthe surface normal. Since electrons have limited penetration depth (nm range), the pole figure
constructed is a surface pole figure. It is in contrast with the conventional x-ray pole figure
which gives an average texture information of the entire film and substrate. Examples of insitu study of biaxial texture evolution of unusual Mg nanoblades grown by oblique angle
vapor deposition using this RHEED surface pole figure technique will be given. Figures 1(a)and 1(b) show SEM images viewed 90o from incident flux direction and facing the incident
flux direction, respectively. The figure 2 below shows the development of normalized (10 1 1)
RHEED pole figures at Mg deposition times (a) 0.5 min (~22 nm thick), (b) 8.5 min (~365
nm thick), (c) 24.5 min (~1.05 μm thick ) and (d) 34.7 min (~1.49 μm thick). The
positions of poles in the figures move towards the incident vapor flux as the film grows. The
center of circle is the geometrical position of the [0001] axis. We will show that very richinformation on the texture evolution can be obtained quantitatively from this pole figure
analysis.

O4C06-A4

QUANTUM OSCILLATIONS AND BEATS IN X-RAY REFLECTION
DURING FILM GROWTH
Y.-R. Lee,1,2,3 A. Gray,1,2 J. Tischler,4 P. Czoschke,5 H. Hong,1 S.-L. Chang,3 and T.-C.
Chiang1,2*
1

Department of Physics, University of Illinois at Urbana-Champaign, 1110 West Green Street,
Urbana, Illinois 61801-3080, USA

2

Frederick Seitz Materials Research Laboratory, University of Illinois at Urbana-Champaign, 104
South Goodwin Avenue, Urbana, Illinois, 61801-2902, USA

3

National Tsing Hua University, 101, Section 2, Kuang Fu Road, Hsinchu, Taiwan 30013, Republic of
China

4

Division of Materials Science and Technology, Oak Ridge National Laboratory, Oak Ridge,
Tennessee 37831, USA5

Seagate Technology, 7801 Computer Avenue South, Bloomington, MN 55435-5412

X-ray reflection from a growing film at an anti-Bragg position, where reflection
amplitudes from two adjacent atomic layers are out of phase and cancel each other, should
exhibit bilayer oscillations caused by interference. In an experiment of TiN growth by laser
ablation onto a sapphire substrate, an unexpected beating envelope function is found tomodulate the oscillations. The successive nodes and antinodes in the envelope function are
identified with the development of new growth domains separated by one atomic layer inthickness. This effect allows atomic layer counting of the film thickness distribution(roughness), and its observation implies that the growth is not characterized by a continuum
stochastic process, as usually assumed.

O4C06-A5

CHARACTERIZATION OF NANOMETER SCALE GRAIN SIZED Pt
ON Si AND PtSi/Si STRUCTURES DEPOSITED BY HIGH RATEMAGNETRON SPUTTERING
V.Uma1 and R.Chandramani2,Ramu2
1. Mount Carmel College, Bangalore. umaa12342001@yahoo.co.in
2.Department of Physics, Bangalore University, rchandramani@rediffmail.com,Bangalore,INDIA.

Thin film silicides become increasingly important with the progress of very large-scale
integrated (VLSI) and ULSI technology. Formation of low-resistance contact, low sheet
resistance diffused region, and interconnection line is crucial for the VLSI circuit performance.
Despite the potential applications of Pt and PtSi materials, the electronic and atomic structuresof platinum silicide (PtSi) films grown on Si surfaces have not been heavily studied. So an
attempt has been made to deposit metal with low substrate temperature in high vacuum athigh rates. Among the various methods in preparing metallic nano particles, the mostsuccessful method for refractory metals is the high rate magnetron R.F sputtering. Low
substrate temperature, high productivity, and high current densities are salient features of highrate sputtering deposition technique. Platinum with sheet resistance 3.40Ω was deposited on
Si using High rate Magnetron Sputtering system. The deposited film was heated to550oC in
the Nitrogen atmosphere to get platinum silicide (PtSi). Samples were subjected to XRD,
AFM and Spectroscopic Ellipsometry.
The XRD and AFM studies revealed the films Pt on Si are nano grain sized The XRD
pattern of the platinum shows the cubic (111) phase whereas PtSi is neither orthorhombic nor
monoclinic.
SampleRp in nmr.m.s roughness

Shape

Grain size
XRD

Grain size
AFM

Pt/Si

10.73

1.7954nm

Plate like surface

11.3nm11-12 nm

PtSi

6.398

1.235 nm

Pin hole free shape~55 nm50-60nmSpectroscopy ellipsometry analysis revealed that optical constants value Nano Pt on
Si shows little variation from the standard .The values have increased in PtSi samples due tothe annealing effects, decrease in roughness, less oxidation. The optical band gap orActivation energy was found to be 0.8eV and 1.4eV for Pt on Si and PtSi respectively.
Any device based on metal –Semiconductor contacts can either form an active
rectifying contact or an ohmic contact. I-V characteristics on Pt on Si confirm that thestructure exhibits Schottky-rectifying characteristics. The PtSi/Si structure exhibited theohmic behavior.
SampleKnee Voltage

Pt /Si

0.8V

PtSi/Si-

Reverse saturation current Barrier height

Ideality factor

0.04473μA

0.371342eV

2.277

0.74473nA

0.13eV

2.903

It can be concluded that contact characteristics are controlled by Fermi level pinning
due to the interface states.

O4C06-A6

SYNTHESIS, STUDIES AND LUMINESCENT PROPERTIES OFTERBIUM OXIDE DOPED LaMn0.9Zn0.1O3+d NANOPEROVSKITE BY
SOL-GEL METHODA A Alemi, E Karimpour Nahari and H Shokri
Department of Inorganic Chemistry, Faculty of Chemistry, University of Tabriz, Tabriz
Iran.

In this research we report the characterization of La1-xTbxMn0.9Zn0.1O3+d (LTMZ) (0.0≤x ≤0.32) nano particles with high surface area were synthesized by the polymerized complex(PC) method based on the Pechini-type reaction. High-quality nanopowders with controlled
stiochiometry and microstructure were prepared at temperature rang of 700-8000C for 6 h,with mean particle sizes of approximately 18.35 nm.
The synthesized materials were characterized by X-ray powder diffraction (XRD),
fourier transform infrared spectrum (FTIR) and Photoluminescence(PL). Photoluminescencemeasurements showed Tb3+ ions characteristic green emission in crystalline LTMZ powders
due to the 5D4 7FJ transitions of the 4f electrons of Tb3+ ions. The structure, homogeneityand particle size of the obtained compounds during different stages were investigated byscanning electron microscopy (SEM).
Key words: Lanthanum; Manganese; Terbium; Perovskite; Sol–gel; Luminescence.

O4C06-A7

STUDIES OF THE NANOSTRUCTURE OF NATURAL VEGETABLEFIBERS
Nguyen Van Tri
Institute of Engineering Physics, Hanoi University of Technology, Hanoi, Vietnam.

Vegetable fiber is a wonder of the nature, a most important and widespread naturalorganic polymer. An effective, modern and intelligential use of full advantage of this gigantic
and precious raw material source will only can be attained when the inside structure of thefiber and its relationship to specific fiber features are sufficiently known.
The chemical structure of the native cellulose, a basic component of the vegetable fiber,
as a linear β-1,4 - Glucose chain is well accepted newsdays. However, the physical structureof the vegetable fiber, i.e. the other key component and the bonding structure between thecellulose chains to create the wonderful fibred network of the supermolecular order is not yet
completely clear.
From our experiments with ESR, especially with the called "ESR Spectroscopy Tomography", in combination with some other methods (X-ray diffraction, SEM, SPM, ...) on
different genera of vegetable fibers (such as cotton, jute, pineapple, sisal, bamboo), we haveto the first time discovered that the inside structure of the vegetable fiber is constituted not
only by polysaccharide cellulose, but also by an another very important component consists offivefold [2Fe-2S] super-exchange metallo-organic combinations. These persist in the form of
the composite aperiodic Nanostructures linking diagonally the cellulose macromolecule
chains creating an elementary fiber.
A visible "macroscopic practical fiber" is constituted by a lot of the elementary fibers
spiraling together about an axis by a sloping angle Θo= 54.7°. This spiral angle is of a deep
significance on the statistic quantum electronic dynamics and the biophysical function of thefibers in the nature.
This fivefold metallo-organic composite Nanostructure plays a decisive role in thespecific features of vegetable fibers (such as the strength, the torsional module, theconductivity, the radiation response). On the basis of these achieved results, some physical andbiological treatment techniques to improve fiber properties have been elaborated and examined.
This research was supported by the National Research Program "New Materials", theNational Basic Research Program in Natural Sciences and the Textile Research Institute of the
Ministry for Industry.

O5A07-M1

CRYSTAL STRUCTURES OF THE COMPLEXES OF C-LOBE OF
LACTOFERRIN WITH NON-STEROIDAL ANTI-INFLAMMATORYDRUGS (NSAIDS) REVEAL THE BINDING PATTERN BETWEENC-LOBE AND NSAIDS WHICH SUGGESTS A NEW THERAPY FOR
MANAGEMENT OF NSAID-INDUCED GASTROPATHY
Sujata Sharma, Rafia Mir, Mau Sinha, Nagendra Singh, and Tej P. Singh
Department of Biophysics, All India Institute of Medical Sciences, New Delhi-110 029, India(lactotransferrin@yahoo.com)

Lactoferrin is a bilobal 80 kDa glycoprotein comprising of a single polypeptide chain
folded into two homologous N- and C-lobes. Each lobe is made up of two domains N1, N2
and C1, C2 respectively with iron binding sites situated in the interdomain clefts.
Non-steroidal anti-inflammatory drugs (NSAIDs) are most commonly prescribed drugs forarthritis and inflammatory conditions. Because of their widespread use, NSAID-related
gastrointestinal complications are recognized as the most prevalent drug toxicity in the world.
This drug toxicity comprises of bleeding and perforation in the esophagus, stomach, andduodenum due to NSAID effects on platelets and on other mucosal lesions. Though previous
studies have shown that orally administered human lactoferrin is effective at preventing
NSAID-induced intestinal injury, however, its mechanism of action was not clear. In thepresent study, the structures of C-terminal molecular half (C-lobe) of bovine lactoferrin withfour NSAIDS ; indomethacin, diclofenac, aspirin and paracetamol have been determined. The
C-lobe of lactoferrin was produced proteolytically with Proteinase K. The structures of thecomplexes of C-lobe with These structures have revealed a new site for the binding of
NSAIDS in the C2 domain The structures of C-lobes also revealed a new role for the
N-terminal residues of C-lobe which were involved in the interactions with N-lobe at theinterface in the intact lactoferrin. These structures reveal the mechanism by which
lactoferrin is effective at preventing NSAID-induced intestinal injury.

O5A07-M2

CRYSTAL STRUCTURES OF NATIVE BACTERIOPHAGEASSOCIATED HYALURONATE LYASE AND ITS COMPLXES WITH
LACTOSE AND ASCORBIC ACID
P. Mishra1, V. Bhakuni1, A. S. Ethayathulla2, R. Prem Kumar2, N. Singh2, S. Sharma2,
Kaur2, A. Srinivasan2 and T. P. Singh2
1

P.

Division of Molecular and Structural Biology, Central Drug Research Institute, Lucknow-226001,

India 2Department of Biophysics, All India Institute of Medical Sciences, New Delhi-110029, India

Hyaluronate lyases (HylP2) are a class of endoglycosaminidase enzymes withconsiderable complexity and heterogeneity. Their function is to degrade hyaluronan, the main
polysaccharide component of the host connective tissues into unsaturated disaccharide units
as the final product. Crystal structures of the cloned native enzyme and its complexes withlactose and ascorbic acid have been determined. The protein crystallized in hexagonal spacegroup with cell dimensions of a = b = 58.5Å, c = 583.5Å. The structure of HylP2 is composedof three intertwined polypeptides centered on a crystallographic three-fold axis. The Nterminal forms a mixed globular α/β capping region that is followed by a coiled region. The
central core of HylP2 forms a cylindrical arrangement with alternating β strands from each of
the three polypeptides. The external faces are shaped with depressions so as to allow theligand binding. The C-terminal region of the structure does not have intertwined β strands but
interdigitating strands. The end is concluded with α helical nose. Both lactose and ascorbic
acid have three binding sites in the central concave part of the molecule. The protein residues
that are involved in the interactions with ligands are Glu 167 and Lys 179 at site 1, Asn 182,
Asn 202, Arg 216 and Glu 214 at site 2 while Gly 223, Asn 241, Gln 261, Tyr 264 and Asn
226 are involved at site 3. At each site, there at least six hydrogen bonded interactions
indicating specific mode of binding of these ligands resulting in the inhibition of enzyme
activity.

O5A07-M3

STRUCTURAL AND MUTATIONAL STUDIES OF ANTHOCYANIN
MALONYLTRANSFERASES ESTABLISH THE FEATURES OF BAHDENZYME CATALYSIS
Hideaki Unnoa, Fumiko Ichimaidab, Hirokazu Suzukib, Seiji Takahashib, Yoshikazu Tanakac,
Atsushi Saitob, Tokuzo Nishinob, Toru Nakayamab and Masami KusunokidaFaculy of Engineering, Nagasaki University; c Department of Biomolecular Engineering, Graduate

School of Engineering, Tohoku University; c Suntory Research Center; d Institute for Protein Research,
Osaka University, 3-2 Yamada-oka, Suita, Osaka 565-0871,

The BAHD family is a class of acyl-CoA-dependent acyltransferases which are
involved in plant secondary metabolism and shows a diverse range of specificities for acyl
acceptors. Anthocyanin acyltransferases make up an important class of the BAHD family andcatalyze the acylation of anthocyanins that are responsible for most of the red-to-blue colorsof flowers. Here, we describe crystallographic and mutational studies of three similaranthocyanin malonyltransferases from red chrysanthemum petals: anthocyanidin
3-O-glucoside-6"-O-malonyltransferase(Dm3MaT1),
anthocyanidin
3-O-glucoside-3",6"-O-dimalonyltransferase (Dm3MaT2), and a homolog (Dm3MaT3).
Mutational analyses revealed that seven amino acid residues in the N- and C-terminal regions
are important for the differential acyl-acceptor specificity between Dm3MaT1 and Dm3MaT2.
The SeMet structure of Dm3MaT3 has been determined by the MAD method and the free andcomplex structures of Dm3MaT3 was refined at 2.2 Å and 2.1 Å resolution, respectively.
Crystallographic studies of Dm3MaT3 provided the first structure of a BAHD member, incomplex with acyl-CoA, showing the detailed interactions between the enzyme and acyl-CoA
molecules. The structure, combined with the results of mutational analyses, allowed us to
identify the acyl-acceptor binding site of anthocyanin malonyltransferases, which is
structurally different from the corresponding portion of vinorine synthase, another BAHD
member, thus permitting the diversity of the acyl-acceptor specificity of BAHD family to beunderstood.

O5A07-M4

CRYSTAL STRUCTURE OF
N-ACETYLGLUCOSAMINE-PHOSPHATE MUTASE, A MEMBER OF
THE ALPHA-D-PHOSPHOHEXOMUTASE SUPERFAMILY
Yuichi Nishitani,a Daisuke Maruyama,a Tsuyoshi Nonaka,a Akiko Kita,a Takaaki A. Fukami,bToshiyuki Mio,b Hisafumi Yamada-Okabe,b Toshiko Yamada-Okabec and Kunio Mikia, da

Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502,

Japan, bKamakura Research Laboratory, Chugai Pharmaceutical Company Ltd., 200 Kajiwara,
Kamakura, Kanagawa, 247-8530 Japan, cDepartment of Hygiene, School of Medicine, Yokohama City
University, 3-9, Fukuura, Kanazawa, Yokohama 236-0004, Japan, dRIKEN SPring-8 Center at
Harima Institute, Koto 1-1-1, Sayo, Hyogo 679-5148, Japan

N-acetylglucosamine-phosphate mutase (AGM1) is an essential enzyme in the synthetic
process of UDP-N-acetylglucosamine (UDP-GlcNAc). UDP-GlcNAc is a UDP sugar thatserves as a biosynthetic precursor of glycoproteins, mucopolysaccharides, and the cell wall ofbacteria. Thus, a specific inhibitor of AGM1 from pathogenetic fungi could be a new
candidate for an antifungal reagent that inhibits cell wall synthesis. AGM1 catalyzes theconversion of N-acetylglucosamine 6-phosphate (GlcNAc-6-P) into N-acetylglucosamine
1-phosphate (GlcNAc-1-P). This enzyme is a member of the alpha-D-phosphohexomutase
superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. Here
we report the crystal structures of AGM1 from Candida albicans for the first time, both in theapoform and in the complex forms with the substrate and the product, and discuss its catalytic
mechanism.
The structure of AGM1 consists of four domains, of which three domains haveessentially the same fold. The overall structure is similar to those of phosphohexomutases;
however, there are two additional beta-strands in domain 4, and a circular permutation occurs
in domain 1. The catalytic cleft is formed by four loops from each domain. The N-acetylgroup of the substrate is recognized by Val-370 and Asn-389 in domain 3, from which thesubstrate specificity arises. By comparing the substrate and product complexes, it is suggested
that the substrate rotates about 180° on the axis linking C-4 and the midpoint of the C-5—O-5
bond in the reaction.

O5A07-M5

SUBSTRATE SPECIFICITY OF PHOSPHODIESTERASES,STRUCTURAL INSIGHT INTO VIAGRA FUNCTION, AND
STRUCTURE-BASED DESIGN OF DRUGS FOR INFLAMMATORYDISEASES
Hengming Ke and Huanchen Wang,
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599,
USA

Cyclic nucleotide phosphodiesterases (PDEs) are key enzymes controlling cellularconcentrations of the second messengers cAMP and cGMP. Family selective PDE inhibitors
have been widely studied as therapeutics for treatment of various human diseases. For example,
PDE4 inhibitors have been studied for treatment of inflammatory diseases such as asthma andchronic obstructive pulmonary diseases (COPD) and PDE10 inhibitors for psychosis. The mostsuccessful example of this drug class is the PDE5 inhibitor sildenafil (Viagra) that has beenused for treatment of male erectile dysfunction and pulmonary hypertension. Human genome
encodes 21 PDE genes that have been grouped into 11 families. Alternative splicing of the 21
genes produces over hundred of PDE isoforms that contain a variable regulatory domain and aconserved catalytic domain. Individual families of PDEs specifically recognize substratescAMP and cGMP and possess their selective inhibitors. However, the basic issues of substratespecificity and inhibitor selectivity of the enzyme have not been extensively illustrated.
To elucidate the substrate specificity, the crystal structures of PDE10 and PDE4 incomplex with the substrates cAMP and cGMP have been determined at high resolution. The
PDE10 structures show that cAMP and cGMP bind in different conformations, suggesting thatthe substrates are recognized by different orientations and interactions. The PDE4 structure
reveals only one hydrogen bond between substrate cAMP and the invariant glutamine andtherefore provides direct evidence against the widely circulated mechanism of “glutamine
switch”. To study the inhibitor selectivity, the structures of PDE5 in complex with various
inhibitors have been determined. These structures reveal multiple conformations of the H-loop
at the active site of PDE5 upon binding of the inhibitors IBMX, icarisid II, sildenefil, andvardenafil (Levitra), in addition to the different configurations of two drugs vardenafil andsildenafil that have similar chemical formulae. These studies provide structure bases for thedifferent physiological behaviors of the inhibitors. The structure-based drug design has led to
discovery of a novel type of PDE4 selective inhibitors that are very potent in anti-inflammation
activity. The best one inhibits the TNFα release in human peripheral blood mononuclear cellsystem with IC50 of 40 nM, at least 10-fold more potent than cilomilast that is a GSK drug-leadin phase III clinic trial for treatment of COPD.

O5B07-M1

COMPLEMENTARY STUDIES OF ENZYME-RESISTANT STARCH IMPLICATIONS FOR HUMAN HEALTH
A. López-Rubioa, M. J. Gidleyb, A. K. Shresthab, B.M. Flanaganb, A. Htoonc,d, H. Chanvrierc,d,S. Uthayakumaranc,d, I.A.M. Appelqvistc,d, A.R. Birdc,e, D.L. Toppingc,e, M.K. Morellc and
E.P. GilbertaaBragg Institute, Australian Nuclear Science and Technology Organisation, Menai, NSWbCentre for Nutrition and Food Sciences, University of Queensland, St Lucia, QLD 4072, AustraliacCommonwealth Scientific and Industrial Research Organisation, Food Futures Flagship, Riverside

Corporate Park, North Ryde, NSW, AustraliadeFood Science Australia, Riverside Corporate Park, North Ryde, NSW, Australia

Food Science Australia, PO Box 10041, Adelaide, SA 5000

Resistant starch (RS) has been defined as the fraction of starch that escapes digestion in
the small intestine of healthy individuals, reaching the large bowel where it is fermented into
short-chain fatty acids (SCFA) by colonic bacteria. The beneficial health effects derived fromincreasing the amount of SCFA delivery in the colon (such as reduced glycaemic load,
apoptosis in colo-rectal cancer cells) have lead to a general interest in understanding thedifferent types of RS, aimed at designing food products with increased contents of thesefractions. Whilst hindering the access of the enzymes to the starch molecules is one of themechanisms preventing hydrolysis in, for example, RS types I and IV (physically inaccessible
and chemically modified starch respectively), processed starches, constituting the bulk ofingested starches in many diets, have a different mechanism of RS formation. Several studies
have focussed on the description of RS fractions from processed starches (RSIII), but little
attention has been paid to the digestion process itself, which from the present in vitro work, issuggested to play a key role.
In this work, a novel approach has been used to investigate the origin of RSIII using a
combination of small-angle X-ray scattering and X-ray diffraction, microscopy,
chromatography and NMR. High-amylose maize starch samples extruded under two different
processing conditions were characterised at different stages of amylase digestion underconditions shown to be representative of in vivo digestion, and compared with control samples
which were kept in the digestion solution without enzyme. From the results a comprehensive
picture of the changes occurring during amylase digestion is gained, providing the rationale
behind the “resistance-to-digestion” mechanism of processed high-amylose starches.

O5B07-M2

CRYSTAL AND MOLECULAR STRUCTURES OFORGANOPHOSPHORUS COMPOUNDS - CONFORMATION AND
BIOLOGICAL ACTIVITY OF HETEROCYCLIC MOLECULES
Musali Krishnaiah and Jadaprolu Radha Krishna

Department of Physics, Sri Venkateswara University, Tirupati-517502-India.

Structure and conformational studies of organophosphorus heterocycles have drawn
much interest in recent years, because of their applications as insecticides, bactericides,
fungicides, flame retardants, lubricants, pesticides, antioxidents, antitumor agents andstabilizers in polymers and oils. The structure determination on a series of organophosphorus
compounds have been carried out, to understand the influence of the substituents on theconformation and molecular geometry of the heterocyclic ring of different sizes and theirrelation to biological activity.
Structures of oxazaphosphorine derivatives reveal that six membered ring exhibits boat,
screw-boat and in between intermediate sofa and half chair conformation, where as
benzodioxaphosphorine ring adopts a boat form with different orientations of the substituents.
Substituted benzo and dibenzo-dioxaphosphepine derivatives (seven membered) show
twist-chair and distorted boat form and similar conformation has been found in eight
membered dibenzo substituted dioxaphosphocin derivatives. The most common geometricalobservation is that the equality in P-O bond lengths with homogeneous substituents andconsiderable variation depending on electronegativity of the fourth substituent at phosphorus.
It is interesting to observe the conformation changes when substituents are common but
differs with ring size and also with different substituents on the same ring. These structuralfeatures are correlated and discussed in terms of their biological activities, useful forindustrial applications.

O5B07-M3

INELASTIC X-RAY SCATTERING STUDY OF EXCITONPROPERTIES IN AN ORGANIC MOLECULAR CRYSTALKe Yang
JASRI/SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5198, Japan

Excitons in a complex organic molecular crystal were studied by inelastic x-ray
scattering (IXS) for the first time. The dynamic dielectric response function is measured overa large momentum transfer region, from which an exciton dispersion of 130 meV is observed.
Semiempirical quantum chemical calculations reproduce well the momentum dependence ofthe measured dynamic dielectric responses, and thus unambiguously indicate that the lowest
Frenkel exciton is confined within a fraction of the complex molecule. Our results
demonstrate that IXS is a powerful tool for studying excitons in complex organic molecularsystems. Besides the energy position, the IXS spectra provide a stringent test on the validityof the theoretically calculated exciton wave functions.

O5C07-M1

HIGH SPEED NEUTRON DIFFRACTION AT THE OPAL RESEARCH
REACTOR: THE WOMBAT INSTRUMENT
A.J. Studer, M. Avdeev, M.M. Elcombe, J.R. Hester, and V.K. Peterson
Bragg Institute, ANSTO, RMB 1, Menai 2234, NSW Australia

Wombat is an instrument designed for high speed powder diffraction at the OPAL
research reactor in Australia. It combines a high flux at the sample with a high speed detector.
The instrument is located along a 300mm high neutron guide which begins at the edge of thereactor core. Combined with a variable vertical focus monochromator, this enables the highflux at the sample. The detector is a compact, curved, continuous 120o design with two
dimensional area detection. It has very high throughput, easily capable of handling a million
events per second.
Wombat achieved “first neutrons” in February 2007, During its commissioning it has
demonstrated its power in rapid real time pattern acquisition. Measurements have been madein both “one shot” mode, where a dynamically changing system is measured in real time, and“stroboscopic” mode, where a rapidly cycling system is measured repeatedly to built up
statistics.
As well as high speed powder diffraction, Wombat is useful for single crystal
applications such as measuring diffuse scattering. The combination of high flux and a detector
with a large solid angle allow large regions of reciprocal space to be mapped with great
efficiency.

O5C07-M2

WATER-REDISPERSIBLE SINGLE WALL CARBON NANOTUBES
AND 40M SANS INSTRUMENT DEVELOPMENT AT HANARO
Sung-Min Choi,a Tae-Hwan Kim a, Changwoo Doe a, Young-Soo Hanb and Steven R KlinecaDepartment of Nuclear and Quantum Engineering, Korea Advanced Institute of Science andTechnology, Daejeon, Korea;Physics,; bHANARO Research Center, Korea Atomic Energy ResearchInstitute, Daejeon, Korea; cNIST Center for Neutron Research, Gaithersburg MD USA

Part I: Single-wall carbon nanotubes (SWNTs) have remarkable properties that have awide range of potential applications. In many cases, however, insolubility and bundling of
SWNTs in aqueous solution due to their strong hydrophobicity and van der Waals attraction,
respectively, are problematic for various practical applications. Here, we report a new type of
non-covalently (no covalent bonding between the dispersants and SWNTs) functionalized andindividually isolated SWNTs (p-SWNT) that are readily re-dispersible (by only 10 minutes ofmild vortex mixing) in water even after freeze-drying and stable for months long time period.
This was achieved by 1) dispersing SWNTs in water using cationic surfactants,
Cetyltrimethylammonium 4-vinylbenzoate (CTVB), which have polymerizable counterions(VB- ions), and 2) permanently fixing the surfactant layer on the SWNTs by polymerizing thecounterions. The dispersion quality and surfactant encapsulation structure of p-SWNTs arecharacterized by SANS, AFM and UV-vis NIR. Unlike the previous SWNT dispersions, thep-SWNT does not form any aggregates or networks at the concentrations investigated in thisstudy.
Part II: A 40m small angle neutron scattering instrument is being developed at
HANARO, Korea. The current progress and some details of design of the 40m SANS will bepresented.

O5C07-M3

FIRST RESULTS FROM THE NEW OPAL RESEARCH REACTOR
R. A. Robinson
Bragg Institute, Australian Nuclear Science and Technology Organisation, Menai, NSW 2234,
Australia.

Australian science is entering a new “golden age”, with the startup of bright newneutron and photon sources in Sydney and Melbourne, in 2006 and 2007 respectively. The
OPAL reactor and the Australian Synchrotron can be considered the greatest single
investment in scientific infrastructure in Australia’s history. They will essentially be “sister”
facilities, with a common open user ethos, and a vision to play a major role in international
science. Fuel was loaded into the OPAL reactor in August 2006, and full power (20MW)
achieved in November 2006. The formal user program commences in mid 2007, and somecommissioning experiments have already taken place well before then. The first three
instruments in operation are a high-resolution powder diffractometer (for materials discovery),high-intensity powder diffractometer (for kinetic studies) and a strain scanner (for mechanicalengineering and industrial applications). These will be closely followed by four more
instruments with broad application in materials science, physics, chemistry, biology,
engineering and the earth sciences. Instrument performance will be competitive with the best
research-reactor facilities anywhere. To date there is committed funding for 9 instruments,
with a capacity to install a total of ~18 beamlines. An update will be given on the status of
OPAL, its thermal and cold neutron sources, its instruments and the first data.

O5C07-M4

VERSATILE NEUTRON DIFFRACTOMETR AT J-PARC- IBARAKI MATERIALS DESIGN DIFFRACTOMETER T. Ishigaki,a A. Hoshikawa,b M. Yonemura,c F. Shikanai d T. Morishima, d T. Kamiyama,d K.
Aizawa,b T. Sakuma,b Y. Tomota,b M. Arai,b M. Hayashi,e K. Ebata,e Y. Takano,e K.
Komatsuzaki,e H. Asano,e Y. Takano,e T. KasaoeaDivision of Research & Development of Ibaraki Beam Line, Ibaraki University, 4-12-1

Nakanarusawa, Hitachi, 316-8511 Ibaraki, Japan; bJ-PARC Center, Japan Atomic Energy Agency,
2-4 Shirakata Shirane, Tokai, 319-1195 Ibaraki, Japan; cInstitute of Applied Beam Science, Ibaraki
University, 4-12-1 Nakanarusawa, Hitachi, 316-8511 Ibaraki, Japan; cNeutron Science Laboratory,
KEK, 1-1 Oho, Tsukuba, 305-0801 Ibaraki, Japan; eIbaraki Prefecture, 978-6 Kasahara, Mito,
310-8555 Ibaraki, Japan

Ibaraki prefecture, the local government of the area for J-PARC site, was decided tobuild a versatile neutron diffractometer (IBARAKI Materials Design Diffractometer) topromote an industrial application for neutron beam in J-PARC. This diffractometer is planned
to be a high throughput diffractometer so that materials engineers and scientists can use it likethe chemical analytical instruments in their materials development process. It covers in drange 0.18 < d (Å) < 5 with Δd/d = 0.16 % at high resolution bank, and covers 5 < d (Å) <800 with gradually changing resolution at three detector bank (90 degree, low angle and small
angle). Typical measuring time to obtain a ‘Rietveld-quality’ data is several minutes with thesample size of laboratory X-ray diffractometer. To promote industrial application, autilization system for this diffractometer is required. We will establish a support system forboth academic and industrial users who are willing to use neutron but have not been familiar
with neutron diffraction. The analysis software is also very important for powder diffraction,
we will also prepare a software package consisting of combination of several
powder-diffraction software, structural databases and visualization. The construction of this
instrument was already begun and will be completed in the beginning of 2008, as one of
day-one instruments for J-PARC. The current status for this instrument also will be reported.

O6A07-A1

TACKLING A MUNC-Y PUZZLE: STRUCTURE OF THE MUNC18C
PROTEIN
Jennifer L Martin1, Shu-Hong Hu1, Catherine F. Latham1, Christine L. Gee1, David E. James2
1 Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD, Australia
2 Garvan Institute, Sydney, NSW, Australia

Sec1p/Munc18 (SM) proteins bind to SNARE (Soluble NSF-attachment protein
receptors) proteins and play an essential role in membrane fusion. Divergent modes ofregulation have been proposed for different SM proteins indicating that they can either
promote or inhibit SNARE assembly. This is in part due to discrete modes of binding thathave been described for various SM/SNARE complexes. One mode suggests that SM proteinsbind only to Syntaxins, preventing SNARE assembly, whereas in another they facilitate
SNARE assembly and bind to SNARE complexes.
The mammalian cell surface SM protein Munc18c binds to an N-peptide in Sytaxin4
and this is compatible with its interaction with SNARE complexes. We determined the crystal
structure of Munc18c in complex with the Syntaxin N-peptide. This structure shows
remarkable similarity with a yeast complex indicating that the mode of binding, which canaccommodate SNARE complexes, is highly conserved throughout evolution. Modelling
reveals that the N-peptide binding mode is present in most but not all yeast and mammalian
SM/Syntaxin pairs suggesting that it has co-evolved to fulfill a specific regulatory function.
The likely regulatory function will be discussed.

O6A07-A2

CRYSTAL STRUCTURE OF DsrEFH, A PROTEIN ESSENTIAL FOROXIDATION OF STORED SULFUR IN THE PURPLE SULFURBACTERIUM ALLOCHROMATIUM VINOSUM
Dong Hae Shin1*
1College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea*

Corresponding author

In the purple sulfur bacterium Allochromatium vinosum, the dsrEFH genes are part ofthe dsr operon the products of which are involved in the oxidation of sulfur stored in
intracellular sulfur globules. We proved the essential role of DsrEFH in this process with an A.
vinosum ∆dsrE mutant unable to oxidize accumulated sulfur. To assist functional assignment
in detail, we also determined the crystal structure of the soluble α2β2γ2-structured A. vinosum
DsrEFH at 2.5 Ǻ resolution. Each of DsrE, DsrF, and DsrH has a single domain with the
YchN fold. Structural comparison revealed that the conserved cysteine 78 of A. vinosum DsrE
corresponds to the active site cysteines of E. coli YchN and TusD. The putative active site in
DsrE is formed between interfaces of DsrE and DsrF with a depth of ~11 Ǻ and a width of ~6Ǻ x 14 Ǻ. Based on a structural comparison with E. coli TusBCD, a sulfur transfer activityof DsrE through Cys78 has been suggested. A big cleft with a depth of ~11 Ǻ and a width ofabout ~ 10 Ǻ x 30 Ǻ is apparent on the surface of DsrFH. Since the highly conserved
residues Cys20, His5 and Trp101 of DsrH are constellated in this pocket, this cleft probably
constitutes another active site. Amino acid sequence comparisons and phylogenetic analyses
indicate that the presence of two different types of putative active sites in DsrE and DsrH is acommon and unique trait of DsrEFH proteins from sulfur-oxidizing organisms.

O6A07-A3

STRUCTURAL AND COMPUTATIONAL STUDIES ON TYPE II RIPs
Alok Sharma,a A.A. Jeyaprakash,a M.J.Swamy b and M.Vijayan aaMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India. bSchool of Chemistry

University of Hyderabad, Hyderabad, India.

The crystal structures of six type II Ribosome Inactivating Proteins (RIPs) have beenreported. Each structure consists of a catalytic domain and a lectin domain made up of two
β-trefoils. Each trefoil involves one sugar binding site. Among the RIPs of known structure,
four are toxic. One is non-toxic on account of defect in carbohydrate binding. The roughstructure of another non-toxic type II RIP is also available, although the reason for theabsence of toxicity has not been elucidated. Here we report the structure of a non-toxic type II
RIP from Snake gourd (Trichosanthes anguina) at 2.4 Å resolution. A detailed analysis of thestructure and its interactions indicates that a combination of changes in the active site in the
catalytic domain and alterations in carbohydrate binding is responsible for the abolition of
toxicity. An exhaustive search of sequence data led to the identification of close to thirty
non-redundant type II RIPs. The three-dimensional structures of some of them are alreadyknown. Homology models were constructed for representatives from the remaining RIPs. A
comparison of these structures and models provides further insights into the molecular basisof the toxicity and the absence of it in some cases, of type II RIPs.

O6A07-A4

STRUCTURAL STUDIES OF THE CPX PATHWAYH ACTIVATOR
NLPE ON THE OUTER MEMBRANE OF ESCHERICHIA COLI
Yu Hirano,a Md. Motarab Hossain,b Kazuki Takeda,a,c Hajime Tokudab and Kunio Mikia,ca Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto, Japan; b Institute of
Molecular and Cellular Biosciences, University of Tokyo, Tokyo, Japan; c RIKEN SPring-8 Center at
Harima Institute, Hyogo, Japan.

NlpE is an outer membrane lipoprotein widely found in Gram-negative bacteria. NlpE isanchored on the periplasimc side of the outer membrane with three acyl chains at the
N-terminal cysteine residue. During envelope stress responses, NlpE functions as an activatorof the Cpx signal transduction pathway. In Escherichia coli, adhesion to abiotic surfaces has
been reported to activate the Cpx pathway in an NlpE-dependent manner. External copper
ions are also thought to activate the Cpx pathway mediated by NlpE. Based on the propertiesof the Cpx pathway, the activating signals are probably related to the accumulation of
misfolded or mislocated proteins in the envelope. We determined the crystal structure of NlpE
from E. coli at 2.6 Å resolution. The structure showed that NlpE consists of two β-barrel
domains. The N-terminal domain resembles the bacterial lipocalin Blc, and the C-terminal
domain has an oligonucleotide/oligosaccharide binding (OB) fold. NlpE from E. coli
possesses characteristic sequence motifs, such as the Cys-X-X-Cys (CXXC) motif (31-CADC)
and the serine protease inhibitor signature (99-MLDREGNPIESQFNYTL). The four
conserved cysteine residues of NlpE were investigated by both biochemical analyses and the
crystal structure. Deducing from these studies, the cysteine residues in the CXXC motif may
be chemically active. Furthermore, two monomers in the asymmetric unit form an unusual 3D
domain-swapped dimer. One of the strands of each N-terminal β-barrel is made of analternative chain in the asymmetric unit. These structural features suggest that NlpE can easily
unfold at the β-strand of the N-terminal β-barrel. The unfolding of the single strand at
the β-barrel has a notable similarity to the loss of donor strand complementation in PapE
causing activation of the Cpx pathway. These findings indicate that tertiary and/or quaternary
structural instability of NlpE may be responsible for Cpx pathway activation.

O6A07-A5

CRYSTAL STRUCTURE OF IL-15/IL-15RALPHA COMPLEX
Mami Chirifu1, Chiharu Hayashi1, Teruya Nakamura1, Sachiko Toma2, Tsuyoshi Shuto1,
Hirofumi Kai1, Yuriko Yamagata1, Simon J. Davis3 and Shinji Ikemizu1
1Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan, 2Graduate
School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan, 3Nuffield Department ofClinical Medicine and MRC Human Immunology Unit, The University of Oxford, Oxford, Oxford UK

Interleukin (IL)-15 contributes to CD8+ T-cell memory acquisition and natural killer cell
generation, whereas IL-2 has a pivotal role in the expansion and functions of regulatory andactivated effector T cells. The IL-15 and IL-2 receptors belong to the common γ cytokine
receptor class and share signal-transducing β and γ subunits. Within the γ-chain class, theIL-15 and IL-2 receptors are unique insofar as specificity is provided by a third, higher
affinity “private” receptor α-subunit. Whereas the private IL-2Rα subunit is co-expressed withβ and γ on T- and B-cells ostensibly to allow cell-autonomous signaling, IL-15Rα is expressedin trans on antigen-presenting cells. The 1.85Å crystal structure of the human IL-15/IL-15Rαcomplex accounts for the specificity of cytokine recognition, highlighting the high degree ofelectrostatic and geometric complementarity between the acidic receptor-binding surface of
IL-15 and the basic ligand-binding region of IL-15Rα, and the essential role of binding-sitewaters in forming this very high affinity complex (Kd = 38 pM). In spite of very low
IL-15/IL-2 sequence homology and the distinct architectures of the cytokine-binding “sushi”
domains of each receptor, the receptor binding foot-prints of each cytokine, and therefore thetopologies of both the IL-15/IL-15Rα and IL-2/IL-2Rα complexes, are remarkably similar.
Overall, there appear to be no structural obstacles to the in trans presentation of either
cytokine. Our findings suggest that antigen-experienced IL-2Rα+ T cells could, in principle,
enhance IL-2Rα- T cells responses via the direct presentation of IL-2.

O6B07-A1

IXS STUDY OF EXCITATION PROPERTIES OF ORGANIC
MOLECULAR CRYSTALS AND SIMPLE MOLECULES
Binping Xie,a Ke Yang,a Y. Q. Cai,b N. Hiraoka,b Donglai Fengaa

Department of Physics, and Applied Surface Physics state Key Laboratory, Fudan University,

Shanghai 200433, China; bNational Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan,
Republic of China.

Inelastic x-ray scattering (IXS) has proven to be a powerful tool for investigating theelectronic excitations in inorganic systems. For example, IXS data have helped ourunderstanding of the metal-insulator transition, Plasmon excitations, and band gap. IXS is aclean and direct probe of the dynamic structure factor S(q, ), which is proportional toq2Im( -1),
being the dynamic dielectric function. In comparison with high energy
electron-energy-loss spectroscopy (EELS), IXS is almost free from multiple scattering effects,
and it can generate reliable information at high momentum transfer q. Therefore, IXS is
particularly advantageous for studying electronic excitations that are more constrained inspace in organic molecular crystals and simple molecules.
Our group developed a new method to study excitons in a complex organic molecular
crystal by IXS. The dynamic dielectric response function is measured over a large momentum
transfer region, from which an exciton dispersion of 130meV is observed. We further
developed this method to study other interesting system like C60 and gas molecules. Good
results are obtained, which will be presented and discussed.

O6B07-A2

MOLECULAR DYNAMICS IN SEVERAL CHLORINE COMPOUNDSON THE BASIS OF X-RAY THERMAL PARAMETER, IR/RAMAN AND
NQR DATA
L. Ramu and R. Chandramani.
E-mail - sarasaramu76@hotmail.com
Phone – +91 -09880047250
Department of Physics, Bangalore University.

Bangalore, INDIA.560056

Molecular dynamics (Torsional frequencies-fT) in several organic and inorganic
chlorine compounds have been evaluated on the basis of X-ray thermal parameters,IR/Raman
and NQR data. NQR Studies gives useful
information
about
the
molecular
dynamics and phase transitions in solids. Usually
the fT obtained through NQR data arecompared with FT IR/Raman data. Here an approach has been made to evaluate fT at room
temperature using available data on X-ray thermal parameters.
Temperature factor of an atom for any set of lattice planes (hkl) depends on the interplanar spacing and on the magnitude of vibration perpendicular to the planes. There is anexpression, which relates general temperature factor, the reciprocal lattice parameters andthermal parameters (Uij) expressed in terms of mean square amplitudes (<θ2>) of vibration in
Pm2. The NQR motional averaging has been shown to arise from temperature dependent
tilting of the z-axis of the EFG tensor. One can therefore estimate <θ2> for various C-Cl bonddirections, which define the respective z-axis of the EFG tensor using the X-ray thermal
parameters.
The fT at T=300K in the following compounds has been done:(1) Barium Chlorate monohydrate.
(2) Bismuth Trichloride.
(3) 1-chloro 2,4 -dinitrobenzene.
(4).4-Chlorophenoxyacetic acid.
(5).2, 4- Dichlorophenoxyacetic acid.
(6).Monochloroacetic acid.

The fT obtained by X-ray thermal parameters, IR/Raman and by NQR data have been
compared. The values obtained in all the three cases are in good agreement. The above
approach is a good illustration of the supplementary nature of the data from X-ray studies inrelation to NQR studies of compounds in solid state. It is also interesting to compare thisvalue with Raman data and Infrared data.
Reference:1).L.Ramu, R.Banu, S.Rani and R.Chandramani. ACTA PHYSICA POLONICA-A,
775,Vol-109(2006).

O6B07-A3

VAPOR INDUCED GUEST EXCHANGE OF ORGANIC INCLUSIONCRYSTAL
Hidehiro Uekusa, Yasunari Ashida, Kotaro Fujii
Department of Chemistry and Materials Science, Tokyo Institute of Technology, Japan

Among many characteristics of organic host-guest crystal, guest releasing and absorbing
ability is one of the most attracting ones. By using this kind of crystal, controlled release offunctional materials such as pharmaceuticals or chemicals is realized. In usual, the guest
releasing is achieved by heating or mechanical crushing; however, it is also possible byapplying vapor to crystal and sometimes the guest exchange occur.
In this study, some examples of the guest releasing or exchange phenomena by vapor
application and their crystal structure change are presented. As the organic host framework
is rather soft and it has guest induced structure, the single crystalline form of the organic
inclusion compound often corrupted after guest release or exchange. In that case, crystal
structure determination from powder diffraction data (SDPD) is very powerful technique andwell utilized in this study.
By application of water vapor, pyromellitic acid di-methanol solvates crystal lost
methanol molecules and new dihydrate crystal was grown as powder crystalline form. Also,
the methanol and water guests were lost in ambient condition or by heating to form
dehydrated powder crystal. The crystal structure analysis was successfully performed by
SDPD technique. In di-methanol and dihydrate form, there are large channels, throughwhich guest molecules are easily in and out. In dehydrate form; the channel is closed bysmall displacement of hosts and hydrogen bonds are formed, so the absorption of watermolecule to recover the dihydrate form proceeds slowly. The reverse process (hydrate tomethanol solvate) was not observed because the methanol solvate is rather unstable in the air.
Reversible guest exchange process by vapor application was observed between
1,1,2,2-tetrakis (4-hydroxyphenyl) ethane methanol and water solvates. Also in this case,
crystal structures share common solvent channel feature and similar hydrogen bonding pattern,which should be the keys for guest exchange phenomena.
O

O

Water vapor
PMA : hydrate

HO

OH

HO

OH
O

heatingO

PMA : methanol

ambient

Water vapor
PMA

O6B07-A4

CONCERTED STRUCTURAL CHANGE AND PHOTOCHROMISM OF
TRANS-BIINDENILIDENEDION DERIVATIVES
Akiko Sekine,a Kumiko Aruga,a Hidehiro Uekusa,a Katsuya Souno b and Koichi Tanaka b
aDepartment of Chemistry and Materials Science, Tokyo Institute of Technology, Tokyo 152-8551,

Japan, bDepartment of Applied Chemistry,, Kansai University, Osaka 564-8680, Japan

Crystals of trans-biindenylidenedione (TBID) derivatives show photochromism and thecolor changes from yellow to red upon irradiation with UV and visible light [1]. In ourprevious study, crystal structure determination of several derivatives and theirpseudo-polymorphs was performed in order to reveal the photochromic reaction mechanism.
The crystal structures after irradiated with UV light (red form) were analyzed to show both
the reactant (1a) and the photoproduct (1b) were located as a disordered structure, indicatingthat the photochromism is caused by an intramolecular (Norrish Type II) hydrogen transfer
reaction.
In this study, the relationship between the crystal structures of TBD and theirphotochromic properties is presented. From the comparison of the crystal structures and thelife-time of red-colored photoproduct, it is elucidated that the following three factors areimportant for photochromism; (1) molecular conformation of the initial crystal, (2) cavity sizearound the reactive part of the molecule, and (3) cooperative movement of the solvent
molecules in the crystal.
For example, both of the crystal of TBID with Ar=4-F-Ph and its toluene solvate haveZ’>1 and they show a very long photoproduct lifetime of more than 200 hrs. A careful
investigation of their crystal structures revealed that only the molecule which has the mostfavorable conformation is photo-reactive and the occupancy of the corresponding
photoproduct is very high. Moreover, the molecules surrounding the photo-reacting
molecule are slightly shifted in position to allow the generation of photoproduct molecules.
Thus, it is concluded that this kind of concerted crystal structure change would stabilize the
red-colored photo-product and realize exceptional long-life photochromic specie.
Reference:[1] Koichi Tanaka et al., CryslEngComm., 2004, 6(2), 1-4
hv
Δ

1a

1b

O6B07-A5

CRYSTAL STRUCTURE ANALYSES OF CIS/TRANS
PHOTOISOMERIZATIONS
Jun Harada, Mayuko Harakawa and Keiichiro Ogawa
Graduate School of Arts and Sciences, The University of Tokyo, Komaba

Cis-trans photoisomerization is one of the most important types of photoreactions, andinnumerable studies on the subject have been carried out. The photoisomerization in the solidstate, however, has generally been considered difficult to take place, and only a limited
number of studies have been reported. In this study, we investigated the solid-state
photoreactions of 2-(9-anthrylmethylene)-1-indanone and its derivatives. We have found thatsome of the compounds photoisomerize in their crystals. We succeeded in observing the
crystal structural changes accompanying the isomerizations using X-ray diffraction analysis.
The results showed that the solid-state photoisomerizations of these compounds proceed
through the one bond flip of the isomerizing double bonds, and that the shapes of themolecules do not change so much before and after the reactions.

O6B07-A6

CRYSTALLINE STATE PHOTO ISOMERIZATION OF ANORGARNO-DIRHODIUM DITHIONITE COMPLEX
Koshiro Toriumi,a Hiroshi Kanamono,a Shouichi Hashimoto,a Yoshiki Ozawa,a Minoru
Mitsumi,a Hidetaka Nakai,b Yousuke Miyano,b Yoshihito Hayashi,b and Kiyoshi Isobe.baGraduate School of Material Science, University of Hyogo, Hyogo 678-1297, Japan;bGraduate School of Natural Science and Technology, Kanazawa University, Kanazawa 920-1192,

Japan.

An orgarno-dirhodium dithionite complex [{Rh(η5-C5Me5)}2(μ-CH2)2(μ-O2SSO2)](1)shows fully reversible photochromism in which one of four terminal oxygen atoms in theside-on type dithionite μ-O2SSO2 moiety is converted to a bridged one to produce geometricalisomer form μ-OSOSO2 by visible light irradiation in crystalline-state [1,2].
An analogous dirhodium complex [{Rh(η5-C5Me4Et)}2(μ-CH2)2(μ-O2SSO2)] (2) whichhas η5-C5Me4Et instead of η5-C5Me5 is isostructure to (1), and both the crystals belong to thesame space group P21/n and have almost the same cell parameters. We have tried to analyze
the photo-isomerization process of the dirhodium complex (2) in crystalline state by X-ray
structure analyses. The photo-irradiation time and light intensity dependencies of thephoto-generated isomer ratio were measured for (2). As a result, it was revealed that kind of
the main product of photo-generated isomers and their total ratio for (2) were different to thecase for (1). Sum of the ratios of the photo-generated isomers for (2) was about 30% for the
low intensity irradiation case but about 90% for the high intensity case. These phenomena
seem to suggest that the photo-isomerization processes in crystalline states occur
stereoselectively depend on reaction cavity and also an increase in crystal mosaicity owing tophoto irradiation.
Reference:
1) H. Nakai, M. Mizuno, T. Nishioka, N. Koga, K. Shiomi, Y. Miyano, M. Irie, B. K.
Breedlove, I. Kinoshita, Y. Hayashi, Y. Ozawa, T. Yonezawa, K. Toriumi, and K. Isobe,
Angew. Chem. Int. Ed., 2006, 45, 6473-6476.
2) Y. Ozawa, T. Yonezawa, T. Yokoyama, M. Mitsumi, K. Toriumi, H. Nakai, Y. Hayashi, and
K. Isobe, AsCA 06/CrSJ, Tsukuba, Japan, 2006/11.

O6C07-A1

STRUCTURE DETEMINATION FROM HIGH RESOLUTIONSYNCHROTRON POWDER DIFFRACTION DATAEIji Nishibori,a Shinobu Aoyagi,a and Makoto SakataaaDepartment of Applied Physics, Nagoya University

The crystal structure determination from powder diffraction (SDPD) has attracted wide
interests for its huge potential to accelerate a design, synthesis, and characterization of thematerials in the fields of nano- and bio- technologies. During past decade, many studies of
SDPD have been reported on the methodology, the software, and also the actual ab initio
structural determinations. Presently, the structure of small molecule with less than 30 atoms
and approximately 10 degree of freedoms can routinely solve by the several software on
single personal computer from powder data of laboratory X-ray source. The SDPD for large
systems such as medium-sized pharmaceuticals are still difficult task due to a large number ofdegree of freedoms. High resolution powder data and additional techniques for structure
solution have been normally required for SDPD in these cases. In the present study, we have
performed SDPD for medium-sized pharmaceutical, Prednisolone Succinate, using highresolution synchrotron X-ray powder diffraction data.
The data used in the present study are collected at BL02B2, SPring-8. The d-spacing
range of the data is d>1.0Ǻ, which is much wider than that of laboratory data, d>2.0-1.4Ǻ.
The structure determination has been carried by the original Genetic Algorithm (GA) system.
The number of degree of freedoms in the GA analysis is 25. In the refinement process, theMaximum Entropy Method (MEM) analysis has played a crucial role to have a better
structure model. The reliability factors, Rwp and RI, of the final structure analysis by the
Rietveld refinement reach less than 3% and 5%, respectively. The reasonable structure
including hydrogen atoms of medium-sized pharmaceutical with no check-cif Alert relating to
the fundamental structure such as inter-atomic distances and bond angles has been determinedin the present study.

O6C07-A2

STRUCTURAL STUDIES EMPLOYING HIGH ENERGY POWDERDIFFRACTION
Peter L. Lee
Advanced Photon Source, Argonne National Laboratory, Argonne, IL 60439, U. S. A.

The structural information is crucial for all materials research projects. The increasing
complex materials process critically needed the timely feed back of the structural information
during the initial discovery stage. However, most of the materials being studied do not havea single crystal form suitable for the routine crystal structure determination. Powder
diffraction becomes a critical tool that can determine the structure or follow structural changes
parametrically.
The high energy third generation synchrotron sources such as Advanced Photon Source
are capable of producing extremely intense high-energy x-rays has opened a wide variety ofimportant structural research opportunities. Combining advanced specialized undulators andoptics designed can produce unprecedented brilliance and photon flux for the high energy
x-rays. The use of high x-ray energies for powder diffraction largely eliminates theabsorption and extinction effects, opening the possibility to study many materials containing
high-Z elements. The ability to penetrate through bulk materials and/or environmental cell
enables us to examine the insight dynamically under extreme and carefully controlled
conditions. The short wavelengths also allow the measurement of very high Q data,
providing more structure detail and satisfying the requirement of the Pair Distribution
Function analysis.
Recent development of high energy powder diffraction at the Advanced Photon Source
will be presented including the advancement of instrumentation and new research
opportunities.
Use of the Advanced Photon Source was supported by the U. S. Department of Energy, Officeof Science, Office of Basic Energy Sciences, under Contract No. DE-AC02-06CH11357.

O6C07-A3

EXPECTING THE UNEXPECTED. PHASE TRANSITIONS IN
MANGANESE PEROVSKITES
Brendan J Kennedy,a and Zhaoming Zhang,baSchool of Chemistry, The University of Sydney, Sydney Australia; b Institute for Materials andEngineering, ANSTO, Australia

Manganese perovskites, have the general formula AMnO3, and exhibit a rich anddiverse range of structures, the precise structure depending on the oxidation state of themanganese, both Mn3+ (d4) and Mn4+ (d3+) are found in perovskite type oxides, the size of
the A-type cation and the presence of any vacancies in the lattice. Following the discoveryof colossal magnetoresistance in LaMnO3 considerable effort has been made towards
understanding the complex interplay between orbital ordering associated with the Jahn-Tellar
active Mn3+ ions and the tilting of the MnO6 polyhedra associated with the relative sizes of
the cations.
The present work describes structural studies, using a combination of high resolution
synchrotron X-ray and neutron diffraction, of three series of manganese perovskites; namely
the Mn4+ containing oxides of the type Ca1-xSrxMnO3; and the mixed valence Mn3+/4+ oxides
Sr1-xCexMnO3 0.075 < x < 0.4 and Sr0.9-xCaxCe0.1MnO3 0.0 < x < 0.9. In the first series the
progressive replacement of the Ca2+ by the smaller Sr2+ cation induces a first orderorthorhombic (Pnma) to tetragonal (I4/mcm) transition associated with tilting of the octahedra.
Introducing Mn3+ into the structure, by partially replacing Sr2+ with Ce3+, results in a large
Jahn-Tellar induced tetragonal distortion of the MnO6 octahedra and the formation of a second
orthorhombic phase in Imma.
Progressive replacement of Sr by Ca in Sr0.9-xCaxCe0.1MnO3
results in a reduction in the distortion of the unit cell, but an increase in the distortion of the
MnO6 octahedra. We present the clearest evidence to date for the independence of theorbital ordering and octahedral titling in these oxides.

O6C07-A4

MORPHOTROPIC PHASE BOUNDARY LIKE CHARACTERISTIC INA LEAD-FREE, AND NON-FERROELECTRIC SYSTEM(1-x)NaNbO3-xCaTiO3
Saurabh Tripathia, Rajeev Ranjana, Dhananjai Pandeya, Sanjay Kumar Mishrab and P.S.R.
KrishnabaSchool of Materials Science and Technology, Institute of Technology, Banaras Hindu University,

Varanasi-221005, India; bSolid State Physics Division, Bhabha Atomic Research Centre, Trombay,
Mumbai-400085, India.

The phase diagrams of several mixed solid solutions of the ABO3 type perovskites
contain a nearly vertical morphotropic phase boundary (MPB) separating tetragonal andrhombohedral phase fields. The MPB composition has been found to be of special
technological significance for numerous sensor and actuator devices, as several physicalproperties like dielectric permittivity, electromechanical coupling coefficients andpiezoelectric strain coefficients are maximized around this composition. In the well known
commercial
MPB
systems,like
Pb(ZrxTi(1-x))O3(PZT),(1-x)[Pb(Mg(1/3)Nb(2/3))O3]-xPbTiO3(PMN-xPT) and (1-x)[Pb(Zn(1/3)Nb(2/3)O3]-xPbTiO3(PZN-xPT), thispeak in the composition dependence of dielectric and piezoelectric properties around the MPB
has been linked with the change of crystal structure from tetragonal to rhombohedral througha narrow range of stability of monoclinic phases. The toxicity of lead oxide and its highvapour pressure during processing of these MPB ceramics have led to the search foralternative environmentally friendly materials free from lead. The MPB systems discoveredso far, be it lead-based or non-lead based, have at least one component, which is ferroelectricin nature (e.g. PbTiO3, KNbO3, LiNbO3). We present here MPB like characteristic in a newlead free system, (1-x)NaNbO3-xCaTiO3 (NN-xCT), in which the end members NaNbO3 and
CaTiO3 are well known antiferroelectric and paraelectric materials, respectively, underambient conditions. At low temperatures, antiferroelectric NaNbO3 transforms to aferroelectric phase while CaTiO3 exhibits quantum paraelectric behaviour. The composition
dependence of the room temperature dielectric permittivity of this mixed system exhibits a
sharp rise in the composition range 0.10<x<0.20 with a peak at x≈0.16. This anomalous risein the dielectric permittivity is shown to be linked with a change of crystal structure from an
orthorhombic structure in the Pbma space group for x≤0.10 to another orthorhombic structure
but in the Pbnm space group for x≥0.20. This behavior is reminiscent of a similar rise in the
dielectric permittivity near the MPB composition of the technologically important PZT and
PMN-xPT ceramics due to a change of crystal structure from tetragonal to rhombohedral.
Further, the composition dependence of the (+) and (-) tilt angles due to M and R point
phonon instability with wave vectors (1/21/21/2) and (1/21/20) of the cubic brillouin zone havebeen discussed in detail. Bond lengths and bond angles have been calculated to show thenature of the octahedral distortion. To the best of our knowledge, the NN-xCT ceramics are
the first example of a non-ferroelectric and non-piezoelectric MPB system in contrast to thewell known MPB systems which are all ferroelectric and piezoelectric.

O6C07-A5

SYNCHROTRON RADIATION X-RAY DIFFRACTION AND
SPECTROSCOPIC ELLIPSOMETRY INVESTIGATION OF Si3N4 ON Si
FOR SUB-50NM Si-IC APPLICATIONSZhe Chuan Fenga,* , Li-Chi Cheng a, Chu-Wan Huang a, Ying-Lang Wang b, and Hwo-Shuenn
Sheu caInstitute of Photonics & Optoelectronics and Department of Electrical Engineering, National Taiwan

University, Taipei, Taiwan 106-17, ROC;b

Taiwan Semiconductor Manufacturing Company, Tainan, 741-44 Taiwan, ROC;c

National Synchrotron Radiation Research Center, Hsinchu, 300-76 Taiwan, ROC.

* E-mail: zcfeng@cc.ee.ntu.edu.tw

Silicon nitride (Si3N4) is an advanced material and has the potential to be used invarious applications due to good performance in mechanical, chemical, electronic, andthermal properties. On the other hand, its high doping concentration, and chemical stabilities
are similar to the III–N compounds such as GaN and AlN, which are used to grow quantum
well structures for obtaining blue laser. They play an important role in the electronics industry,
especially in Si-based large-scale integration circuit technology and possibly in
optoelectronics. The sample is constructed from 50 nm Si3N4 thin film grown on 12” silicon
substrate by chemical vapor deposition (CVD) process which is from our collaboratorTaiwan Semiconductor Manufacturing Company (TSMC) company. We have performed thesynchrotron radiation X-ray diffraction (SR-XRD) experiments on Si3N4 using a shortwavelength (~0.443Å) in National Synchrotron Radiation Research Center (NSRRC). The
thickness, reflectance index and extinction coefficient of Si3N4 thin film were also determinedusing variable angle spectroscopic ellipsometer (VASE). By the using of superior
experimental instruments, we found from the XRD pattern that there is a mixture state of αand β- Si3N4 and other impurities present in the samples. We are going to plan another set ofsynchrotron XRD measurements using another energy synchrotron source to have different
wavelengths excitation XRD data on the samples. This will benefit to analyze the studiedmaterials and lead to better understand materials properties.

P05-001

ENGINEERING MATERIALS DIFFRACTOMETER AT J-PARC
Stefanus Harjoa, Atsushi Moriaia, Kentaro Suzuyaa, Kazuya Aizawaa, Kaori Shirakiharab, Yo
Tomotac, Koichi Akitad, Masatoshi Araia, Yukio MoriieaJ-PARC Center, Japan Atomic Energy Agency, Tokai, Ibaraki, Japan; bDepartment of MechanicalEngineering, Suzuka National College of Technology, Suzuka, Mie, Japan; cInstitute of Applied Beam
Science, Ibaraki University, Hitachi, Ibaraki, Japan; dDepartment of Mechanical System Engineering,Musashi Institute of Technology, Tokyo, Japan; eQuantum Beam Science Directorate, Japan Atomic
Energy Agency, Tokai, Ibaraki, Japan.

The Engineering Materials Diffractometer TAKUMI is now being developed at J-PARC
project. TAKUMI is one of the prospective instruments to promote industrial users at J-PARC,
and has main specifications as follows. A high intensity to realize short measuring times thatare particularly necessary for in situ measurements, a high resolution to assure high accuracies
on stresses measurements and microscopic strains measurements, an enough wavelength
bandwidth to assure many reflections for analyzes of anisotropic deformation behaviors andtextures in bulk engineering materials, etc.
TAKUMI views a decoupled-poisoned liquid H2 moderator, having the primary and thesecondary flight paths of 40m and 2.0m, respectively. It will have the 90 degree scattering
detector banks with 75° < 2θ < 105° and off angle of ±20°, and a curved supermirror neutron
guide with focusing-vertically tapered at the tail part. From a Monte Carlo simulation, an
appropriate resolution of about 0.15% in Δd/d has been confirmed at a high resolution mode.
TAKUMI has an effective wavelength bandwidth of about 3.5Å at a 25Hz disk chopper
operation (similar to pulse repetition rate), that gives more than 15 reflections including thelowest index for steel samples. Details of the designs and the construction progresses arepresented.

P05-002

CURRENT STATUS OF IBARAKI BIOLOGICAL CRYSTALDIFFRACTOMETER IN J-PARC
Ichiro Tanaka,a Takashi Ohhara,b Kazuo Kurihara, b Katsuhiro Kusaka, c Takaaki Hosoya, cKatsuaki Tomoyori, d Nobuo Niimura, d Tomoji Ozeki, e Kazuya Aizawa, c Masatoshi Arai, cYukio Morii, b Makoto Hayashi, f Kazuhiro Ebara f and Yoshiki Takano faDept. Biomol. Func. Eng., Ibaraki Univ.; bQuantum Beam Sci., Japan Atomic Energy Agency, Tokai,

Ibaraki 319-1195, Japan; cJ-PARC Center, Japan Atomic Energy Agency; dInst. Appl. Beam Sci.,
Ibaraki Univ.; eDept. Chem. Mat. Sci., Tokyo Institute of Technology; fIbaraki Prefectural
Government.

IBARAKI Biological Crystal Diffractometer is a new single-crystal neutron
diffractometer for biological and chemical crystallography, and is now being constructed at
J-PARC by Ibaraki Prefectural Government in Japan. This diffractometer is designed for theprotein crystals with the cell dimension up to 135Å. The measurement efficiency is more than
50 times larger than the present neutron diffractometer, BIX-3/BIX-4 in JRR-3 reactor at
JAEA. To achieve this performance, we’ve selected a coupled moderator, and worked out the
optimisation of the neutron guide tube. For the detector, a new wavelength-shifting-fiber type
scintillation area detector system with high spatial (0.5-1.0mm) and time (1μs-) resolution are
in development.

P05-003

PROGRESS REPORT ON SUPER HIGH RESOLUTION POWDERDIFFRACTOMETER IN J-PARC
Shuki Toriia, Yasuo Kobayashia, Junichi Suzukia, Hidenori Sagehashia, Minoru Nagaia,
Kenichi Oikawab, Kazuhiro Moric, Masao Yonemurad, Toru Ishigakid and Takashi
KamiyamaaaHigh Energy Accelerator Research Organization; Oho Tsukuba, Ibaraki 305-0801, Japanb

Japan Atomic Energy Agency; Tokai-mura, Naka-gun, Ibaraki 319-1195, Japanc

Kyoto University Research Reactor Institute; Kumatori-cho, Sennan-gun, Osaka 590-0494, Japand

Ibaraki University; Nakanarusawa-cho, Hitachi, Ibaraki 316-8511, Japan

Neutron Science Division of High Energy Accelerator Research Organization (KEK) isconstructing a Super High Resolution Powder Diffractometer (SHRPD) at a Materials andLife Science Experimental Facility (MLF) in Japan Proton Accelerator Research Complex(J-PARC). SHRPD is designed to have the world best resolution with Δd/d = 0.03% in 0.5 <d [Å] < 4 and covers 4 < d [Å] < 45 with gradually changing resolution. The combination of
the high quality data from SHRPD and their high-precision analysis gives us information ontiny structural changes that have been overlooked previously. SHRPD is located at 100 mfrom a thin side of a decoupled poisoned moderator, which has been developed to produce ahigh-resolution & good S/N data to achieve the 0.03 % resolution within 100 m flight path.
SHRPD has a 32 m curved guide and 50 m straight guide section between the instrument andthe moderator. A beam line building with 50 m length and an annex experimental hall with
7 m (H) x 10 m (W) x 13 m (L) for the SHRPD instrument are under construction in the eastside of MLF experimental hall. The first beam is scheduled to be delivered on May 2008.

P05-014

SHORT-RANGE ORDER PARAMETERS OF AsGeSe GLASSES
A.H. Moharram, M. A. Hefni and A.M. Abdel-Baset
Physics Department, Assiut University, Assiut, Egypt

Short range order (SRO) parameters of the bulk AsxGe40-xSe60 (with x = 0, 10 & 20 at.%)alloys have been determined using the x-ray Cu(Kα) radiation in the wave vector interval
0.28≤ K ≤ 6.5

Å-1. The radial distribution functions, RDF (r ) , have been obtained either byMonte-Carlo simulation or by Fourier transformation of the experimental data (conventional
method). The Monte Carlo method used to generate the numerical radial density
function, g (r ) , and randomly modified until the corresponding interference structure factor

I (K ) fit with the experimental data for all the investigated glasses. Gaussian analyses of thefirst four peaks in the total correlation function shows that Ge2(Se1/2)6 and Ge2(Se1/2)4
molecular units are the basic structural units for the binary and ternary alloys, respectively.
Insignificant structural changes have occurred as a result of replacing Ge atoms by As atoms
in the ternary glasses.

P05-015

STRUCTURAL AND SPECTROSCOPIC STUDIES OF CATIONDISORDER IN SOME Bi CONTAINING PYROCHLORES
Qingdi Zhou, Brendan J. Kennedy
Centre for Structural Biology and Structural Chemistry and Centre for Heavy Metals Research, Schoolof Chemistry, The University of Sydney, Sydney, NSW, 2006, Australia

Metal oxides displaying the pyrochlore type structure have been extensively studied asthey possess important electronic and magnetic properties. These properties are strongly
dependent on the nature and bonding of the B-site cations as well as disorder of A-site cations
from the ideal position. To be better understanding the A-site disorder in pyrochlore oxide, anumber of bismuth or lead containing pyrochlores based on Bi2CrNbO7 and Pb2TiNbO6.5
together with the A-site substituted (Bi1-xYx)2(Z1-xNbx)2O7-δ (Y = Pb, Na, K; Z = Cr, Ti) oxides
have been investigated using room-temperature powder neutron and synchrotron X-ray
diffraction methods. Also bismuth and lead L-edge X-ray absorption fine structure (XAFS)
experiments were performed in the solid state at low temperature (10 K) to investigate thelocal structure of the A-site cations. All samples exhibited an A2B2O7 pyrochlore like cubic
structure. Precise local structures for the Bi and Pb cations were obtained from single- andmultiple-scattering fits to the XAFS data.

P05-016

APPLICATION OF LARGE RADIUS IMAGING PLATE CAMERA FORSYNCHROTRON POWDER X-RAY DIFFRACTION TO STRUCTURAL
PHASE TRANSITION STUDIES
Masahiko Tanakaa and Yoshio Katsuyaba

BL15XU /SPring8, National Institute for Materials Science, Kouto, Sayo, Hyogo, Japan; bSPring8

Service Co. Ltd. Kouto, Sayo, Hyogo, JapanA newly developed large radius imaging plate (IP) camera system for the diffractometerof BL15XU, which is an undulator beamline of synchrotron facility, SPring-8, was applied for
powder diffraction studies altering sample condition.
We have developed a new large radius imaging plate camera system for high angularresolution and high throughput synchrotron X-ray powder diffraction. The new IP camera
system consists of a cylindrical shape IP cassette installed on the 2-theta arm of thediffractometer of BL15XU. Powder diffraction data were recorded on an IP by multiple
exposures changing 2-theta setting angles and separately collected diffraction data can beprovided for various powder crystal-structure analysis methods after data processing such asdata format conversion, connection and correction. The sample-to-IP distance of this camera
was designed to be 954.9mm and the large sample-to-IP distance brings high angularresolution. The angular resolution of this IP camera was evaluated by the FWHM of NBS-Si
111 peak and the observed FWHM value was smaller than that of a powder diffractometerwith Ge(111) analyzer at a bending magnet beamline of 2nd generation synchrotron. An
exposure time was less than 120 seconds for most samples, thus a total measurement time forone powder diffraction pattern was less than 20 minutes. This new system has achieved
twenty-times faster powder diffraction improving the high resolution of current synchrotron
powder diffractometer. The high angular resolution and high throughput realized by this
newly developed IP camera is suitable for diffraction experiment altering the sample
conditions diversely, such as the detailed observation of structural phase transition and thedetermination of thermal expansion coefficient. We will demonstrate the application
experiments of this camera to such experiments of inorganic crystal powder samples.

P05-017

MORPHOTROPIC PHASE BOUNDARY IN (1-x)BiFeO3-xPbTiO3 :PHASE COEXISTENCE REGION AND UNUSUALLY LARGETETRAGONALITY
Shuvrajyoti Bhattacharjee, Saurabh Tripathi and Dhananjai Pandey
School of Materials Science and Technology, Institute of Technology, Banaras Hindu University
Varanasi – 221005, India.

Multiferroics are promising materials for technological exploitation in actuator, sensor
and data storage devices. Perovskite BiFeO3 (BF), in bulk form, is ferroelectric,
antiferromagnetic and ferroelastic multiferroic material with antiferromagnetic (TN ~ 643 K),
ferroelectric (TC ~ 1103 K), and structural ordering temperatures well above room
temperature. It shows weak magnetism at room temperature due to canted spin arrangements
in G-type antiferromagnetic structure (with an incommensurate spiral magnetic ordering). It
has a rhombohedrally distorted perovskite structure in the R3c space group with a-a-a- tilt
system in which the neighbouring oxygen octahedra of the elementary perovskite cells arerotated anti-clockwise about the [111] direction due to a ferroelastic transition involving R(q=1/2 1/2 1/2) point phonon. BiFeO3 forms a continuous solid solution with PbTiO3 (PT) andshows a morphotropic phase boundary (MPB) similar to the MPBs in the well known
Pb(ZrxTi1-x)O3 (PZT) and (1-x)Pb(Mg1/3Nb2/3)O3-xPbTiO3 (PMN-xPT) ceramics. There isconsiderable controversy about the location and width of the MPB in the(1-x)BiFeO3-xPbTiO3 (BF-xPT) system. For example, the tetragonal phase is reported to bestable upto compositions (xT) in the range 0.3<xT≤0.4. In the MPB region, the tetragonal
and rhombohedral phases coexist over a composition range xR<xMPB<xT, where xR marks theonset of the stability of single phase rhombohedral region. The width (xT- xR) of the MPB
region is still unsettled, as values as small as ~0.06 and as high as 0.10 have been reported
in the literature. The existing controversy about the stability field of the room temperature
tetragonal structure of multiferroic BF-xPT and width of the morphotropic phase boundary
are settled using powder x-ray diffraction data. It is shown that BF-xPT shows pure tetragonal
structure upto xT = 0.31 and rhombohedral structure for xR ≤ 0.27. In the intermediate
composition range (0.27<xMPB <0.31), the two phases are found to coexist. The composition
width,
Δx ~ 0.03, for the MPB observed by us is the narrowest reported so far in theliterature for this system. We have carried out Rietveld refinement of the pure tetragonalcomposition ( x = 0.31) closest to the MPB showing the highest c/a ratio of 1.18739(2).
Results of Rietveld refinement of the powder x-ray diffraction data for BF-0.31PT provide
some structural insight into the unusually large tetragonality of this composition.

P05-018

DISORDER OF Pb ATOM IN CUBIC PHASE OF PEROVSKITE-TYPE
SOLID SOLUTIONS PZT AND PZN-PT
Yoshihiro Terado,a Chikako Moriyoshi,a Yoshihiro Kuroiwa,a,d Yasuhisa Yamamurab and
Makoto IwatacaDepartment of Physical Science, Hiroshima University, Kagamiyama, Higashi-Hiroshima 739-8526,

Japan; bDepartment of Chemistry, University of Tukuba, Tennodai, Tsukuba 305-8571, Japan;c

Department of Engineering Physics, Electronics and Mechanics, Nagoya Institute of Technology,

Showa-ku, Nagoya 466-8555, Japan; dCREST, Japan Science and Technology Agency, Honmachi,
Kawaguchi 332-0012, Japan

Ferroelectric properties of perovskite-type oxides with the chemical formula ABO3 areenormously influenced by substituting the other atoms for the A and/or B atoms. A lot ofpromising materials have been discovered by taking advantages of this substitution effects.
Among them, Pb-based perovskite-type solid solutions PbZr1-xTixO3 (PZT) are well known as
piezoelectric ceramics for the industrial applications due to their high electromechanicalcoupling constant and piezoelectric constant. All PZT do not show the high piezoelectricperformance. A PZT with a morphotropic phase boundary (MPB) composition possesses thehigh piezoelectric properties. In (1-x)Pb(Zn1/3Nb2/3)O3–xPbTiO3 (PZN–PT) and(1-x)Pb(Mg1/3Nb2/3)O3–xPbTiO3 (PMN–PT) systems, the prominent properties are also
reported around their MPB compositions. Hence, it is essential to understand the formation
mechanism of MPB for designing new piezoelectric ceramics nowadays.
The aim of the present study is to investigate the relationship between the crystal
structure of the Pb-based perovskite-type solid solutions in the cubic phase and theappearance of MPB that separates the ferroelectric phase by the vertical phase boundary.
High-energy synchrotron-radiation powder-diffraction experiments for PZT (0 ≤ x ≤ 1, MPB
at x ~ 0.5) and PZN–PT (0 ≤ x ≤ 0.3, MPB at x ~ 0.1) in the cubic phase were performed at
BL02B2 in SPring-8.
Thus far, every crystal structure of the paraelectric phase has generally been considered
to be isomorphous to the classical perovskite with a cubic symmetry, where Pb and B-site
atoms are settled at the cubic corner and body center, respectively, and O atoms at the facecenters. Our precise Rietveld analyses for PZT and PZN-PT with various compositions haveshowed clear evidence that the Pb atom is disordered around the cubic corner site and thethermal motions significantly change near the MPB composition, while no anomaly on thethermal parameter is revealed for the B-site atoms. Hence, we considered that the appearanceof MPB is strongly related to the changes in local environment around the Pb atom caused by
the B-site substitution.

P05-019

X-RAY STRESS ANALYSIS FOR FIBER TEXTURES BASED ON
SYMMETRY IN RECIPROCAL LATTICE SPACE
Ryouichi Yokoyama, and Jimpei Harada
Rigaku Corporation, Tokyo, Japan

A technique to derive analytical formulae is shown in obtaining residual stress ofpoly-crystalline materials with fiber textures from the XRD measurement of a strain
component. The relation between the strain measured by XRD, <εL33>, and stress, σkl, in a
specimen for Reuss model is given by<εL33> = ω3iω3j <SPijkl> σkl
where <SPijkl> is the elastic compliance constants defined in Specimen coordinate andω3iω3j the transformation matrices from Specimen coordinate to Laboratory coordinate and thesuperscripts L and P represent the Laboratory and Specimen coordinates, respectively.
The key point is how to calculate average elastic compliance constants <SPijkl> for
specimen with fiber texture in terms of the well known elastic compliance constants definedfor a constituent single crystallite. For such calculation it is very advantageous to take into
account symmetry, Laue symmetry, of the intensity distribution in reciprocal lattice space, forthe constituent micro crystallite in specimen. By taking up a stress state of σ13=σ23=σ33=0,
which is so-called non-equi-biaxial state, for the [111] cubic fiber texture as an example,
relations between strain measured and stress are given for both Reuss and Voigt models.
When this technique is applied to the equi-biaxial state, that is, σ11=σ22=σ in addition to
the above stress state, the resultant equation for Reuss model is in agreement with that for
Voigt model, indicating the approval of the present derivation.

P05-020

GENERALIZED METHOD OF STRUCTURE ANALYSIS FOR MICROIMPERFECT CRYSTALS USING SR.
Ken-ichiro Yamamoto,a Yoshio Nogami,a Naoshi Ikeda,a Takayoshi Ito,b Toru Matsuura,cTaku Tsuneta,c Satoshi TandacaDepartment of Physics, Okayama University, Japan; bJapan Synchrotron Radiation ResearchInstitute SPring-8, Japan; b Department of Applied Physics, Hokkaido University, Japan.

For many years, to determine the atomic coordinate for imperfect crystals was particulardifficult. For perfect single crystals, one can use well-defined structure analysis method with
Direct method, least square method and the UB matrix obtained by the k-space positions of
Bragg reflections. On the other hand, one can use powder crystal method using perfectpowder crystals without preferred orientation.
Recently, S. Tanda et al. found that the instability against deformation of thin whisker
crystal of quasi one-dimensional conductor NbSe3 results in several new crystal forms withfolded structures named topological crystals[1]. Surprisingly, the new crystal forms areseamless ring (cylinder, tube), seamless Möbius strip and seamless figure of eight strip, all
few tens of micrometers.
Determination of atomic arrangement in the topological crystal was also very difficult
owing to the curved shape. In other words, the orientation of each crystallite composing a
topological crystal has positional dependence reflecting its shape. Thereby, we abandoned
single crystal method applicable only to a perfect crystal with constant crystal orientation. On
the other hand, powder crystal method also faced the difficulty of strong positional variationof the crystal orientation depending the curved shape. If we divide or crash a topologicalcrystal to average its crystal orientation and to obtain good powder crystal, we may lose
important structural information originated from its bound and twisted shape.
Bearing this difficulty in our mind, we determined to develop new camera and analysis
method to solve the structure of the topological crystal without any sample treatment. For the
suppression of preferred orientation, we get some hint from traditional Gandolfi camera anddeveloped new two-axis sample rotator. The original Gandolfi camera with the two-axis
rotator was used in the mineralogy for qualitative analysis of constituting elements. However,their rotations were not independent nor incommensurate, because of the geared transmission
between the two axis rotation.
Reference:[1] S. Tanda and T. Tsuneta et al. Nature 417 (2002) 397.

P05-021

SYNTHESIS, REACTIVITY AND 3-D STRUCTURAL DETERMINATIONBY POWDER DIFFRACTION ON MOLYBDOPTERIN COMPLEX
Jey Jau Lee*a, Hwo-Shuenn Sheu a ,Keng S. Liang a , Baidyanath Ghoshb and Parag
Sinchan RoybaNational Synchrotron Radiation Research Center Hsinchu 30076, Taiwan R.O.C. b. Department ofChemistry, University of North Bengal, Dist.- Darjeeling – 734013, India.

The biological function of Molybdenum has been known to be contained in more than
30 distinct enzymes. The molybdenum-cofactor (Mo-co) consists of a mononuclear
molybdenum ion coordinated by one or two molybdopterin ligands. Crystallographic results
are very rare because of the crystal are very hard to grow up. The few results havedemonstrated that the molybdopterin ligands are tricyclic and nonplanar, and that they
coordinate the metal through their dithiolene sulfurs.
The molybdopterin ligand may participate in the various electron transfer reactions
associated with the catalytic mechanism of these proteins, as suggested by both oxidation
state-dependent changes in the metal coordination environment and the molybdopterin
structure, and by the interaction of the molybdopterin with other redox groups within
Mo-co-containing enzymes. In here the 2-pivaloylamino-6-acetonyl- isoxanthopterin (1, H2L)
has been reacted with Na2MoO4 2H2O under suitable conditions in presence of cysteine and
Ph4PBr for synthesizing the new compound (Ph4P)2[MoIV(L)(cys)2].0.5CH3OH. Synchrotron
powder diffraction studies throw light on its structural aspect. Here we report the 3-D
structure determination of bio-mimic molybdenum coordination compounds from synchrotron
powder diffraction data. The asymmetric unit contains more than 400 atoms. The synthesis,
reactivity and structure determination from synchrotron radiation powder diffraction will beshown and discussed.

P05-022

SOLVING ZEOLITE STRUCTURES FROM POWDER DATA USINGDENSITY BUILDING FUNCTIONS AND HISTOGRAM MATCHING
Chris Gilmorea and Douglas Dorsetb
a

WESTCHEM, Department of Chemistry, Unversity of Glasgow, Glasgow G12 8QQ, UKbAdvanced Characterization, ExxonMobil Research and Engineering Co.,1545 Route 22 East,

Annandale, New Jersey 08801, USA.

Recently we have applied techniques that use density building functions and density
histogram matching methods coupled with entropy maximisation and likelihood analysis tosolve a number of structures ab initio using electron diffraction data in 2- and 3-dimensions.
The same methodology can be used with powder diffraction:
1. A low resolution structure is generated using non-overlapped low resolution
structure factors combined with the origin defining rules of direct methods [1].
2. New reflections are given permuted phase angles (and intensities if overlapped)
and analysed using density building functions [2].
3. The optimal phase sets are subjected to entropy maximisation [3].
4. Likelihood and density histograms are used to select the optimal phase set.
Applications to a number of varied zeolite systems will be presented.
Reference:[1] Rogers, D. (1980) Theory and Practice of Direct Methods in Crystallography edited by M.F.C. Ladd &R.A. Palmer pp. 23-92. New York: Plenum Press.
[2] Gilmore, C.J., Bricogne, G & Bannister, C. (1990). Acta Cryst. A46, 297-308.
[3] Bricogne, G & Gilmore, C.J. (1990). Acta Cryst. A46, 284-297.

P05-023

BIO-MEMBRANE STRUCTURE PROBED BY THE LAMELLAR X-RAY
DIFFRACTION AND THE SMALL ANGLE X-RAY SCATTERING AT
NSRRC
Ming-Tao Lee, Yu-Shan Huang, U-Ser Jeng, Ying-Huang Lai, and Ya-Sen Sun
National Synchrotron Radiation Research Center, Hsinchu, Taiwan, 300, R.O.C.

The bio-membrane structure has long been an interesting issue in life science. Various
techniques, including X-ray diffraction, small-angle scattering and nuclear magnetic
resonance (NMR), have often been introduced in revealing bio-membrane structures undervarious humilities and temperatures as well as interactions with proteins. In this study, thelamellar X-ray diffraction (LXD) and small angle X-ray scattering (SAXS) are used todetermine the membrane structures under various environments. Temperature- and humilitydependent LXD experiments for a multilamellar membrane on a plane substrate wereconducted with 12keV photons of the BL13A beamline at the National Synchrotron Radiation
Research Center (NSRRC). The electron density profile and thickness of membrane are
extracted from the data fitting. Furthermore, temperature-dependent SAXS experiments forunilamellar vesicles in an aqueous solution were measured with 10.5keV photon of the
BL17B3 beamline, NSRRC. Combining model fitting and SAXS data, the membranethickness of vesicles in the solution has been determined.

P05-024

ANOMALOUS X-RAY SCATTERING AND ABSORPTIONSPECTROSCOPY INVESTIGATE THE MORPHOLOGY OF FePt
MONOLAYER NANOPARTICLE ON SURFACE MODIFIEDSUBSTRATES WITH AU OVERLAYER
Tzu-Wen Huang,a,b, Kuan-Li Yu,c, Yen-Fa Liao,a and Chih-Hao Leeaa

Department of Engineering and System Science, National Tsing Hua University, Hsinchu, Taiwan;bInstitute of Physics, Academia Sinica, Taipei, Taiwan; cNational Synchrotron Radiation ResearchCenter, Hsinchu, Taiwan.

The anomalous grazing incidence small angle scattering was used to verify the intact of
FePt nanoparticles under the Au overlayer during the anneal temperature at 800 C. The
structural stability of self-assembled FePt monolayer nanoparticles on functional substratewith the Au overlayer during the annealing were studied. To deposit a monolayer of particles
under control, the functional substrates such as polyethylenimine (PEI) or[3-(2-aminoethlyamino)ropyl] trimethoxysilane (APTS) modified silicon wafers were used tocapture the FePt nanoparticles coated with oleic acids. With the X-ray diffraction, anomalous
X-ray absorption spectroscopy and the anomalous grazing incidence small angle x-ray
scattering techniques, the FePt nanoparticles monolayer were found to be free fromcoalescence and convert into ordered alloy under the annealing process after 5-10 nm of Au
overlayer deposited on the top of FePt nanoparticles. The result indicates that the particle size
4.5±0.5 nm is typically unchanged, but the distance between particles is reduced from 7.5±1.5
nm to 5.5±1.1 nm after annealing. The results suggest that the 5 nm Au coverlayer is aneffective diffusing barrier layer to prevent the FePt nanoparticles from sintering during theannealing process. The ordered FePt(001) diffraction peak was obscured under the strong Au
background, but its spectrum of diffraction anomalous X-ray absorption fine structure at
FePt(111) shows an order FePt structure was formed.

P05-025

SPINODAL CRYSTALLIZATION KINETICS ON SUPERCOOLEDLIQUID OF POLY(TRIMETHYLENE TEREPHTHALATE)
Wei-Tsung Chuanga, Hwo-Shuenn Sheua,U-Ser Jenga, Po-Da HongbaNational Synchrotron Radiation Research Center, Hsinchu,300 Taiwan.

b

Department of Polymer Engineering, National Taiwan University of Science and Technology, Taipei

106, Taiwan

Polytrimethylene terephthalate (PTT) is a promising material for engineering plastic andtextile fiber, and in particular it combines many advantages of nylons and other polyesters.
Resently, we found that crystallization of supercooling liquid strongly influences process of
PTT. However, crystallization from supercooling liquid, which is the metastable state, is very
poor understood in polymeric crystallization. We have systematically investigated the
crystallization kinetics on the supercooled liquid of poly(trimethylene terephthalate) using
small-angle X-ray scattering (SAXS), wide-angle X-ray scattering (WAXS), and small-angle
light scattering (SALS) measurements. The superstructure of PTT crystallization fromsupercooling liquid is composed of the few adjacent chains come together with parallelorientation to form a fringed-micelle /or bundle-like crystallite probed by atomic force
microscopy (AFM) and transmission electron microscopy (TEM). However, in the early stageof PTT crystallization, we find that the logarithm of SAXS intensity was increased linearly,
corresponding to spinodal kinetics proposed by Cahn. This phenomenon indicates that theprecursory mesophase induce density fluctuations by spinodal decomposition before
fringed-micelle crystallites. This mechanism is different from common crystallization
associated with nucleation and growth.
.

P05-026

AN INSTRUMENT FOR TIME RESOLVED AND ANOMALOUS
SIMULTANEOUS SMALL AND WIDE ANGLE X-RAY SCATTERING(SWAXS) AT THE NSRRC
Chiu-Hun Su,a Ying-Huang Lai,a Ya-Sen Sun,a U-Ser Jeng,a,* Jhih-Min Lin,b Tsang-Lang
Lin,b Yu-Shan Huang,a Hwo-Sheunn Sheu,a Wei-Tsung Chuang,a Chia-Hung Hsu,a Ming-Tao
Lee,a Keng S. LiangaaNational Synchrotron Radiation Research Center, Hsinch 30049 Taiwan. bDepartment of Engineeringand System Science, National Tsing Hua University, Hsinchu 30013, Taiwan.

A SWAXS (small- and wide-angle X-ray scattering) instrument was recently installed at
the wiggler beamline BL17B3 of the National Synchrotron Radiation Research Center(NSRRC), Taiwan. The instrument which is designed for studies of static and dynamic
nanostructures and correlations between the nano (or meso) structure (SAXS) and crystalline
structure (WAXS) provides a flux of 1010 - 1011 photon/s at the sample at energies between 5
and 14 keV. With a SAXS area detector (MarCCD165 or Gabriel-type gas detector) and a
WAXS linear detector connected to two data acquisition systems operated in master-slave
mode the instrument allows one to perform synchronized SAXS/WAXS for time-resolved
measurements. Data reduction algorithms have been developed for rapid processing of thelarge SWAXS data sets collected during time-resolved measurements. The performance of the
instrument is illustrated by examples taken from different classes of ongoing projects: (1)time-resolved SAXS/WAXS/differential scanning calorimetry (DSC) with a time resolution of
60s on a semi-crystalline syndiotactic polystyrene sample, (2) anomalous SAXS/WAXS
measurements on a nanoparticulate Pt-Ru catalyst and (3) grazing-incidence SAXS of amonolayer of oriented semiconductor quantum wires and humidity-controlled ordering of
Alamethicin peptides embedded in an oriented lipid membrane.

Fig. 1: Scanning electron microscope (SEM) image of the oriented GaSb quantum wires (a). GISAXS pattern ofthe oriented quantum wires recorded with the area detector (b).

P05-027

SOLUTION SAXS AND NMR ON DOMAIN ORIENTATION AND
BINDING OF THE COMPONENTS OF THE HUMAN BCKD COMPLEX
Chi-Fon Chang,a,* Yu-Shan Huang,b,* U-Ser Jengba

Institute of Biomedical Sciences, Academic Sinica, Taipei, 11529, Taiwan, bNational Synchrotron

Radiation Research Center, Hsinch 30049 Taiwan.

The mammalian mitochondrial branched-chain-α-ketoacid dehydrogenase (BCKD)
complex, containing E1, E2, and E3 domains, catalyzes the oxidative decarboxylation of
branched-chain-α-ketoacids derived from leucine, isoleucine, and valine, hence, gives rise tobranched-chain acyl-CoAs. The transacylase subunit (E2) of BCKD complex carries three
independently folded domains linked together by flexible loops: the hbLBD (a.a. 1-84),
hbSBD (a.a. 104-152), and di-domain (hbDD) comprising residues 1–168 of E2. With
multidimensional heteronuclear NMR techniques, the structures and dynamics of the threetruncated fragments were determined, respectively. For the quaternary structure, solution
small angle X-ray scattering (SAXS) result reveals a linear-like arrangement of the
sub-complex of hbLBD linked with hbSBD (DD) by the flexible chains, based on a rigid bodyrefinement of the two individual structures of LBD and SBD determined by NMR.
Furthermore, from the changes of the SAXS profile of the E1 component of BCKD, upon thebinding of the DD sub-complex, most likely, the DD sub-complex keeps a free LBD end after
the binding to the E1 domain.

SBD
Intensity

LBD

Q (Å-1)
Fig. 1: A quaternary model and the protein envelope deduced from the SAXS data for the sub-complex DD(LBS+SBD) of BCKD, using rigid body refinement with the PDB data of each component.

P05-028

EXPERIMENTAL ELECTRON DENSITIES AND MOLECULAR
INTERACTIONS: INTER-MOLECULAR HYDROGEN BONDING.
Azadeh Matin, Thanh Ha Nguyen, Jane Hanrahan and David Hibbs
Faculty of Pharmacy, University of Sydney, Sydney, Australia

The successful practice of materials and medicinal chemistry is crucially dependent
upon an understanding of the principles of intermolecular interactions and becomes ofparamount importance when investigating the mechanisms of molecular recognition.
The solid state offers the opportunity to study the structure of co-crystallized complexes
in detail; and if high-resolution, low-temperature X-ray data can be obtained, then quantitative
aspects of electrostatic interactions and hydrogen bonding can be analyzed in even greater
detail using experimental charge density methods.
To this end, we are investigating the design and synthesis of co-crystal systems thatmimic biological macromolecular host-guest complexes, with a view to carrying out suchcharge density experiments. The syntheses of receptor mimics have been completed, and theco-crystallization of the receptor mimic with dicarboxylic acid (glutaric and adipic acid)followed by high-resolution X-ray studies has been accomplished (Figure 1).

Figure 1:Intermolecular interaction in the receptor complex
The combination of theoretical and experimental data on hydrogen bonding provides aunique insight into the nature of weak intermolecular interactions.

P05-029

EXPERIMENTAL ELECTRON DENSITIES AND MOLECULAR
INTERACTIONS: INTER-MOLECULAR Π-STACKINGINTERACTIONS.
Thanh Ha Nguyen and David Hibbs
Faculty of Pharmacy, University of Sydney, Sydney, Australia

π-π interactions in aromatic systems have been studied extensively in the past two
decades by many theoretical methods as they play an important role in chemistry and biology.
Despite the many reviews that deal with intermolecular interactions in π-stacked systems,
there are still relatively few practical applications of these ideas.
The topological analysis of the electron density deduced from theoretical calculations asdevised by R. F. W. Bader is well documented and has shown to be a useful tool in obtaining
valuable information about chemical bonding and the properties of atoms in molecules. Thesestudies have recently been extended to experimental electron densities obtained by X-ray
diffraction.
Currently, we have investigated the crystal electron density of π-systems on the basis of
the collected X-ray diffraction data and from quantum chemical calculations (Figure 1). The
combination of theoretical and experimental data for these systems provides a unique insight
into the nature of aromatic π-π stacking.

Figure 1:π-π interactions in an aromatic complex

P05-030

Yb-DOPING EFFECT AND TEMPERATURE DEPENDENCE IN CoSb3
SKUTTERUDITE STRUCTURE
Atsuko Ohno,a Satoshi Sasaki,a Eiji Nishibori,b Shinobu Aoyagi,b Makoto Sakatab and Bo
Brummerstedt Iversenc
aMaterials and Structures Laboratory, Tokyo Institute of Technology, Yokohama, 206-8503, Japan;b

Department of Applied Physics, Nagoya University, Nagoya 464-8603, Japan;c

Department of Chemistry, University of Aarhus, Aarhus, 8000, Denmark

Metal-doped CoSb3 skutterudite is known as a good candidate for thermoelectricmaterials with high-electrical and low-thermal conductivities. A rattling effect of the doped
atoms in the cages can reduce the lattice thermal conductivity. It is important to study how the
doped Yb atom affects the host framework of the skutterudite structure. By using thehigh-resolution powder diffraction data, we have analyzed the crystal structure of Yb-doped
CoSb3 in comparison with non-doped one.
Synchrotron X-ray powder diffraction experiments were carried out at the beamline
BL02B2 of the SPring-8. The wavelength used in this study was λ = 0.43081 Å. The
diffraction data were collected at an interval of 0.01º step within the 2θ range from 3º to 74º,corresponding to the d spacing up to 0.36 Å. Rietveld refinements were carried out with
software named as Synchrotron-Powder (SP). The structural parameters of Yb-doped CoSb3
were determined within temperature ranges from T = 90 to 700 K. The structural parametersof non-doped CoSb3 were also determined within temperature ranges from T = 10 to 300 K.
Lattice constants for Yb-doped and non-doped CoSb3 are a = 9.04095(1) Å and 9.03246(1) Åat room temperature, respectively. The lattice constants increase as a function of temperaturefor both crystals. Yb-doped skutterudite has a lattice constant change of 0.01510 Å within thetemperature range from T = 90 to 300 K. On the other hand, the change for non-doped
skutterudite is 0.01377 Å within the temperature range from T = 80 to 300 K. In CoSb3
skutterudite structure, there are three types of crystallographically different bond, which are a
Co-Sb and two Sb-Sb bonds. The interatomic distances for Yb-doped and non-doped CoSb3
were calculated from the structure parameters finally refined. The presentation will discuss
the rattling and doping effects in the structural aspects such as the change of inter-atomic
distances in the cages and host framework.

P05-031

SITE PREFERENCE AND DOPING EFFECT IN(Hg,Pb)(Ba,Sr)2Ca2Cu3O8+δ SUPERCONDUCTORS
Satoshi Sasakia and Kouji YamawakiaaMaterials and Structures Laboratory, Tokyo Institute of Technology, Yokohama, 226-8503, Japan

Hg-1223 superconductor has the highest critical temperature of Tc = 135 K for samples
synthesized at an atmospheric pressure, which is a layered perovskite having a structural unit
sequence of -HgO-BaO-CuO-Ca- along the c-axis. The substitution of mercury by lead canenhance the stability of the Hg-1223 phase. The doping effect into the mercury layers is
deeply related to an interstitial oxygen defect and cation substitution. In order to synthesize
high-quality superconductors, the substitution of barium by strontium is one of the mostimportant factors to improve such properties as the hole doping of CuO2 planes.
Single crystals with various strontium contents were grown at T = 1130 K by theencapsulation method. EDX and SQUID experiments were carried out to measure thechemical composition and magnetic property, respectively. The single-crystal intensity
measurements were first made using a conventional Rigaku AFC-5 four-circle diffractometerwith Mo Kα radiation. The integrated intensity data were collected up to 2θ = 110° in the
ω-2θ scan mode at a scan speed of 1°/min. The absorption correction was made by the
grid-integration method for the arbitrary-shape crystal. Site-occupancy experiments were
performed with the synchrotron radiation at BL-10A of the Photon Factory. A vertical-typefour-circle diffractometer was used with wavelengths of λ = 1.3906 and 1.0191 Å, which is
0.01 Å longer than Cu K and Hg LIII absorption edges, respectively. Atomic coordinates andanisotropic temperature factors were first refined with the Mo Ka data. Then, site-occupancy
parameters were determined with the anomalous scattering effect. Final R factors range from
6.4 to 6.7 % in the Mo Kα refinements.
The cation distribution among mercury, lead and copper in the Hg sites was determined
the two-wavelengths anomalous dispersion (TWAD) method using the diffraction data at Cu
K and Hg LIII edges. The minimum residual factors in the analyses indicated that no copper
exists in the Hg sites for all samples. The occupancy parameters for the Ba sites were also
determined from the Mo Kα diffraction data and compared with the chemical composition ofstarting materials. The presentation will discuss the site preference and structural change in
the aspects of strontium content, superconductivity transition temperature, concentration ofholes and so on.

P05-032

CLOSE CL···CL CONTACT: IS IT ATTRACTIVE OR REPULSIVE?
Daisuke Hashizume
Molecular Characterization Team, RIKEN, Saitama 351-0198, JAPAN

Cl…Cl contact is frequently found in organic crystals. Because of their strong
directionality, the contact has been used for designing the structure of crystal andsupramolecular aggregate. The nature of the contact, however, has not been characterized
experimentally. The aim of the study is characterize the nature of the contact from electron
density distribution, which is obtainable from X-ray diffraction data.
In the crystal of 3,4-dichlorophenol, there are different directional Cl…Cl contacts.
Since the different directional contacts can be compared in the same crystal, the crystal issuitable to examine the nature of the contacts. Single crystal diffraction data were collected
at BL04B2 beam line of SPring-8. The electron density distribution was refined applying
pseudo atom models. Topological analysis for total electron density reveals that bond paths
and bond critical points are found for each of the Cl…Cl contacts. The outer shell electrons
on the Cl atoms deformed. Nevertheless, the different directionalities of the Cl…Cl contacts,
the electrons distribute similar way between Cl atoms in contacts. The outer shell electron
concentrate regions direct toward electron deficient regions.
In conclusion, the Cl…Cl contact is an interaction between electron donor and accepter
even if the directionality of the contact is different.

P05-033

THEORETICAL CALCULATION OF XMCD SPECTRA AT K-EDGE Ni
AND Fe SPINEL FERITE
Koichi Ohkuboa, Takeshi ToyodabaEarth Appraisal Co,LTD , Tokyo 101-0063, Japanb

Industrial Research Institute of Ishikawa, Kanazawa, 920-8203, Japan

Spinel ferrites are well known as materials which consist of Fe with varioustransition-metal cations in A (tetrahedral Td) and B(octahedral Oh) sites of the crystal
structure. The physical property of the ferrites depends on the site occupancy of such ions.
Therefore, specific information on the site as electronic and magnetic properties of Ni ferrite
together with the other transition-metal ferrites have been examined by means of X-ray
absorption experiments along with theoretical calculations.
Theoretical XMCD (X-ray Magnetic Circular Dichroism) studies were performed tofocus the ferric ions surrounded by oxygen atoms. The XMCD spectra provided the local
information on magnetic ions within the investigated molecular systems.
In the numerical calculation based on the expansion on perturbation in electro-magnetic
fields showed a good agreement between the XMCD measurements and numericalcalculations on inverse type Ni ferrite. In this study, other effect (e.g. ligand field) is
discussed by theoretical calculation.

P05-034

ELECTRONIC STRUCTURE OF MERCURIC IODIDE USINGCOMPTON SCATTERING TECHNIQUE*M. Sharma, Gulzar Ahmed and B. L. Ahuja* Department of Physics, Arya College of Engg. and I. T., Kukas, Jaipur – 303 001
Department of Physics, Univ. College of Science, M. L. Sukhadia University, Udaipur – 313 001

In this paper, we report the experimental Compton profile of mercuric iodide using
our 20 Ci 137Cs [1] and 100 mCi 241Am [2] Compton spectrometers, at the instrumental
resolutions 0.38 a.u. and 0.55 a.u., respectively. We have also computed theoretical
Compton profile along with energy bands and density of states within the framework of
Linear Combination of Atomic Orbital (LCAO) scheme as employed in CRYSTAL03 code ofTornio group [3]. The experimental Compton profiles of both measurements have been
compared with the pseudopotential scheme within the Hartree Fock (HF) and density
functional schemes. It is observed that the density functional calculations are in better
agreement the experimental data.
Reference:
1. B.

L. Ahuja, M. Sharma and S. Mathur
Nucl. Instrum. and Meths. B244, 419 (2006).

2. B. L. Ahuja and N. L. Heda
Z. Naturforsch. A61, 364 (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, M. Llunell
CRYSTAL03 User’s Manual, University of Torino, Torino, 2003

P05-035

CHARGE DENSITY DISTRIBUTION AND BOND
CHARACTERIZATION ON COMPLEX MN(H2O)2NI(CN)4⋅3H2O
Lai-Chin Wu,a I-Jui Hsu,a Gene-Hsiang Lee,b Yu Wang.aaDepartment of Chemistry, National Taiwan University, Taipei, Taiwan, R.O.C.,b

Instrumental Center National Taiwan University Taipei, Taiwan, R.O.C.

The title compound is a bimetallic complex bridging by cyanide groups. It is crystalizedin space group Pnma with cell dimension a=12.0791(9), b=14.071(2), c=
7.308(2). The
local coordination geometry of manganese is octahedral with four nitrogen atoms of cyanidegroup in horizontal positions and two water molecules at axial positions. The nickel iscoordinated with four carbon atoms of cyanide group in a square planar geometry. However,there is an unusual short distance 2.657(1) Å between Ni and O of water in the axial directionof Ni. The MnNi(µ-CN)4 unit forms 2-D layer and the three non-coordinated water molecules
are pack between layers. Each water molecule is H-bonded to three nearest water molecules.
The contact short distances between these oxygen atoms of water molecules are 2.786(1) Å to
2.849(1) Å. In order to characterize all the chemical bonds as well as the weak interactions
such as hydrogen bonds etc., X-ray diffraction data was collected at 100K with resolution up
to 0.36 Å (sinθ/λ~1.38). The deformation density, Laplacian of the total electron density interms of multipole model is applied to investigate the bonding character. Topologicalproperties associated with bond critical points, energy density, etc. based on AIM theory will
be presented.

P05-036

CHEMICAL BONDING AND INTERMOLECULAR INTERACTIONS
OF A NICKEL(II) COMPLEX
Yu-Chun Chuanga, Yu Wanga, Gene-Hsiang Leeb, Ben-Jie Liawc, Chen-Wei Liuca

Department of Chemistry, National Taiwan University, Taipei, Taiwan, bInstrumentation Center,

National Taiwan University, cNational Dong-Hwa University

A Nickel(II) complex, bis-(di-isopropyl-diseleno-phosphato)-Nickel(II), is a squareplanar complex, where Ni ion is bonded to four Se ligand. The electron density distribution isinvestigated by single crystal x-ray diffraction at 100K using Mo Kα on a Kappa CCD
diffractometer. It crystallized in space group is P-1, the inter-set agreement index, Rint, is0.033, (total # reflections/unique reflection = 75997/11924) with the max resolution(sinθ/λ)max of 1.08 Å-1. The nickel atom is located at the inversion center. There are twodifferent Ni-Se distances: one at 2.3615(6)Å and the other at 2.3294(6)Å. Interestingly, there
is a short Se-Se contact of 3.294 Å between the neighboring molecules; which is roughly thesame as intra molecular Se---Se contact distance. Thus there is a Se square network
throughout the crystal. The aim of this study is not only looking into the chemical bonding
interactions of this Ni complex but also search for the interesting intermolecular interactions
through short contact of Se---Se interaction. The experimental electron density will be
produced with multipole model. The electron density distribution of metal ligand and Se---Se
interactions will be presented in terms of deformation density and respective Laplacian ofdensity. The topological properties associated with bond critical points will also be discussed.

P05-037

MIXED LIGAND COPPER(I) COMPLEXES OF
TRIPHENYLPHOSPHINE AND PHENYLTHAIOUREA
Ruthairat Nimthonga, Chaveng
SaithongaaPakawatchaia, Yupa Thunyasirikula andSaowanit

Department of Chemistry, Faculty of Science,Prince of Songkla University, Hatyai, Songkhla, 90112

Thailand.

Copper(I) halide complexes (CuX; X= Cl, Br, I) containing triphenylphosphine(PPh3)
and N-phenylthiourea (ptu) ligands have been synthesized and characterized by elemental
analysis, X-ray fluorescence spectrometry, Fourier transform nuclear magnetic resonancespectroscopy and Fourier transform infrared spectroscopy. The complexes obtained by theaddition of ptu ligand to a CuX-PPh3 adduct in solution. The molecular structures of[CuCl(PPh3)2(ptu)](1), [CuBr(PPh3)2(ptu)](2), [CuI(PPh3)2(ptu)](3)have been establishedby single-crystal X-ray diffraction. The complex(1) is isomorphous and isostructural with−complex(2),crystallize in triclinic system space group P 1 , Z = 2 with cell parameters a =10.5226(1), b = 11.3035(2), c = 17.1848(2) Å, α = 97.605(1), β = 103.508(1), γ = 103.605(1)°and a = 10.6236(4), b = 11.2135(4), c = 17.1481(7) Å, α = 97.957(1), β = 102.424(1), γ =102.994(1)° for complex(1) and complex (2), respectively. Complex (3), crystallizes in space−group P 1 Z = 2 with cell parameters a = 10.9505(9), b = 18.7294(15), c = 21.3731(18) Å, α
= 67.4220(10), β = 77.2150(10), γ = 73.2240(10)°. Each of these structures features a
distorted tetrahedral copper(I) center coordinated to two phosphorus atoms from two
triphenylphosphine molecules, one sulfur atom of phenylthiourea molecule and one halideatom.

P05-038

INVESTIGATION OF ELECTRON DENSITY DISTRIBUTION IN
ANATASE (TiO2) WITH- AND WITHOUT UV-IRRADIATION
Ken-ichi Ito and Hiroki Okudera
Division of Earth and Environmental Science, Graduate School of Natural Science & Techology,
Kanazawa University, Kanazawa, 920-1192 Japan

Anatase-phase TiO2 is widely recognized as an effective photocatalyst for the
degradation of organic pollutants in air and water. This photocatalytic activity is due to aformation of OH radical on the surface, and transition of electrons from valence band to
conduction band by UV irradiation is ascribed to the formation of hole and electron on thesurface. Electron density distribution in anatase, however, has not been well established.
Electron density distribution was examined by means of single crystal X-ray
diffractometry. Natural single crystal of anatase (Tisey, Norway) was spherically ground in
200 μm in diameter and used for the experiments. Trace amounts of Fe and Nb were found as
impurities. A Rigaku AFC-5S four-circle diffractometer was used (radiation: MoKα). Threesets of diffraction intensities were collected; set 1 was collected under no light, set 2 underUV (λ = 253.6 nm: 4.9 eV) plus fluorescent light, and set 3, again, under no light. Results ofFourier syntheses were compared with each other to estimate an amount of experimental
uncertainty (ρ3-1 = ρset3 - ρset1) and extract difference in electron density with- and without UV
irradiation (ρ2-1 = ρset2 - ρset1). Residual density (eÅ-3) was in the range -0.16 ~ 0.17 on ρ3-1 and-0.22 ~ 0.43 on ρ2-1 in YZ plane (x = 1/2), and -0.13 ~ 0.17 on ρ3-1 and -0.13 ~ 0.30 on ρ2-1 in
XY plane (z = 0).
Conventional difference Fourier maps commonly showed electron densities which canbe ascribed to Ti-O bonding orbitals among three data sets. On the other hand, ρ2-1 maps
showed weak concentration of positive density in the vicinity of Ti (8a) site, one is found on
the line along longer Ti-O bond and the other on <110> where there is no Ti-O bond. The
latter density may be ascribed to electron density transferred from non-conductive bonding
orbital to antibonding Ti t2g(dxy) orbital, while the former does not match antibonding Ti eg
orbital which requires higher activation energy. Change in electron configuration with- andwithout UV irradiation and mechanism of photocatalytic activity will be discussed based on
the results.

P05-039

CHARGE DENSITY STUDIES ON HETEROBIMETALLIC
PHOSPHIDO-BRIDGED Mo AND W COMPLEXES
Chi-Rung Lee,a I-Jui Hsu,b Hsiu-Mei Linc and Shin-Guang Shyuda

Department of Chemical Engineering, Minghsin University of Science and Technology, Taiwan.

b

Department of Chemistry, National Taiwan University, Taiwan.

Biotechnology, National Taiwan Ocean University, Taiwan.

dcInstitute of Bioscience andInstitute of Chemistry, Academia Sinica,

TaiwanThe heterobimetallic phosphido-bridged complexes, CpW(CO)2(μ-PPh2)Mo(CO)5 (1)with W-Mo distance 3.1723(4) Å and CpW(CO)3(μ-PPh2)Mo(CO)5 (2) with W-Mo distance
4.510(4) Å have been reported with special chemical reaction properties because of theinteraction between W and Mo. For example, complex 2 will be converted into 1 after
irradiation with UV or heating at reflux temperature. In order to realize how chemical bonds
influence the reaction properties in complex 1 and 2, the X-ray diffraction data of bothcomplexes at 100 K are collected and the experimental electron density in terms of multipole
model are used to investigate the electron density distribution and chemical bonds. All
chemical bonds will be quantified based on atoms in molecule (AIM) theory to elucidate thenature of those interactions. All interactions are verified by the location of the bond criticalpoint and its associated topological properties, such as local density, Laplacian, and energy
density at bond critical points. Moreover, the isovalue surface of Laplacian charge density
distribution and the detailed atomic graph around each atomic site will reveal the shape of thevalence-shell charge concentration and provide a reasonable interpretation of the bonding ineach atom. All extracted chemical bonding characters from experimental charge density will
be further compared with the density functional theory calculation and give out a reasonable
explanation related to the different chemical reaction properties between 1 and 2.

P05-040

EXPERIMENTAL CHARGE DENSITY STUDY ON A Fe(II) COMPLEXAT HIGH SPIN AND LOW SPIN STATES
Chou-Fu Sheu1, Che-Hsiu Shih1, Szu-Miao Chen1, Yu-Chun Chuang1, Gene-Hsiang Lee1,
Yu-Shan Huang2, Kuan-Li Yu2, Yu Wang*1
1

Department of Chemistry, National Taiwan University, Taipei 106, Taiwan

2

National Synchrotron Radiation Research Center, Hsinchu 30077, Taiwan

Charge density study, on polymorph D of a spin crossover complex, [t-Fe(abpt)2(NCS)2](abpt = 4-amino-3,5 bis(pyridine-2-yl)-1,2,4-triazole), is undertaken. It crystallizes inmonoclinic space group P21/c with two crystallographic independent mononuclear moleculesin the unit cell. Out of two unique iron sites, only one iron (Fe) undergoes a thermal spintransition from high spin (HS) to low spin (LS) state at 162 K, while the other site (Fe’)
remains in HS state in the temperature range studied. The aim of this study is to probe theelectron density distributions in HS and LS state of Fe(II) with exact same coordinationgeometry within a single sample at 100K. The electron density distributions around the twoiron sites are expected to be very different due to the distinct electronic configurations in HS(eg2)(t2g4) and LS (eg0)(t2g6) state. Two diffraction data were collected at 100 K; one with an
in-house kappa CCD using MoKα radiation and the other with synchrotron radiation using
the wavelength of 0.5 Å (25 KeV). The results in terms of multipole model from two sets ofdata are comparable. The detail of necessary correction on the CCD detector will be discussed.
The apparent difference in electron density distribution of Fe at HS and at LS will bedemonstrated in terms of deformation density and Laplacian of density. Topological properties
associated with the bond critical points will be discussed. A DFT calculated charge density
will also be presented for comparison. d-Orbital populations at HS and LS states are as
expected.

P05-083

PRELIMINARY STRUCTURAL REFINEMENTS AND A NEWSYNTHETIC ROUTE TO δ-Bi2O3-RELATED PHASES IN THE Bi-W-O,
Bi-Mo-O, Bi-Ta-O AND Bi-Nb-O SYSTEMS
Neeraj Sharmaa, Rene Macquarta and Chris D. Linga,baSchool of Chemistry, University of Sydney, Sydney, AustraliabBragg Institute, Australian Nuclear Science and Technology Organisation, Menai, Australia

The floating zone image furnace is an ideal tool to grow micrometre to millimetre sized
metal-oxide crystals. During crystal growth there is no contact with crucibles orquartz/platinum tubes, minimising the formation of impurities. The rapid cooling of the melt
produces quenching conditions, allowing synthesis of crystals that do not form with slow
cooling; e.g. crystals within the solid-solution range. Here we report the use of the floatingzone image furnace technique to grow single crystals of the δ-Bi2O3-related solid-solution
phases of nominal composition Bi8Nb2O17, Bi5.6WO11.4, Bi16Ta2O19 and Bi38Mo7O78. The
Bi5.6WO11.4 and line phase Bi38Mo7O78 single crystals were analysed with synchrotron andlaboratory based X-ray diffraction to determine metal cation positions and neutron diffraction
to determine the oxygen anion positions. The diffraction methods are also applied to the 3-D
incommensurately modulated structures of Bi8Nb2O17 and Bi16Ta2O19. There are challenges
encountered in these latter complicated structures; e.g. integration of the collected ‘6-D’ dataand subsequent refinements. Each sample studied presents different methods of approaching
the structural solutions. The ability to grow single crystals of the Bi-rich transition-metaloxides and solve these structures, highlight the potential for the exploration of phase diagramsby the use of the floating zone technique.

P05-084

INSIGHT INTO THE STABILITY OF TETRAGONAL AND
RHOMBOHEDRAL PHASES IN DOUBLE PEROVSKITES
P. J. Saines, J. Spencer and B. J. Kennedy
School of Chemistry, The University of Sydney, Sydney, New South Wales, 2006, Australia.

The precise structure adopted by double perovskites is known to have a significant
influence on the interesting and useful properties displayed by these materials such as
magnetism, ferroelectricity and colossal magneto-resistance. It is therefore important tounderstand why apparently similar perovskite systems adopt different structures. An
example of this is the significantly different structures adopted by members of the series ofdouble perovskites of the type Ba2LnB’O6 (Ln = lanthanide and B’ = Nb5+, Ta5+ or Sb5+). It
has recently been established that members of the Nb5+ series adopt I4/m tetragonal symmetry
while Sb5+ adopts R 3 rhombohedral symmetry as intermediate phases between the I2/m
monoclinic and the Fm3 m cubic phase. The cause of the difference in the intermediatephase adopted in these two similar systems is still not certain.

In order to develop an understanding of why changes to the pentavalent cation influence
the symmetry of the intermediate phase we have studied the structures of the Ba2LnTaO6
series using a combination of synchrotron X-ray and neutron powder diffraction. The majorityof oxides adopting the intermediate symmetry at room temperature exhibited the same
tetragonal intermediate phase seen in the niobates. Ba2LaTaO6 however adopts therhombohedral intermediate seen in the antimonates. This prompted us to examine the phasetransitions of other members of the tantalate and niobate series using variable temperature
X-ray diffraction. This indicated that where Ln3+ = La3+ or Pr3+ rhombohedral symmetry isadopted while in all other cases examined the intermediate symmetry was found to be
tetragonal. That some tantalates and niobates exhibit rhombohedral symmetry while others
exhibit tetragonal symmetry indicates that the factors causing the difference in symmetry
adopted are particularly subtle and that the systems are finely balanced between these two
possibilities. This paper will examine the results in these and other related compounds andattempt to explain the relative stability of the rhombohedral and tetragonal symmetries in thiscontext.

P05-085

A STUDY OF STRONTIUM, ALUMINIUM AND INDIUM TUNGSTEN
BRONZESM. S. Rahman and A. Hussain
Department of Chemistry, University of Dhaka, Dhaka – 1000, Bangladesh

The tungsten bronzes and bronze type compounds have received much attention over
the years because of their interesting physical and chemical properties such as intense colour,
electronic conductivity and chemical inertness. Tungsten bronzes, MxWO3, arenon-stoichiometric oxides where M is generally an electropositive metal in the range 0< x <1.
There are many reports available in literatures on the alkali metal tungsten bronzes but very
few reports are there on alkaline earth metal and also on aluminium group metal tungsten
bronzes.
Attempts were made to prepare SrxWO3, AlxWO3 and InxWO3 with 0 < x ≤ 0.25 at atemperature 800 0C and in ambient pressure by conventional solid-state method using
appropriate amount of M2(WO4)3, WO3 and WO2 in evacuated sealed silica tubes. However,the starting material for strontium bronzes was SrCO3 instead of SrWO4. Optical microscopic
study shows that the colour of the products becomes more intense with increasing x. In mostcases, the X-ray analysis of the samples shows a mixture of various bronze phases. A detailed
phase analysis of these systems will be presented in the conference.

P05-086

CRYSTAL STRUCTURE AND HABIT OF CaIrO3
Masahiko Sugaharaa, Akira Yoshiasaa, Takafumi Hashimotoa, Syunsuke Sakaia, Akihiko
Nakatsukab, Maki Okubec and Akira YonedadaGraduate School of Science and Technology, Kumamoto University; bFaculty of Engineering,

Yamaguchi University; cTokyo Institute of Technology; dInstitute for Study of the Earth’s Interior,
Okayama University.

The CaIrO3-type post-perovsike structure of MgSiO3 has been shown experimentallyand theoretically to occur at the temperature and pressure conditions of D’’ layer of the lowest
Earth’s mantle extend to 2700~2900 km depth. The discovery of a post-perovskite phase has
attracted considerable attention because of its potential relevance to the D’’ layer. The CaIrO3
type structure is closely related to the Earth’s lower mantle. Similar pressure-induced phasetransition to the CaIrO3-type structure has been reported in other familiar compounds
including MgGeO3, MnGeO3, Fe2O3 and Al2O3. CaIrO3 type phases of these compounds areunquenchable to ambient conditions. Detailed knowledge of the structure is, therefore,
important not only for understanding the Earth’s mantle but also for high-temperature andhigh-pressure crystal chemistry.
Single crystals of CaIrO3 were prepared via flux growth. Precise crystal structuralparameters, including the anisotropic displacement parameters, are determined based on asingle-crystal X-ray diffraction experiment. Cell dimensions: a=3.147(2), b=9.866(6),c=7.302(5) (Å). The structure is actually a three-dimensional dense structure with small
vacant spaces. The IrO6 octahedra are distorted greatly. The O-O distances for the sharedfaces and edges among polyhedra are shorter than other non-shared edge distances. These
effects are explained by Pauling’s rules and occur to decrease the repulsion between the
cations. Thermal vibration of all atoms is significantly anisotropic. The large anisotropy andamplitude of thermal displacements for Ca and Ir atoms are observed toward the b-axis whilethat for O(1) and O(2) atoms are observed toward the c-axis. Thermal vibrations of Ca and Ir
atoms are restricted toward the shared face, shared edges and shortest cation-cation directions.
Moreover, a component of thermal vibration toward the vacant space is added because the
CaIrO3 structure is highly dense structure. The single-crystal experiment shows that CaIrO3
crystal grows toward the a-axis and that it has a prism- or needle-shaped crystal habit.
Strongly preferred orientation of such prism shaped CaIrO3 type post perovskite MgSiO3
crystals may develop under the share flow in Earth’s mantle.

P05-087

SYNCHROTRON POWDER DIFFRACTION STUDY ON GAMMAAl2O3
Seiichi Matsuda, Takashi Ida, Kazuhiro Asai and Hisashi Hibino
Ceramics Research Laboratory,Nagoya Institute of Technology;Asahigaoka 10-6-29, Tajimi,
Gifu ,Japan

1,Introduction
Many studies on the structure of gamma-Al2O3 have assumed that it has a defect spinel
structure, while a tetragonal structure model has also been proposed based on neutron
diffraction and NMR experiments (Paglia et al., 2003). However, both indexing andevaluation of integrated intensity from X-ray diffraction data of gamma-Al2O3 are generally
quite difficult because of intrinsically broad width of diffraction peaks. In this study, thediffraction intensity profile of gamma-Al2O3 measured with a synchrotron powder
diffractometer has been analyzed by deconvolution and profile fitting methods to extract
maximum information about the structure from the X-ray diffraction data.
2,Experimental
Alumina samples were prepared by treatment of chemically synthesized boehmite powder at
780, 840, 900, 960, 1020, 1080, 1140, 1200, 1260 K for 8 hours. The diffraction intensity data
were collected with a synchrotron powder diffractometer (multiple-detector-system; MDS) on
the beam-line BL-4B2 at the Photon Factory in Tsukuba. Apparent asymmetric deformation ofpeak profile caused by optical aberration and spectroscopic distribution of the source X-ray
was removed by an originally developed deconvolution method.
3,Results
The observed diffraction patterns of samples treated at 780~960 K were similar to the typical
pattern reported for gamma-Al2O3. Significant narrowing and splitting of overlapped peaks
have been observed for the samples treated at temperatures higher than 960 K. The diffraction
patterns of the samples treated at 960~1200 K were almost identical to that reported asdelta-phase. The splitting of pseudo-cubic {400}-reflections is systematically enlarged onelevating the treatment temperature in the range from 1020 to 1260 K. When the tetragonal
deformation of the pseudo-cubic unit cell is assumed, the observed change in the {400} peak
profile can be explained by shift of 400 and 040 peaks to the lower angle side and 004 peak to
the higher angle side at higher treatment temperatures, which correspond to expansion of aaxis and shrinkage of c axis, respectively. The change of profile observed for the {440}reflections was also consistent with the above tendency, while the change in {311} reflections
could not be fully explained by the tetragonal deformation of a pseudo-cubic structure. Moredetailed profile analysis has been conducted aiming at evaluation of coherent domain size
along each crystallographic directions.

P05-088

STRUCTURE DETERMINATION OF HYBRID STRUCTURES FOUND
IN BaTiO3 CRYSTAL
Y. Yoshimura,a K. Sone,a H. Sumiyoshi,a T. Kondo,a A. Kojima,b K. TozakicaFaculty of Science and Engineering, Ritsumeikan University, Shiga 525-8577, Japanb

Department of Materials Science, University of Shiga Prefecture, Shiga 522-8533, Japanc

Department of Physics, Faculty of Education, Chiba University, Chiba 263-8522, JapanBaTiO3 crystal is known to have four phases: for convenience we call here α-phase (Pα),β-phase (Pβ), γ-phase (Pγ) and δ-phase (Pδ) from high to low temperatures, undergoing threephase transitions at approximately 403 K (T1), 283 K (T2) and 183 K (T3). As for the crystal
system of Pβ, we have reported very recently that the single crystals reveal a notable feature[1]: different from the commonly accepted notion, BaTiO3 changes its structure on coolingfrom the cubic to a coherent hybrid structure composed of tetragonal and monoclinic forms,
having the tetragonal ( 1 01)T lattice plane in common. In Pγ between T2 and T3, the crystal also
has a coherent hybrid structure composed of tetragonal and monoclinic forms sharing thetetragonal (101)T lattice plane in common but it is different from another coherent hybrid
structure in the room temperature β-phase [2]. In Pδ below T3, it reveals a tetragonal structurevery close to a cubic system [2].
Accordingly, we tried to analyze the crystal structure of each phase. Before the crystal
structure analyses, we examined possible crystal structure models explaining the X-ray
diffraction data fairly well. We show that the relations between the reciprocal lattices of thetetragonal and monoclinic forms of the hybrid structure play an important role to a uniquelydetermined space group and a provable crystal structure model for both forms. The details
about the analytical procedures and the results will be presented and discussed.

P05-089

DIFFRACTION AND XAFS STUDY OF AgI UNDER HIGH PRESSURE
AND HIGH TEMPERATURE
Akira Yoshiasaa, Hiroshi Arimab, Hiroshi Fukuib, Osamu Ohtakab, Maki Okubec, andYoshinori KatayamadaGraduate School of Scienc, Kumamoto University, Kumamoto 860-8555, Japan; bGraduate School of

Science, Osaka University, Toyonaka 560-0043, Japan; cMaterials and Structures Laboratory, Tokyo
Institute of Technology, Yokohama 226-850 Japan; dJapan Atomic Energy Agency , Hyogo 679-5198,
Japan

Using multi-anvil high-pressure devices and synchrotron radiation at BK11XU and
BL14B1 beam lines in Spring-8, Japan, extended x-ray absorption fine structure (EXAFS) andangular dispersive X-ray diffraction observations of AgI up to 6.0 GPa and 1000K have been
performed to investigate the phase relations, precise structure and effective potentials in various
phases. The melting curve of α-AgI has a temperature maximum at 1.0 GPa, which indicates theexistence of dense liquid phase above this pressure. The three phases of α-AgI disordered rocksalt type, and liquid meet in a triple point at 823K and 1.3 GPa. X-ray absorption near edge
structure spectra are quite sensitive to the three-dimensional atomic configuration around X-ray
absorbing atoms, they are useful for phase study under high temperature and high pressure.
α-AgI and disordered rock-salt type phase have super-ionic conduction behaviors. Ag ionsoccupy both octahedral and tetrahedral sites in the disordered phase and twenty percent of Ag
ions occupy the tetrahedral site as a maximum value at 2GPa. The transition between the rocksalt type and disordered rock salt type phases is a broad and diffuse disorder type within thesame structure. Some sudden changes are recognized near the phase transition point. EXAFS
provides the useful information about thermal vibration of local structure under pressure. In
EXAFS analysis, we have directly carried out the numerical integration of EXAFS function.
The anharmonic effective pair potentials, V(u)=au2/2+bu3/3! for I-Ag bond have been
determined under pressures. The potential parameter a for α-AgI at 1 GPa is 2.5(1) eV/A2. The
potential parameter a for rock-salt type is 1.7(1) eV/A2 at 1.0 GPa and which increases to 1.9(1)eV/A2 at 6.0 GPa. The extent of anharmonicity is larger in α-AgI than in rock salt type AgI.
Pressure influences greatly the effective pair potential of anti-bonding side and anharmonicity
decreases with increasing pressure. The phonon energies can be estimated using the potential
parameter a by calculating the dynamical matrix. Analysis of EXAFS Debye-Waller factor isuseful because the force constant can be decided directly even at high pressure and hightemperature.

P05-090

CAGE SUBSTRUCTURES AND SITE OCCUPANCIES IN CLATHRATECOMPOUNDS,La3Pd20T6 (T = Si And Ge)
Y. Matsushitaa, A. Satoa, H. Kobayashib, A. Dönnia, H. Kitazawaa, F. Izumia, Y. Nemotob, T.
Gotob, M. Kanekob, S. Sasakib, and N. KishimotoaaNational Institute for Material Science, Tsukuba, Ibaraki, Japan bNiigata University, Niigata, Japan

Ln3Pd20T6 (Ln = Lanthanoids, T = Si and Ge) system shows various kinds of interesting
unusual physics under low temperature. For example, Ce compounds show metallic
Kondo-lattice antiferromagnetic behaviour, and Ln3Pd20Ge6 (Ln = Nd, Dy and Tb) show
successive antiferromagnetic orderings. These interesting physical properties may be due tothe existence of the following specific crystallographic characters. In the system, all ofcompounds belong to C6Cr23-type structure (Fm3m). The crystal structures have two kinds ofcrystallographically independent lanthanoid sites, and the sites locate in cage substructures
formed by Pd-Pd and Pd-T like a clathrate compound. Site-occupancy information of eachsites and crystallochemical natures of these Pd-Pd and Pd-T, are also indispensable knowledge
to understand the interesting properties, because the elements forming cage substructure give
direct influence to the center lanthanoid. Our target La compounds are important compounds
to clearly show the contrast between La compounds and other lanthanoid compounds tounderstand the physical properties because La takes trivalent without any 4f electrons asvalence electrons.
The La3Pd20T6 crystals are grown by floating zone method with high purity elements.
Intensity measurements are carried out Bruker Smart-1000 CCD diffractometer (MoKα) at
room temperature. Final R1-values are 2.23 % for Si and 2.34 % for Ge, respectively. In bothcompounds, all of sites are fully occupied without any disordering behaviour. In the structures
there are five crystallographic independent sites, two lanthanum, two paradium and one T
elements. La1 is located at centre of non-polar Pd12 cluster formed by Pd1, and T is connectedto each of Pd4 square plane of the cluster as the second neighbour. On the other hand, La2 islocated in more complex cluster formed by Pd and T. The first neighbour around La2 is polar
Pd16 cluster formed by Pd1 and Pd2, and T connects to triangle plane by two Pd2 and one Pd1
as second neighbour of the cluster.

a) La1 clusterb) La2 cluster

P05-091

MODULATED STRUCTURES IN THE AMOB2O5 FAMILY FROMVARIABLE TEMPERATURE X-RAY POWDER DIFFRACTION DATA
Siegbert Schmid
School of Chemistry, The University of Sydney, Sydney NSW 2006, Australia

Non-centrosymmetric oxo pyroborates, AMOB2O5 (A = K, Rb, Cs, Tl; M = Nb, Ta),
have attracted considerable interest owing to their potential use as non-linear optical materials.
All members of the family possess a common underlying average structure. In addition most
exhibit superstructures of varying multiplicities (2, 5 and 8) along the b axis (corresponding to
the Pmn21 setting of CsNbOB2O5).
The structures of RbNbOB2O5 and RbNbOB2O5 have been refined previously using a
super space approach. While for RbNbOB2O5 the structure is incommensurately modulated,
despite the apparent value of the modulation wave vector of 2/5 b* exactly, the structure of
KNbOB2O5 refined significantly better as commensurate modulated structure and wastherefore reported as a superstructure.
Given the ambiguity in deciding whether a structure is commensurately or
incommensurately modulated using metrics alone, a variability of the magnitude of themodulation wave vector with composition (e.g. for solid solutions) or temperature is usuallytaken as a means to make an informed decision.
Variable temperature X-ray powder diffraction data were collected for both
RbNbOB2O5 and KNbOB2O5 at the Australian National Beamline Facility, Photon Factory,
Tsukuba, Japan. Diffraction patterns were collected at RT and from 150 °C to 800 °C in 25 °C
steps. The results of the analysis of these data, which supports the previously suggested
reason for the modulation, will be presented here.

P05-092

RXMS STUDY ON A MAGNETIC HELIX OF BaTiCoFe10O19
Maki Okube,a Seiji Ohsawa,a Takeshi Toyoda,b Takeharu Mori,c Satoshi SasakiaaMaterials and Structures Laboratory, Tokyo Institute of Technology, Yokohama, 226-8503;b

Industrial Research Institute of Ishikawa, Kanazawa, 920-8203, Japan;cPhoton Factory, Institute of Materials Structure Science, KEK, Tsukuba, 305-0801

Barium hexaferrite BaFe12O19 is ferrimagnetic and has the strong uniaxial magnetic
anisotropy. The M-type ferrite has a spin collinear structure, in which all the magnetic
moments in five independent iron sites are ordered parallel or antiparallel to c axis. It is
known that the substitution of Fe3+ by a pair of Ti4+ and Co2+ causes a magnetic helix
propagated along the hexagonal c axis and results the reduction of the anisotropy. Resonant
X-ray magnetic scattering (RXMS), which has the selectivity between iron and cobalt atoms,
is a useful tool to determine the structure and electronic state of the magnetic helix. Therefore,
we investigate the magnetic structure of BaTiCoFe10O19 by RXMS at the Fe K absorption
edge.
RXMS experiments were carried out at the BL-3A/6C of Photon Factory. X-rays
monochromatized by Si(111) crystals were guided into a transmitted-type phase retarder toproduce the circular polarization near the 111 Bragg condition of diamond in the asymmetric
Laue case. Diffraction profiles were measured at wavelengths of λ = 1.7406 and 1.7390 Å,
using a four-circle/triple-axes diffractometer. An ω step-scan technique was applied forsingle crystals in the weak magnetic filed. Low-temperature experiments at T = 100 K were
performed with the Oxford Cryostream Cooler, where cold and dry nitrogen gas is directly
blown onto the crystal.
The crystal structure with spin orientation can be determined based on the difference
between observed and calculated asymmetry ratios. The observed asymmetrical ratio ΔRobs
was obtained for 32 Bragg reflections through the RXMS measurements. The ΔRcalc wasestimated from the crystal structure factors related to charge, anomalous, magnetic andresonant magnetic scattering terms, based on the structural model. The canting angles of spins
were estimated with residual factors of Σ(ΔRobs - ΔRcalc)2, where each iron sites had aminimum for the multiplicity. The relation between the substitution of Fe3+ and the magnetic
helix structure was obtained from the estimation of the degree of the spin canting. In thepresentation, the magnetic structure and magnetic anisotropy will be discussed in comparison
with the results of BaFe12O19 and BaTiCoFe10O19.

P05-093

SODIUM ARRANGEMENT IN NAXMO2 P2 STRUCTURE AS A
FUNCTION OF TEMPERATURE, TRANSITION METAL TYPE, AND
SODIUM STOICHIOMETRY
Angélique Jarrya, Maxim AvdeevbaMagistère Materiaux, university of Rennes 1, Franceb

The Bragg Institute, Australian Nuclear Science and Technology Organisation, Sydney, Australia

Recently renewed research interest in NaxMO2 compounds (M=transition metal) has
revealed a range of interesting properties of this system. Due to its potential for thermoelectric
applications and superconductivity in the hydrated form, NaxCoO2 has been subjected toextensive study.
The γ-NaxCoO2, or P2 in Hagenmuller’s notation [1], structure type is built ofhexagonal layers [MO2]2∞ with Na ions sandwiched between planes of edge sharing MO6octahedra. Sodium ions can occupy two different types of trigonal prisms sharing either edges
or faces with MO6 octahedra. Due to the repulsion between sodium and transition metal M,
the latter type of prisms is less electrostatically favorable. Delicate balance between
sodium-sodium and sodium-transition metal interactions results in various arrangements of
Na+ in the interlayer space [3].
We extend previous theoretical and experimental studies of sodium clustering in sodium
cobaltate by investigating sodium arrangement in P2 structure type as a function of transition
metal type M, sodium content x, and temperature using X-ray and neutron powder diffraction.
References:[1] C. Delmas et al, Physica 99B (1980) 81-85[2] P. Zhang et al, Phys. Rev B 71 (2005) 153102[3] M. Roger et al, Nature 445 (2007) 631.

P05-094

UNUSUAL SITE PREFERENCE OF BORON IN SYNTHETIC
MgAl2-xBxO4 SPINEL (x = 0.11 and 0.13) UNDER HIGH PRESSURE
Shunsuke Sakai,aAkira Yoshiasa,a Takafumi Hashimoto,a Akihiko Nakatsuka,b Kazumasa
Sugiyama,c Maki Okube,d and Eiji Itoea

Graduate School of Science and Technology, Kumamoto University, Kumamoto 860-8555, Japanb

Department of Advanced Material and Engineering, Faculty of Engineering, Yamaguchi University,

Ube 755-8611, Japanc Institute for Materials Research, Tohoku University, Sendai 980-8577, JapandMaterials and structure laboratory, Tokyo Institute of Technology, Yokohama 226-8503, Japane

Institute for study of the Earth’s Interior, Okayama University, Tottori 682-0193, Japan

Using “6-8” type uniaxial split-sphere apparatus Single crystals of MgAl2-xBxO4 (x =0.11 and 0.13) spinel were synthesized of 9GPa and 11GPa at 1000℃. Site preference ofBoron and structural variation in MgAl2-xBxO4 spinel solid solution, have been investigatedby single crystal X-ray diffraction technique. The intensity data of X-ray diffraction were
measured at room temperature using Rigaku AFC-5S four-circle diffractometer withgraphite-monochromatized MoKα radiation (λ= 0.71069 Å; 40KeV, 30mA). The crystal
structure refinements using single-crystal X-ray diffraction method were carried out todetermine the site preference of B, Mg and Al atoms. The crystals were ascertained to satisfy
the systematic absence of space group Fd3m from precession photographs. Structuralrefinements were carried out using the full-matrix least-square program RADY92. The R
factors for x = 0.0, x = 0.11 and x = 0.13 were reached 2.25 %, 2.97 % and 2.52 %,repetitively. All B3+ occupy the octahedral site. Based on the site preference refinements andobserved bond length of each site, the chemical formula of B-bearling spinels are (Mg0.63,
Al0.37)[Mg0.37, Al1.50, B0.13]O4 and (Mg0.63, Al0.37)[Mg0.37, Al1.50, B0.13]O4, respectively. These
results are very important; the small B ion dose not occupying the small tetrahedral site, but it
occupies the largely octahedral site. When we compare the pure MgAl2O4 spinel, disordernesof cation site preference is increase with Boron contents. It is well known that spinel structure
wih higher symmetry has a peculiar site preference. The octahedral sites in spinel are
proffered by smaller Al ion than larger Mg ion. More ever, the smallest B ion gives priority tothe octahedral site most in the Mg-Al-B systems. The site preference depends greatly on the
structure of host crystal.

P05-095

PHOTOISOMERIZATION OF RUTHENIUM DIMETHYL SULFOXIDECOMPLEXES AND THEIR CRYSTAL STRUCTURES
Yuji Karakane, Hidehiro Uekusa
Department of Chemistry and Materials Science, Tokyo Institute of Technology, JAPAN

Ruthenium DMSO complex (Fig.1) shows photochromism from orange to red byirradiation of UV light. It is suggsted that the color change is caused by photoisomerization of
DMSO ligand (from Ru-S=O(S-form) to Ru-O=S(O-form)) from spectroscopic studies.
However, the relationship between the photo-reactivity and molecular/crystal structure was
not discussed well. In this study, geometrical features in the crystal structure that characterize
the photoisomerization process are investigated by X-ray single crystal analysis. In order tomodify the crystal structure and reaction cavity around DMSO group (Fig.2) from known[Ru(bpy)(tpy)(DMSO)](OTf)2 crystal, [Ru(bpy)(tpy)(DMSO)](PF6)2 was synthesized byliterature method, and crystal structure was determined.
The change of UV/VIS specta and powder diffraction pattern after UV irradiation
indicated that the photoisomerization reaction was occurred in solid-state. Also, the reaction
rate of [Ru(bpy)(tpy)(DMSO)](OTf)2 was faster than [Ru(bpy)(tpy)(DMSO)](PF6)2. The
reaction cavity volume calculation indicated that [Ru(bpy)(tpy)(DMSO)](OTf)2 crystal(14.8Å3) has larger cavity than [Ru(bpy)(tpy)(DMSO)](PF6)2 crystal (14.2Å3) and it may
contribute to the lower energy barrier of photoisomerization.

Fig.1 [Ru(bpy)(tpy)(DMSO)]2+

Fig.2 [Ru(bpy)(tpy)(DMSO)](OTf)2reaction cavity

P05-096

CRYSTALLOGRAPHIC STUDY ON DEHYDRATION BEHAVIOR OF
CHABAZITE
Akihiko Nakatsuka, Hironao Okada, Keiko Fujiwara, Noriaki Nakayama and Tadato Mizota
Graduate School of Science and Engineering, Yamaguchi University, Ube, Yamaguchi 755-8611,
Japan

Chabazite [idealized formula Ca2(Al4Si8)O24·12H2O], one of the most widespreadnatural zeolites, is a promising heat absorbent for the zeolite-water heat pump system becauseof its high heat-exchange abilities at low temperatures. The heat-exchange abilities of zeolites
are closely related to their thermodynamic hydration-dehydration process, and hence candepend on the strengths of the interactions between water molecules and their neighbors(framework atoms and exchangeable cations). Therefore, investigation of the dehydration
behaviors of water sites in chabazites is important for elucidating their properties as heatabsorbents. However, the dehydration behaviors of water sites in chabazites have been
unknown to date owing to the uncertainty of positions of water molecules and exchangeable
cations. In the present study, we carry out single-crystal X-ray diffraction study of fully
hydrated and partially dehydrated chabazites to examine the dehydration behaviors of watersites.
Single crystals of a natural chabazite [Ca1.57Na0.49(Al3.39Si8.55)O24·12.47H2O] from
Komuro, Oh-hito, Shizuoka Prefecture, Japan, were used in the present study. Selected
crystals were put into silica-glass capillaries, attached to a vacuum line, and dehydrated byheating at 100, 150 and 200 °C for 1 hour under 5 × 10−5 Torr. After that, the capillaries weresealed and slowly cooled to room temperature.
The present structure analyses have revealed the presence of five partially-occupied
water sites and four partially-occupied exchangeable-cation sites. The final structurerefinements converged to R = 0.0280−0.0303 and Rw = 0.0276−0.0302 for each sample. From
the resulting occupancies of the water sites, we confirmed that the prepared
dehydrated-samples have different water contents. The present results show that exchangeable
cations migrate to the exchangeable-cation sites located near the 6-ring windows withdehydration. Moreover, the dehydration behaviors of the water sites will be discussed withattention to the interactions between water molecules and their neighbors (framework atoms
and exchangeable cations).

P05-097

TEMPERATURE DEPENDENCE OF CRYSTAL STRUCTURE OFPYROPE GARNET
Mami Shimokawa,a Akihiko Nakatsuka,a Makio Ohkawab and Noriaki NakayamaaaGraduate School of Science and Engineering, Yamaguchi University, Ube, Yamaguchi 755-8611,

Japan;bGraduate School of Science, Hiroshima University, Higashi-Hiroshima, Hiroshima 739-8526,
Japan

Pyrope garnet (Mg3Al2Si3O12) is an important mineral as constituents in the Earth’s
upper mantle. In this garnet, Mg, Al and Si occupy dodecahedral, octahedral and tetrahedral
sites, respectively. Since the dodecahedral cavity size is too large for the ionic radius of Mg,
which would fit better into an octahedral coordinated site, Mg in pyrope has a geometricalanomaly. The large difference between the dodecahedral cavity size and the ionic radius ofMg suggests that positional disorder of Mg could occur together with its strong vibrationalmotion. Indeed, it is well known that the displacement parameter of Mg in pyrope is muchlarger than those in other silicate garnets. However, conclusive evidence for the positional
disorder of Mg has not been obtained to date, although efforts to solve this problem have been
made by several researchers. In the present study, to examine the possibility of positional
disorder of Mg, we investigate the temperature dependence of crystal structure of pyrope,with attention to temperature dependence of displacement parameter.
Single crystals of pyrope were synthesized at 8 GPa and 1600 °C. X-ray diffraction
intensities of a selected crystal were measured in the temperature range of 88−473 K using afour circle diffractometer. The structure refinements at each temperature converged to R =0.0198−0.0291 and Rw = 0.0126−0.0234.
The present result shows that the isotropic equivalent displacement parameter of Mg[Beq(Mg)] decreases linearly with decreasing temperature. The possibility of positional
disorder of Mg will be discussed from the extrapolation of the displacement parameter to 0 K.
Moreover, the residual electron density distribution around the dodecahedral site obtained
from the difference Fourier synthesis will be also discussed to clear whether or not there is the
positional disorder of Mg.

P05-098

EVOLUTION OF CORUNDUM STRUCTURE AT HIGHTEMPERATURES
S. Kondo, K. Tateishi, H. Hibino and N. Ishizawa
Nagoya Institute of Technology, Tajimi, Japan.

The evolution of corundum (α-Al2O3) structure was investigated at 297, 573, 873 and1173K using single-crystal X-ray diffraction method and molecular dynamics simulation. The
results were smoothly extrapolated to the previous high-temperature data of the compound at
2170 K 1), revealing a significant shift of fractional coordinate z of the Al atom as a functionof temperature. The Al atom shift indicates that the Al-Al repulsion force across a pair offace-sharing octahedra becomes conspicuous over the other interatomic forces at hightemperatures. The increasing Al-Al repulsion is relieved by both the preferential expansion of
the unit cell along the c axis and the change in the z coordinate of Al atom. The molecular
dynamics simulation experiments qualitatively agreed with the X-ray results. The thermal
expansion of the crystal was well described by the quadratic functions, a = 4.75385 (1.0 +5.05841x10-6 T + 1.69084x10-9 T2) Å, and c = 12.9782 (1.0 + 4.61344x10-6 T + 2.63802x10-9
T2) Å. The thermal expansion data of corundum in the literature 2-4) will be discussed.
Reference:
1) N. Ishizawa, T. Miyata, I. Minato, F. Marumo and S. Iwai : Acta Cryst. B36 (1980)
228-230.
2) W. M. Yim & R. J. Paff: J. Appl. Phys. 45. (1974) 1456-1457.
3) Yu. V. Shvy’ko, M. Lucht, E. Gerdau, M. Lerche, E. E. Alp, W. Sturhahn, J. Sutter & T. S.
Toellner: J. Synchrotron Rad. 9. (2002) 17-23.
4) M. Lucht, M. Lerche, H.-C. Wille, Yu. V. Shvyd’ko, H. D. Rutter, E. Gerdau & P. Becker: J.
Appl. Cryst. 36. (2003) 1075-1081.

P05-099

PHASE TRANSITION OF Gd3RuO7
K. Okada, S. Kondo, T. Suwa and N. Ishizawa
Nagoya Institute of Technology, Tajimi, Japan.

The series of Ln3MO7 crystals composed of trivalent lanthanide (Ln) and pentavalenttransition metal (M=Ru, Os) oxides are expected to possess quasi one-dimensional electric
conduction properties along the MO6 octahedral single-chains. The series shows apolymorphism. A noncentrosymmetric orthorhombic P21nb modification has been recently
found for Gd3RuO7 1) in addition to the centrosymmetric Cmcm. The present study shows that
Gd3RuO7 undergoes a phase transition at approximately 382 K from P21nb tocentrosymmetric Cmcm.
Crystals were grown by cooling the SrCl2-RuO2-Gd2O3 solution at the rate of 5 Kmin-1
from 1373 K. Data were collected in nitrogen atmosphere by the CCD single crystal
diffractometer (Smart Apex II, Bruker) equipped with a heating apparatus. The structure wasdetermined at 297, 423, 773 and 1173 K. The structure at 297 K was confirmed to be P21nb
while those at 423, 773 and 1173 K were Cmcm with halved b-length. Changes of the celldimensions and superstructure reflection intensities were examined in the temperature range
between 296 and 523 K at the interval of 20 K. The anomalies were observed in both b and ccell dimensions while not clear in a. The superstructure reflections associated with the P21nb
modifications were gradually weakened with increasing temperature and disappeared between
363 and 383 K. A reverse change occurred with decreasing temperature. The transition
observed by the present X-ray diffraction study presumably corresponds to the anomaly at
382 K reported from the specific heat measurement 2).
The phase transition between the P21nb and Cmcm modifications can be structurally
characterized by an additional tilt about a which occurs in the low temperature form (P21nb)
for the half of the RuO6 octahedra. A reduction of coordination number from 8 (Cmcm) to 7
(P21nb) also occurs for some Gd atoms bridging the adjacent RuO6 single-chains. A positional
disorder reported for several Ln atom sites in the P21nb modifications 3) was also observed in
the Cmcm modification, suggesting that the phase transition is not the origin of the positional
disorder of Ln atoms.
References:
1) N. Ishizawa et al., Acta Cryst., E62, i13-i16 (2006).
2) D. Harada and Y. Hinatsu, J. Solid State Chem. 164, 163-168 (2002).
3) N. Ishizawa et al., Acta Cryst. C63, i43-i46 (2007); Acta Cryst. E63, i163 (2007).

P05-100

ANOMALOUS STRUCTURAL PHASE TRANSITION ABOVE LIQUIDNITROGEN TEMPERATURE IN THE MULTIFERROIC PEROVSKITE
Dy(Mn0.5Fe0.5)O3
Fu-Kuo Chiang (蔣復國)1,2,3, Fei-Ting Huang (黃妃婷)1,2,4, and Ming-Wen Chu (朱明文)1
1

Center for Condensed Matter Sciences, National Taiwan University

2

Taiwan International Graduated Program, Academia Sinica

3

Department of Engineering and System Science, National Tsing-Hwa University

4

Department of Chemistry, National Taiwan University

Multiferroics represent a novel class of materials whose constituent electric/magnetic
orders can be manipulated by external magnetic/electric fields, i.e., the magnetoelectric
coupling. Potential integration of the materials into modern memory storage media would
enable an electric/magnetic control of the magnetic/electric degree of freedom, thus bringing
the performance and design of the devices to a new era. The representative materials reported
up to date are TbMn2O5, TbMnO3 and DyMnO3 perovskites, and geometrically frustrated
CdCr2S4 spinel, and the origin of the multiferroic properties is still of much debate. Rare-earth
orthoferrites, which have been discovered in 1960~1970’s, exhibit weak ferromagnetism(canted antiferromagnetism) below 600K and a spin reorientation transition at low
temperature. Among them we are particularly interested in DyFeO3 (space group Pbnm) thatis the only orthoferrite undisputedly undergoing a spin transition from Γ4 (Fz) to Γ1 (0) at 36K.
We investigate the effects of Dzyaloshinksii-Moriya interaction according to the canted
antiferromagnetism in DyFeO3 and incommensurate antiferromagnetism in DyMnO3 (spacegroup Pbnm) and report a possible ferroelectricity by a systematic substitution of Fe3+ in
DyFeO3 with Mn3+.
Using the soft-chemistry method, firstly we synthesized the phase-pure andstoichiometric Dy(Mn0.5Fe0.5)O3 perovskite in the form of powders. The subsequent X-ray
powder diffraction of the material at room temperature, performed on NSRRC BL01C2,
indicates an increase (decrease) in the b-axis (c-axis) lattice parameter with respect to theparent phase. In contrast, the a-axis is little affected by the substitution, suggesting that thecomplex orbital-lattice coupling occurs principally within the bc-plane. The X-ray powder
diffraction at low temperatures further revealed the onset of several satellite peaks at 120 ± 2
K, and the intensity of these peaks increases monotonically with the decrease in temperature,reaching the maximum at 90 ± 2 K. Below ~90 K, the intensity of these peaks decreases andcompletely vanishes at 10 ± 2 K. The careful Rietveld refinements of the low-temperature
XRD patterns indicated that these peaks arise from the tripling of the lattice parameter along
c-axis. Noted that in the material there exists no driving force for this structural phasetransition, neither ionic (should have taken place at room temperature) nor charge ordering. It
is, therefore, most likely that a new magnetic ordering onsets and couples to the lattice degreeof freedom in the temperature window, 10 ~ 120 K. Measurements of the physical properties,
magnetization and heat capacity, show the anomaly around 120K indicating the spin-latticecoupling at the phase transition temperature. Dielectric constants measurement also shows achange at liquid nitrogen temperature revealing the magnetoelectric effect ofDy(Mn0.5Fe0.5)O3 and further detailed measurements are underway.

P05-101

SYNTHESIS AND STRUCTURE OF FERROMAGNETIC RUTILE
Takashi Mochiku,a Kazuhiro Yamaki, b Natsumi Shimizu,b Akinori Hoshikawa, c Hiroki
Fujii,a Katsura Yamada,a Shinji Itoh, a Itsuhiro Kakeya, b Kazuo Kadowakib and Kazuto
HirataaaNational Institute for Materials Science, Tsukuba, Ibaraki 305-0047, Japan; bUniversity of Tsukuba,

Tsukuba, Ibaraki 305-8573; cJapan Atomic Energy Agency, Tokai, Naka, Ibaraki 319-1195, Japan

There were many reports that ferromagnetism at room temperature was observed in
TiO2 (rutile and anatase) doped with 3d transition metals. However, these samples weresynthesized by the thin film growth techniques under thermally nonequilibrium conditions.
We have succeeded in the single crystal growth of rutile doped with 3d transition metals by
floating zone method from the melt in equilibrium conditions to investigate the mechanism offerromagnetism at room temperature.
The crystals doped with 1 at.% Co and 0.5 at.% Ni exhibit ferromagnetism at room
temperature when those are grown in reduced atmosphere. The magnetic properties of the
doped crystals are strongly dependent on the oxygen deficiency. Ferromagnetism was notobserved in the crystals annealed in air or oxygen atmosphere. The crystal lattice is enlarged
by doping and is compressed by annealing in spite of low doping concentration of Co and Ni.
These support that the doped elements are situated at the substitutional locations and theoxygen deficiency is important for exhibiting ferromagnetism.

P05-102

TEMPERATURE AND PRESSURE INDUCED TRANSITIONS OFPEROVSKITES ABX3 TO OTHER STRUCTURE TYPES
Maxim Avdeeva, Sergey YakovlevaaBragg Institute, Australian Nuclear Science and Technology Organisation

Using empirical approach based on polyhedral volume ratios and ab initio DFT
calculations we identified a number of perovskites ABX3 close to the boundaries ofperovskite structure type stability. Experimental results obtained during following in situ
X-ray powder diffraction studies at high temperature or high pressure combined with theanalysis of crystal chemical information accumulated in the Inorganic Crystal Structure
Database (ICSD) allowed us to establish quantitative parameters defining stability of ABX3
compositions in perovskite, post-perovskite (CaIrO3), or ilmenite structure type. Rare cases
when high pressure results in amorphisation of ABX3 materials rather than phase transition
will also be discussed in this context.

P05-103

SYNTHESIS AND CHARACTERIZATION OF SERIESHETERMETALLIC COORDINATION POLYMER MaxMb1-x(tda)H2O(Ma, Mb=Zn, Co AND Ni, 0<x<1 )Ming-Cheng Wu and Chi-Shen Lee*
Department of chemistry and Institute of Molecular Science, National Chiao Tung University, Hsinchu,
Taiwan, 300, R.O.C.

A series of two dimensional coordination polymer of mixed metal thiodiacetate
MaxMb1-x(tda)H2O(M=Zn, Co, and Ni, 1>x>0, thiodiactate=tda) were synthesis underhydrothermal condition. The structural of these compounds features a 2-dimensional
metal-oxygen network connected through edge or corner sharing of the MO5S polyhedra.
These MM’-tda-H2O have similar structure (e.g. Zn0.5Co0.5-tda-H2O: P21 monoclinic a=15.561(10)Å b =5.187(3)Å c =17.391(11)Å β=114.571(11)°). With different transition metal
as central ion, MaxMb1-x(tda)H2O exhibits many interesting properties due to excitation of d-dtransition orbital and unpaired electron. Zn-tda-H2O is needle shapes colorless crystal, but Co
series show pink color and Ni series are green. Such physical properties measurements
revealed that the optic and magnetic properties could be controlled by tuning thecompositions of metal ions in MaxMb1-x(tda)H2O. Besides, the crystal structures of
MaxMb1-x(tda)H2O with different doping concentration were analyzed by using high-resolution
powder X-ray diffractions with synchrotron radiation. The thermo-behavior of
MaxMb1-x(tda)H2O were characterized by TGA and temperature-dependent powder X-ray
diffractions indicate these compounds are stable till 300°C.

P05-104

SYNTHESIS AND CHARACTERIZATION OF NEW QUATERNARYSELENIDE In1.91Pb4Bi4.09Se13
Ming-Fang Wang and Chi-Shen Lee*
Department of Applied Chemistry and Institute of Molecular Science, National Chiao Tung University,
Hsinchu, Taiwan, 300, R.O.C.

The new quaternary compound of In1.91Pb4Bi4.09Se13 was synthesized by direct
combination of the In:Pb:Bi:Se = 1.91:4:4.09:13 at temperature at 1023 K. The structure wasdetermined by single-crystal X-ray diffraction. The compound crystallized in theorthorhombic space group Pbam with a = 22.29(2) Å、b = 27.52 (2) Å、c = 4.144(2) Å、V =2542(3) Å3、Z = 4. The final R values are R1 = 0.0322, wR2 = 0.0706 and GOF = 1.04. The
structure of In1.91Pb4Bi4.09Se13 features three-dimensional framework containing building
blocks of wide rectangular NaCl-[100] type infinite rod type unit and corner-shared infinite
one-dimensional [InSe4] chains running parallel to the c-axis. Band structure calculation
based on the model In1.91Pb4Bi4.09Se13 suggests that the material is a narrow band gap
semiconductor. Four probe electroconductivity measurements in temperature range between
30-800 K show declines of the resistivity with increase of temperature. Thermopower of
In1.91Pb4Bi4.09Se13 is ~ -200-300 μV/K over temperature range between 300 and 550 K, whichindicates n-type semi-conducting property. The room temperature power factor of
In1.91Pb4Bi4.09Se13 is 0.67 μW/cmK2.

P05-105

MAGNETIC PROPERTIES OF DINUCLEAR ONE-DIMENSIONALCOMPLEXES WITH TRIAZOLE BASED LIGANDS
S. M. Chen,a C. F. Sheu,a Y. S. Wen,b and Y. Wang*aaDepartment of Chemistry, National Taiwan University, Taipei, TaiwanbInstitute of Chemistry, Academia Sinica, Taipei, Taiwan[{FeII(μ-bpt)(NCS)}2L] (bpt = 3,5-bis(pyridin-2-yl)-1,2,4-triazole), L = pyrazine(1),4,4’-bipy(2) have been synthesized by one-step solvo-thermal syntheses; both exhibit an
abrupt spin transition at 130 and 156K respectively. The FeII centers are connected with two
bi-dentate ligands “bpt” equatorially and bridged axially by linking ligand of “pyrazine” or“4,4’-bipy” to form an one-dimensional dinuclear zigzag chain. There is only one unique Fesite in the structure due to the center of symmetry at the center of the dinuclear species. Whenthe temperature is cooling down through the phase transition temperature, the spin state of Fe
centers will change from high spin state to low spin state, namely a [LS–LS] pair of 1 and[HS-LS] of 2 dinuclear complexes. The typical change of ~0.2 Å in Fe-N bond lengths isobserved associated with the spin transition.
The another dinuclear Fe(II) complex, [Fe2(μ-bpt)2(C6H4NO2)2‧H2O], with the FeII
centers connected with bpt and isonicotinic acid is an one-dimemsional flexuous chain ofdinuclear FeII complex. It is also synthesized by solvo-thermal synthesis and characterized by
x-ray diffraction. The bond lengths of Fe-N are 2.331(1) Å, 2.130(1) Å, 2.233(1) Å, 2.126(1)Å and Fe-O are 2.057(1) Å, 2.093(1) Å at 300 K which are characteristic high spin state of
FeII centers. This chain complex shows distinct ferromagnetic interaction between the FeII
centers. The comparison between these dinuclear complexes and other similar structures
will be presented.
Keywords: spin crossover, ferromagnetic interaction, dinuclear complex

P05-106INVESTIGATION OF THE ELECTRONIC STRUCTURE OF
LANTHANIDE ZIRCONATES
Richard Clementsa,b, Brendan Kennedya, Chris Linga,b, Anton StampflbaSchool of Chemistry, The University of Sydney, New South Wales, 2006, Australia; bBragg Institute,

Australian Nuclear Science and Technology Organisation, PMB 1, Menai, New South Wales, 2234,
Australia.

The lanthanide zirconates are of interest for potential use in inert matrix fuels andnuclear wasteforms. To determine the suitability of a material as an inert matrix or wasteform,
the material's structure must be resistant to radiation damage and its thermal, thermodynamic
and mechanical properties must be known. The structure's ability to incorporate an actinide
host into the lattice vacancy must also be known. These properties may be better understoodby investigating the f-electronic structure, which has historically proved troublesome tomodel.
We have undertaken a synthesis of the full range of lanthanide zirconate series using
solid state techniques. We have obtained powder laboratory X-ray diffraction and synchrotron
powder XRD patterns on a selection of the series. These results will be presented, along withdetails of the analysis and synthetic techniques used.

P05-107

STRUCTURAL PHASE TRANSITION ACCOMPANIED BYMETAL-INSULATOR TRANSITION IN HOLLANDITE VANADATE
Masahiko Isobe, Shigenori Koishi and Yutaka Ueda
Institute for Solid State Physics, The University of Tokyo, Kashiwanoha 5-1-5, Kashiwa, Chiba
277-8581, Japan.

K2V8O16 have a hollandite structure with space group I4/m at room temperature. In the
crystal structure, the double rutile-type chains of VO6 octahedra share corners with theneighboring chains to form a V8O16 stoichiometry framework that encloses large four-sided
tunnels. The K+ cations are located in the tunnels. K2V8O16 is a mixed-valence compound,since the crystallographic site of the vanadium atom is unique. The formal oxidation of thevanadium is +3.75. We reported a metal-insulator transition in K2V8O16 for the first time lastyear [1]. This transition was accompanied by structural change from a tetragonal to a
monoclinic structure.
Recently we have prepared a new hollandite vanadate Rb2V8O16 and observed a similar
metal-insulator transition. Also the solid solutions K2-xRbxV8O16 and K2V8-yTiyO16 have been
prepared successfully. These structural changes at the transition have been investigated byusing powder X-ray diffraction.
The metal-insulator transition of Rb2V8O16 was accompanied by structural change froma tetragonal to another tetragonal structure, which is different from that of K2V8O16. In thesolid solutions K2-xRbxV8O16, K1.6Rb0.4V8O16 showed two structural transitions. At the firsttransition, we observed the structural change from a tetragonal to another tetragonal structure.
At lower temperature the second transition from the tetragonal to a monoclinic structure wasobserved. The first transition seems to correspond to the metal-insulator transition. In contract,
at the second transition the magnetic susceptibility did not show any anomaly. The second
transition disappears with increasing Rb contents. In K2V8-yTiyO16 system, similar two
structural transitions were also observed. However the both transitions disappear withincreasing Ti contents rapidly.
Reference:[1] M. Isobe, S. Koishi, N. Kouno, J. Yamaura, T. Yamauchi, H. Ueda, H. Gotou, T. Yagi and
Y. Ueda, J. Phys. Soc. Jpn. 75, 073801 (2006)

P05-108PSEUDO-MEROHEDRAL TWINNING : HOW TO TREAT A SIX-FOLD
TWIN
Martin Adam, Anita Coetzee, Leo Straver and Rob Hooft
Bruker AXS, Oostsingel 209, NL 2612 HL Delft, The Netherlands

The introduction of two dimensional detectors for single crystal diffraction has made it
possible to easily collect data of pseodo-merohedral twins, incommensurate structures andstructures including diffuse scatter. Many programs exist, e.g. GEMINI, CELL_NOW and
DIRAX, with which these more complex matrices can be indexed.
A common problem with pseudo-merohedral twinning is cell refinement due to closely
overlapping spots. Careful selection of trusted areas to refine the cell in, will improve thereliability of the cell parameters.
Recent versions of integration programs, such as SAINT and EvalCC utilize thedifferent orientation matrices and can integrate the entire intensity of every reflection labelingthem as overlapping or not. One of the pitfalls during integration of data frompseudo-merohedral twins is that the spot shape changes continuously due to the systematic
overlap of areas of adjacent spots. Special care has to be taken when setting up the integration
parameters.
Most semi-empirical scaling and absorption correction programs are not able to handle
datasets of such complexity. The program TWINABS was developed specifically to carry out
absorption correction and scaling on datasets which contain reflections from different
domains. Resultant data files distinguish between non-overlapping and overlappingreflections and can be seamlessly used for structure refinement.
The approach is illustrated using a six-fold twin that shows a reversible transition to
single crystal state.

P05-109

THE CRYSTAL STRUCTURE OF GUEST-REMOVEDMELANOPHLOGITE
Akihiro Idaa, Kuniaki Kiharaa and Shuhei FujinamibaGraduate School of Natural Sciences and Technology, Kanazawa University; bDepartment ofChemistry, Faculty of Science, Kanazawa University, Kakuma, Kanazawa, 920-1122, Japan

Melanophlogite (MEP), 23SiO2 • M12 • 3M14 (Z = 8 for low MEP and 2 for high MEP),
is a silica clathrate mineral, containing small molecules such as CO2, CH4, N2 and so on in
two kinds of cage-like voids, which are represented by M12 and M14 in the formula. Thesemolecules, hereafter called as guest-molecules, would be held in the cage via van der Waals
contact with the framework atoms. According to Liu et al. (1997), the guest-molecules are
perfectly removed from a natural MEP by heating treatment above 950 °C for 6 hours. The
knowledge of the temperature dependences of structural data in a guest-removed MEP(GR-MEP) would be important to clarify the correlation between the guest-molecules and the
SiO2 framework , or further to assess the stability of natural MEP.
The sample crystals of GR-MEP were obtained in heating natural MEP from Mt.
Hamilton, California, USA at 950 or 1000 °C for 6 hours. The originally colorless andtransparent crystals became jet black-deep brown, after the heat treatment, likely in previous
reports. The crystal structure of GR-MEP was investigated with least-squares refinement
based on the single-crystal X-ray diffraction data at four different temperatures. The
integrated intensities were measured on CCD diffractometer (Rigaku Mercury) at -50 and 23°C, and on 4-circle diffractometor (Rigaku AFC7S) at 23, 100 and 200 °C. An opticalobservation under polarization microscope at room temperature suggested that the specimen
was optically isotropic. Intensity-relationship among reflections, which are to be, equivalent
in the expected cubic symmetry, i.e., m 3 m, indicated no sign of departure from thatsymmetry. This applies to all the measurements at the 4 temperatures, apparently being
inconsistent with Liu et al. (1997), who found possibilities of two phase-transitions at 140 and
60 °C in NMR experiments. The space group of our GR-MEP is Pm 3 n, the same as high
MEP with a = 13.4482(12) Å at room temperature. The unit cell volume of GR-MEP slightly
expanded approximately 0.9 % compared to that of natural MEP. This is anotherinconsistency to Liu et al. (1997). Difference-Fourier maps obviously indicated that residual
electron densities appeared in the cages, (proved to be 32.3 % in M12 and 84.8 % in M14 in theleast-squres refinement). The refinements confirmed that the original framework structure isretained with nominal Si-O bond lengths and Si-O-Si angles only insignificantly changed.
The harmonic least-squares refinements showed that mean-square displacements (MSD)
for all atoms except O3 and O4 decreased with increasing temperature. Such peculiar
behaviors are known in some temperature ranges above the phase-transition points in high
MEP and β-quartz. A generalized probability density function (PDF) analysis showed the
PDF contours on O1 and O2 to be of a tendency of splitting. The contour shape of O1changes from unimodal to bimodal with decreasing temperature. The same is also applicableto the PDF of O2, but with a clearer splitting. The symmetry breaking from Pm 3 n to andPm 3 will occur at lower temperature, than the present temperature in our specimen, if any.

P05-110

STRUCTURE REFINEMENT OF THE SAMPLE OBTAINED BY
NASA’S STARDUST MISSION
Kazumasa Ohsumi,a Kenji Hagiya,b Takashi Mikouchic and Michael ZolenskyaaNASA/Johnson Space Center; bGraduate School of Life Science, Univ. of Hyogo; cGraduate School of

Science, Univ. of Tokyo

Many tiny samples from the comet named Wild2 were obtained by the NASA’s
Stardust Mission in January of 2006. We reported the results of the structure refinements ofolivine and orthopyroxen included in the track of C2054,0,35,4 of cometary materials at
AsCA’06/CrSJ in Tsukuba in the last November. These results showed the site occupancies(Mg/[Mg+Fe]) of octahedral sites of olivine and orthopyroxene as 0.905(4), 0.894(4) and0.98(6), 0.81(9), respectively.
Olivine in the other track of C2067,1,111,4 was newly refined as follows. The Lauepattern of this sample was obtained by 120 min. exposure with the ring operation of 2.5 GeV.
All of the Laue spots were indexed base on cell dimension of olivine. Although more than
200 spots were indexed, integrated intensities of 124 spots were used for structure refinementby taking into account of absorption effect. It becomes serious at the wavelength emitted atmore than 1.5 A.
After several cycles of least-square refinement of the structure, the refinement includingsite occupancies was carried out, and showed the site occupancies [Mg/(Fe+Mg)] of
octahedral sites as 0.72(2) and 0.69(2). Although these values are different from ourprevious results, they are acceptable considering the obtaining knowledge of Wild2 materials.

P05-111

CRYSTAL STRUCTURE AND PHOTO-EXCITATION ENERGYMIGRATION IN CRYSTALS OF DOUBLE-COMPLEX SALTS
M[Ru(bpy)3][CrxAl1-x(ox)3] (M+ = Na+, Li+; 0≦x≦1)
Satoshi Ishii, Tomoko Nakaguchi, Takuhiro Otsuka and Youkoh Kaizu
Department of Chemistry, Tokyo Institute of Technology; Tokyo, Japan

Double complex salts of MI[Ru(bpy)3][MII(ox)3] (MI+ = Li+, Na+, K+; MII3+ = Cr3+, Al3+)
are obtained by mixing [Ru(bpy)3]Cl2 and MI[MII(ox)3] solutions. Na[Ru(bpy)3][MII(ox)3](= Na salt) and Li[Ru(bpy)3][MII(ox)3] (= Li salt) are the same crystal structure except for thelattice constant. In the crystals, [MI(ox)3]3- constructs three-dimensional network structure(3D-network) linked by the alkali cations. [Ru(bpy)3]2+ is located in the space of the
3D-network of [MI(ox)3]3-. However, crystal structure of K[Ru(bpy)3][MII(ox)3] is different
from the Na and Li salts; [MI(ox)3]3- does not construct the 3D-network in the crystal.
We have studied one-step excitation energy-transfer from [Ru(N-N)3]2+ (N-N = bpy,phen) to [Cr(CN)6]3- in crystals of double complex salts [Ru(N-N)3]2[Cr(CN)6]Cl.1), 2) The
energy transfer is much effected by relative-orientation between [Ru(N-N)3]2+ and [Cr(CN)6]3rather than distance and spectral overlap between them.2)
In this work, we focus on the different types of crystal structures composed of[Ru(bpy)3]2+ and [Cr(ox)3]3- in order to investigate multi-step energy transfer which is called
energy-migration among [Ru(bpy)3]2+. When visible light is irradiated to MI[Ru(bpy)3][Al(ox)3], [Ru(bpy)3]2+ absorbs the radiation light. Then, the photo-excitation energy
transfers to the neighboring [Ru(bpy)3]2+. This energy-transfer occurs repeatedly, which iscalled energy migration. If Cr(III) complexes co-exists as an quencher in the crystal, theexcitation-energy is finally transferred to the Cr(III) complexes. At 77K, luminescence from
Cr(III) complexes can be observed.
We evaluated the energy-migration rate-constants with luminescence lifetime bychanging the concentration of Cr(III) complexes in the double complex salts from 4.2 K to300 K. We discuss the effect of lattice size and crystal structure on the energy migration.
Reference:
1)

Otsuka, Takuhiro; Takahashi, Naoto; Fujigasaki, Naoki; Sekine, Akiko; Ohashi, Yuji; Kaizu, Youkoh.
Inorganic Chemistry2)(1999), 38(6), 1340-1347.

Otsuka, Takuhiro; Sekine, Akiko; Fujigasaki, Naoki; Ohashi, Yuji; Kaizu, Youkoh.
Inorganic Chemistry(2001), 40(14), 3406-3412.

P05-112

STRUCTURE AND MAGNETIC PROPERTY OF CYANIDE BRIDGE
MOLECULAR SQUARE AND MOLECULAR SQUARE CHAIN
Chin-Lin Yang, Yu Wanga

Department of Chemistry, National Taiwan University; Taiwan, 300, R.O.C.

Poly-nuclear metal complexes often exhibit interesting photo-physical and magnetic
property. For example, Prussian blue related compounds do give interesting magnetic
property as being magnet at room temperature or exhibit photo-magnetic property due tocharge transfer induced spin transition(CTIST). Two metal ions bridged by cyanide ligand
normally show interesting magnetic coupling between them since the CN bridge makes two
metal centers apart for about 5Ǻ, which is an efficient distance for magnetic coupling and themetal coordinated by carbon and nitrogen atom is often in its low spin (LS) and high spin (HS)state respectively.
Two kinds of tetra-nuclear molecular square complexes were synthesized by thehydrothermal method: one is Fe4(phen)4(CN)4Cl4*3H2O (1) and the other is[Fe2Co4(phen)6(CN)9Cl4][FeCl4] *CH3OH (2). The former one has a square unit of formed by
two unique Fe ions linked by cyanide with a center of inversion at the center of the square,
Fe4: the Fe(1) is six-coordinated with two CN and two bi-dentate phen ligands; Fe(2) isfour-coordinated with two NC groups and two chlorides. The latter one is the molecularsquare formed by two types of square unit: one is formed by two Fe ions and two Co ionslinked by cyanide, Fe2Co2, the Fe(1) is again tetra-coordinated with two NC and two chlorides,
whereas Co(1) is six-coordinated with four CN and one bi-dentate phen ligand; the other typeof square unit is formed by four Co ions linked by cyanide, Co4.: two Co(1) ions are shared by
the Fe2Co2 square two Co(2) is six-coordinated with two NC and two bi-dentate phen ligands.
Thus a chain like squares are formed throughout the crystal. The counter anion here is FeCl4From magnetic measurement, both of compounds (1) and (2) show antiferromagnetic
interaction between metal centers. XmT value of compound (1) at room temperature, is about
6.4 , which is slightly larger than the spin only value (~6) based on two Fe2+ in HS state at Td
and two Fe2+ in LS at Oh. XmT value decreases smoothly to 5.5 at 15K and then decrease
sharply to 3.5 at 2K. In compound (2) XmT value is 16.5 at 300K which is a slightly larger
than spin only value of 14.12 XmT value decreases graduately to 9.3 at 2K. Detail distributionof the unpaired electron will be discussed. The geometries and magnetic properties in thesetwo compounds will be presented.

P05-113

LIGHT AND THERMAL INDUCED META-STABLE STATESTRUCTURE OF SPIN CROSSOVER COMPOUND {Fe(abpt)2[N(CN)2]2}
C. F. Sheu1, S. Pillet2, S. M. Chen1, Y. C. Lin1, I. J. Hsu1, G. H. Lee1, Y. H. Liu1, C. Lecomte2,
Y. Wang1*
1

Department of Chemistry, National Taiwan University, Taipei 106, Taiwan

2

LCM3B, UMR CNRS 7036, Université Henri Poincaré, BP 239, 54506 Vandœuvre-lès-Nancy Cédex,France{Fe(abpt)2[N(CN)2]2} is an intriguing spin crossover system which crystallizes in two
separate phases. The crystal structure of polymorph A has one unique iron center, which has
been first investigated by Moliner et al.[1], while that of polymorph B consists of two
crystallographic independent iron centers. Magnetic measurements indicate polymorph A isparamagnetic in the range of 2-300 K and polymorph B undergoes an incomplete two-stepspin transition with T1/2 = 86 K. There are around 37% of HS molecules trapped in the
low-temperature region (below 50 K) when standard cooling or warming modes (2K / min)are used. By rapid thermal quenching from room temperature to 5 K, a residual HS fraction ofnearly 50 % was achieved. After warming to 52 K, it induces HS -> LS relaxation; relatively
fewer HS residue is found compared to the standard cooling or warming modes. To
understanding the magneto-structural relationship, the crystal structures of{Fe(abpt)2[N(CN)2]2} polymorph B in particular conditions corresponding to the different
spin states are characterized, including (1) room temperature at pure HS state, (2) close to thestep in the thermal transition at T = 87 K, (3) 52 K by standard cooling mode, (4) 15 K
thermally quenched (5) 15 K photo-induced and (6) also the thermally relaxed state at 52 K. A
unique order-disorder phase transition was observed for the first time for spin transition
compounds, induced either by laser light irradiation or through rapid thermal quenching.
Reference:[1] Moliner N., Gaspar A. B., Munoz M. C., Niel V., Cano J. & Real J. A. Inorg. Chem. 40,
3986, (2001).

P05-114

STRUCTURAL STUDIES OF BIOLOGICALLY IMPORTANT
HETEROCYCLIC COMPOUNDSPeriyasamy Murugana, Munusamy Thirumavalavana, Tian-Huey Lub, Kuo Chu HwangaaDepartment of Chemistry, bDepartment of Physics, National Tsing Hua University, Hsinchu, Taiwan,
300, R.O.C.

Synthesis of three heterocyclic compounds viz. diethyl-3,4-dimethyl thieno[2,3-b]thiophen-2,5-dicarboxylate(compoundI),
diethyl-4-(phenyl
ethynyl)-2,6pyridinedicarboxylate (compound II) and 3-(4-fluorophenyl)-2-(4-pyridine N-oxide)-1-phenyl-2-propene-1-one (compound III) and their X-ray structural and mass and NMR
spectral studies will be reported. We shall present the facile synthetic routes of biologicallyimportant heterocyclic compounds I, II and III and the structural identification using various
spectroscopic measurements, including mass, IR, NMR, and X-ray crystallography.
The M+ peaks in the mass spectra match with the expected values for compounds I, II,
and III. The 1H NMR spectra show that the thiophene and pyridine rings exhibit modest
de-shielding effects on the moieties which are directly chemical bound to the aromatic rings.
The X-ray crystallographic measurements un-ambiguously confirmed the structures of thecompounds I, II, and III. Selected bond lengths will be compared with those of the existing
structures. The π-π interactions between the intermolecular rings will be indicated in figures.

P05-115

HYDROGEN BONDING INTERACTIONS AND SHEET-LIKE
STRUCTURES IN NICOTINAMIDE COMPLEXES
S. Athimoolam and S. Natarajan
Department of Physics, Madurai Kamaraj University, Madurai - 625 021. India.
e-mail id: xrdsopmku@yahoo.com

The phenomenon of hydrogen bonding has significance in the areas of molecular
recognition, crystal-engineering and organic synthons for supramolecular research.
Carboxylic acids and amides are two commonly used functional groups in crystal engineering,
because they generally form robust architectures via O-H...O and N-H...O hydrogen-bonded
dimers. The present investigation is concerned with the X-ray analyses of crystalline
complexes involving one of B vitamins (nicotinamide) with inorganic/organic acids.
Nicotinamide was reacted with the inorganic/organic acids, and the single crystals of thefollowing complexes were grown, viz., Nicotinamidium perchlorate, C6H7N2O+.ClO4- (NAP),
Nicotinamidium hydrogen oxalate, C6H7N2O+.C2HO4- (NAOX), Bis(nicotinamidium)bis[(2R,3R)-tartrate] 1.25 hydrate, 2(C6H7N2O)+.2(C4H5O6)-.1.25(H2O) (NATAR) andnicotinamidium trifluoroacetate, C6H7N2O+.C2O2F3- (NATFA). In all the four complexes, thecarboxamide plane is twisted from the plane of the protonated pyridine ring. The magnitudeof the twisting is measured from the dihedral angle between the planes of pyridine ring andcarboxamide which have the values of 7.4(2)° in NAP, 6.3(1)° in NAOX, 22.4(6) and 8.83(8)°for the two nicotinamidium residues in NATAR and 16.3(8)° for NATFA, respectively.
Protonation on the N atom is confirmed by the C-N bond distances and C-N-C bond angles.
One of the characteristic features, viz., outrage of N atom from the pyridine ring, is observedin all the four structures with the slightly larger C-N-C bond angle (>120°). Lamellar or
sheet like structures are observed through N—H···O and O—H···O hydrogen bonded motifs ofcations and anions in NAP, NAOX and NATFA complexes. These sheets are aggregatedthrough the chain motifs of C(4), C(5) and C(4) in NAP, NAOX and NATFA, respectively. In
NATFA, the sheets are found to have distorted or corrugated lamellar features. Ring motifs
of R12(4) in NAP and R12(5) in NAOX are observed through pyridine-anion bifurcated
N—H···O interactions. In NAOX, carboxamide group form N—H···O dimers around theinversion centres of the unit cell with the ring motif of R22(8). A 21 screw related helical or
ribbon like structure along the b axis is seen in NAOX through the carboxamide andpyridinium N—H···O hydrogen bonds with the oxalate anions. In NATAR, the anions are
forming ring motifs (or) assembly of hydrogen bonded arrays through O—H···O hydrogenbonds and the cations are sandwiched within these arrays of assembly.

P05-116

PYRIDOXINIUM NITRATE AND TRICHLOROACETATE
S. Athimoolam and S. Natarajan
Department of Physics, Madurai Kamaraj University, Madurai - 625 021. India.
e-mail id: xrdsopmku@yahoo.com

Vitamin B6, a water-soluble vitamin, is also known as pyridoxine. It is essential for bothmental and physical health. Other forms of vitamin B6 include pyridoxal and pyridoxamine.
Pyridoxine is involved in the production of antibodies, which protect humans against bacterial
diseases. Also, the combination of pyridoxine with immunosuppressive drugs improves theefficiency of that therapy. Pyridoxine has been found to play an essential role in the nervous
system and aids in the metabolism of fats, carbohydrates and proteins. In the present
investigation, Pyridoxine was reacted with nitric and trichloroacetic acids and the single
crystals of pyridoxinium nitrate, C8H12NO3+, NO3- (PYN) and pyridoxinium trichloroacetate,
C8H12NO3+, C2O2Cl3- (PYTCA) were obtained. In contrast to many of the vitamin B6
structures so far determined which exist as zwitterions in which the phenolic group isdeprotonated and pyridine N atom is protonated (a form found in metal-pyridoxine
complexes), the present complexes are found to have protonated cations. The asymmetricpart of the unit cell of PYTCA, contains a pyridoxinium cation and a trichloroacetate anion inwhich one of the -CH2OH groups of the cation, is disordered over two positions. As acharacteristic feature of pyridoxine complexes, twisting of the -CH2OH group is observed inboth the structures. The twisting is measured by the dihedral angles between the planes ofpyridinium ring and -C-CH2OH group which have the values: 16.2(4)° and 11.6(3)° in PYN
and 10.0(7)° [21.1(8)° for the minor disordered component] and 0.7(5)° in PYTCA. In PYN,
the cations and anions are oriented nearly parallel to each other, the angle between thepyridinium and nitrate planes being only 2.52(1)°. In PYTCA, the -CH2OH groups decrease
the overall planarity of the cation (r.m.s. deviation is 0.044 Å), particularly in comparison
with that of the pyridinium ring for which the r.m.s. deviation is only 0.0072 Å. Anothercharacterestic feature, viz., intramolecular hydrogen bond between the phenol OH and the-CH2OH group is seen through the S(6) motif in both the complexes. The zig-zag chain
C22(11) motifs are observed through the hydrogen bonding interactions of the cations andanions in both the complexes. In PYN, planar cations and planar anions are arranged incolumn-like structures leading to aggregation of the cations and anions, forming a sheet-likestructure parallel to the ( 8 08) and (80 8 ) planes. In PYTCA, the pyridoxinium cation islinked by the anion and forms a closed ring structure through N-H...O and O-H...O hydrogenbonds around the inversion centres of the unit cell leading to the graph-set motif of R24(16).

P05-117SYNTHESIS, GROWTH AND CHARACTERIZATION OF NEW
ORGANIC NONLINEAR OPTICAL CHALCONE DERIVATIVESSINGLE CRYSTALS
P. S. Patil a, S. M. Dharmaprakash a, G. Bhagavannarayana b and Hoong-Kun Fun caDepartment of Studies in Physics, Mangalore University, Mangalagangotri, 574 199, India;b

Materials Characterization Division, National Physical Laboratory, New Delhi, 110 012, India;c

X-ray Crystallography Unit, School of Physics, Universiti Sains Malaysia, 11800 USM, Penang,

Malaysia.

From the viewpoint of applications to optical devices, organic materials have several
distinguishing features; processability, cost effectiveness, high damage threshold, large
nonlinearity, and the ease with which large crystals of high optical quality can be grown andfabricated into desired shapes. For NLO materials with large second-order nonlinearities,
noncentrosymmetry at both the molecular and the macroscopic level is a prerequisite fornonvanishing molecular hyperpolarizabilities β and macroscopic susceptibilities χ (2).
Unfortunately, only a few molecules with large β values crystallize in noncentrosymmetricstructure, and fewer of them are useful for NLO materials. Recently, it has been noted that,among many organic compounds reported for their second harmonic generation, chalcone
derivatives are known for their excellent blue light transmittance and good crystallizability. In
these materials, the C = O bond acts as the electron withdrawing group, and electron-rich
substituents on the aromatic rings serve as the electron-donating group, forming a so-called
D–π–A type molecule.
Eight derivatives of chalcone were synthesized by Claisen – Schmidt condensation andevaluated their conversion efficiency of optical second- harmonic generation (SHG), UV –VIS transmission range and thermal stability. All the materials exhibit SHG efficiency
higher than that of urea and also excellent UV – VIS transparency. Among them,
1-(3-methoxyphenyl)-3-(4-methoxyphenyl) prop-2-en-1-one (3MMC) has SHG activity 10.7
times as large as urea. We have also determined structures of these compounds by single
crystal X – ray diffraction. All these materials crystallize in noncentrosymmetric space group.
Among these, single crystals of four SHG derivatives chalcone viz., DMMC, MCC, MNC,
and Ci3NC were grown by a slow evaporation solution growth technique (SEST) at room
temperature. The crystalline perfection was evaluated for the grown crystals by highresolution X-ray diffractometry (HRXRD). Though the crystals contain low angle boundaries,
the relatively low angular spread of the diffraction curves and the low FWHM values showthat the crystalline perfections are reasonably good.

P05-118

CRYSTAL STRUCTURES OF MONO- AND DI-SUBSTITUTEDFERROCENE DERIVATIVES
Naotake Nakamura, Kazuya Hiro and Takeshi Takamatsu
Department of Applied Chemistry, Ritsumeikan University, Kusatsu, 525-8577, Japan

A few mono- and di-substituted ferrocene derivatives were designed and synthesized in

our laboratory in order to obtain liquid crystals containing transition metal such as ion atom.
Some of them showed indeed liquid crystallinity.
In 2005, one of the present authors (N.N.) reported the crystal structure of
1,1’-bis[2-[4-(4-methoxyphenoxycarbonyl)phenoxy]ethoxycarbonyl]ferrocene, one of the
di-substituted ferrocene derivatives (abbreviated hereafter as bMAF-2). The “S” shaped and“U” shaped structures of bMAF-n, where n is number of the methylene chain in thederivatives, were known already except bMAF-2, then. However, bMAF-2 assumed to novel
structure as shown in Figure 1. The substituents of bMAF-2 had gauche conformation aroundthe methylene chain, and it was named “Z” shaped structure by the authors. This derivative,bMAF-2, didn’t show liquid crystallinity. The reason why may be considered that an aspectratio of bMAF-2 is not large enough to show liquid crystallinity.
Crystalstructure
analysisofmono-substituted
ferrocenederivative,
2-[4-(4-methoxyphenoxycarbonyl)phenoxy]ethoycarbonylferrocene, (abbreviated hereafter as
mMAF-2), of which substituent is the same as that of bMAF-2, was carried out using X-ray
diffraction method in the present study. The molecular structure obtained is shown in Figure 2.
This is also included gauche conformation around the methylene chain, and it is almost thesame as a half of bMAF-2 structure as easily understand from Figure 2. The derivative,
mMAF-2, didn’t show liquid crystallinity. The reason why may be considered that themolecular shape vary considerably from rod like one which is advantageous to show liquid
crystallinity.

Figure 1. Molecular structure of bMAF-2.
Figure 2. Molecular structure of mMAF-2.
(N.Nakamura & M.Nishikawa)(This work)
The details will be presented and discussed at the conference.

P05-119SUPRAMOLECULAR HYDROGEN-BONDING NETWORKS IN
ADENINIUM SALTS
Balasubramanian Sridhar and Krishnan Ravikumar
Laboratory of X-ray Crystallography, Indian Institute of Chemical Technology, Hyderabad – 500007,
India.
Email : sshiya@yahoo.com

Adenine is one of the two purine nucleobases used in forming nucleotides of the nucleic
acids DNA and RNA. It occurs free in tea and in combined form in nucleic acids, ATP,vitamin B12, and several coenzymes. Adenine nucleobases provides interesting building
blocks for forming extended structures, not only by the multiple possibilities in which bases
may interact by hydrogen bonds, but also for the possible π-stacking between them(Houlton, 2001). Adenine and guanine form hydrogen bonds with other nucleobases thatcan lead to the formation of supramolecular structures, which can be of chemical andbiological interest. Protonated nucleobases are present in many biochemical processes such as
enzymatic reaction, stabilization of triplex structures, and they play a key role in a newly
emerging feature of nucleic acid chemistry, namely acid-base catalysis. The asymmetric unitof (I) contains two adeninium cations (1 and 2), two half phthalate dianions having
crystallographic C2 symmetry, one neutral phthalic acid molecule, and one fully occupied andone partially occupied site (0.45) for water molecules, while, (II) contains one adeninium
cation, one phenylacetate anion, one neutral phenylacetic acid and one water molecule, and(III) comprises one adeninium cation, one succinate anion and one water molecule with oneof the carboxyl groups in the succinic acid deprotonated. In all the structures, the adeninium
cations form N---H...O hydrogen bonds with their anion counterparts andadeninium-adeninium self-association base pairs with the R22(10)-type motif. Conventionalhydrogen-bonds lead to layer structures in (I) and (II) and two-dimensional infinite polymericribbons in (III). The details about the crystal structure, conformation and hydrogen bonding
aspects will be presented and discussed.

P05-120

CRYSTAL OF 6-[BIS(2-CHLOROETHYL)AMINO]-12-OXO-DIBENZO[d,g] [1,3,2]DIOXAPHOSPHOCIN 6-OXIDE
Jadaprolu Radha Krishnaa, Musali Krishnaiaha, Vedavati G. PuranikbaDepartment of Physics, Sri Venkateswara University, Tirupati-517502-India; bCentre for Material

Characterization, National Chemical Laboratory, Pune-411 008, India

The crystal structure and conformation of organophosphorus compounds have become
the subject of intense study due to their involvement in many biological processes. The
proven toxic effects of phosphoric acid esters on pests and their possible application as
lubricant additives prompted the synthesis of a new class of organophosphorus heterocyclic
esters. To our knowledge, there have been few reports of structural studies on eight-memberedheterocyclic organophosphorus compounds, and hence undertaken the crystal structure of thetitle compound.
Crystal data: C17H16Cl2NO4P, Mr = 400.18, Rectangular yellow crystals, monoclinic,
P21/c , a= 21.273(4), b = 8.538(11), c = 19.353(7) Å, β =90.864(6)°, V= 3514.7(12) Å3, ρm=
1.50,
ρc= 1.513 Mg/m3, Z = 8, (MoKα) = 0.71073Å, & F(000)= 1648. Final R= 0.039
and Rw= 0.081 for 6585 with [I ≥ 2 σ (I)].
The eight-membered dioxaphosphocine ring adopts a distorted boat conformation withthe phosphoryl O atom equatorial and ‘oxo’ group in a pseudo equatorial arrangement. The
planar benzene groups fused to heterocyclic ring makes an angle of 53.7º in molecule-I and
50.3º in molecule-II with one another. The bond lengths around P-atom and ‘oxo’ group (C=O)
are increased due to N-mustered group attached as exocyclic substitution. The structure isstabilized by intra- and intermolecular C-H---O hydrogen bonds, linking the molecules into
chains.

P05-121

CRYSTAL STRUCTURE OF 4-(4-CHLORO-PHENYL)-5-PHENYLISOXAZOLE
A.K.Balajia, J.Radha Krishnaa, M.Krishnaiaha, Than Zaw Oob, Thetmar Winb and Pho KaungbaDepartment of Physics, Sri Venkateswara University, Tirupati-517502, INDIAb

Department of Physics, Yangon University, Myanmar.

The isoxazoles are a group of heterocycles, generated by the insection of nitrogen atom
at 2nd –position of the furan. Isoxazoles are unique in their chemical behaviour like aromatic
system particularly at the N-O bond.
The structural studies of isoxazoles and their derivatives have attracted considerable
attention with their multifaceted applications as monoamine oxidase inhibitors used in
psychotherapy, anti-inflammatory and anti-tumer agents. Some of them are industrial
important as semiconductors and corrosion inhibitors in fuels and lubricants. In agriculture
applications, herbicidal activity has been identified for some isoxazoles. The X-ray structure
determination of some isoxazoles have been undertaken to investigate the effect of thesubstituents on the conformation of the heterocyclic ring with respective to their orientations.
Crystal data: C30 H20 Cl2 N2 O2, Mr = 511.38, Colourless transparent crystals,
triclinic, P- 1 , a = 6.554(7), b =25.966(17), c=7.472(10) Å, α = 90.07(9), β = 106.17(9) γ= 89.78(7)°, V= 1221(2) Å 3, ρc = 1.391 Mg/m3 , Z = 2, (MoKα) = 0.71073Å, & F(000) = 528,
Final R= 0.0554and Rw= 0.1691for 2845 with[I ≥ 2 σ (I)].
Isoxazole ring is planar. At the point of linkage of substituents to the isoxazole ringenlargement in bond lengths, bond angles and torsion of the substituted moieties with respect
to isoxazole ring are observed. In the crystal, molecules are packed with van der Waals
interactions.

P05-122

MOLECULAR RECOGNITION OF 2-PHENOXYBUTANOIC ACID BYCHIRAL AROMATIC AMINES
Ryoma Aoki,a Yukio Takahashi, b and Isao FujiiaaDepartment. of Biological Sci. and Tech., Tokai Univ., Japan., bDaito Chem. Co., Ltd, Japan

The production of non-naturally occurring-amino acids or amines has great importancein the pharmaceutical industry. An aqueous solution of racemic compound and optically pure2-phenoxypropionic acid [PPA] has been applied in the diastereomer salt separation. We
have applied PPA in the resolution of such compounds, 2-methylpiperadine, pipecolic acid,alanine, valine, 2-aminobutanoic acid.1-3) We recently reported that the chiral interface
between hydrophobic and hydrophilic layers (chiral shallow pockets on the hydrophobic
layers) formed by PPA recognizes the chirality of compounds.4) The CH…π interaction
between the methyl and phenyl groups of PPA strongly affects the stability of pockets on thehydrophobic layers. In this study, we focused to clarify the inherent structure of substituted
2-phenoxybutanoic acid [PBA], and disclose the varieties of chiral interface formed by PBA
molecules. The complexes of S-1-naphtylethylamine [S-NAP] and S-2-phenylethylamine[S-PEA] with S-PBA, and the pure S-PBA were examined by X-ray analysis.
Reference:
1) T Watadani, Y Takahashi & I Fujii, Anal Sci, 21, x25 (2005).
2) I Fujii, T Watadani, S Nunomura & Y Takahashi, Anal Sci, 21, x41 (2005).
3) I Fujii, H Baba & Y Takahashi, Anal Sci, 21, x175 (2005).
4) I Fujii, T Watadani, S Nunomura & Y Takahashi, Anal Sci, 22, x75 (2006).

Et
O

NH2
COOH

Et
O

.

S-NPA

NH2
COOH

.
S-PEA

P05-123

STRUCTURE DETERMINATION OF PENTACENE DERIVATIVE BY
SYNCHROTRON POWDER DIFFRACTION DATA
Hwo-Shuenn Sheu,a Wei-Ju Shih,a Wei-Tsung Chuang,a and Yu-Tai TaobaNational Synchrotron Radiation Research Center, Taiwan. b Institute of Chemistry, Academia Sinica,

Taiwan.

Organic thin-film transistors have attracted much attention for their potential applicationas alternatives to the traditional amorphous silicon-based TFTs. The pentacene derivative
stands out as a promising material because of its ability to form ordered films and its
reasonably high field-effect mobility and on/off ratio. Numerous efforts were attemptedaiming at improving the electronic properties of pentacene-based devices. The crystal
structure of the pentacene derivative thin film is the main theme to understand the physicalproperties and provide the base for theoretical calculation. We have solved the crystal
structure of tetra chlorodiazapentacene (TCDAP) by synchrotron powder diffraction data. The
compound is difficult to growth large enough crystal for single crystal diffraction study. Fromthe powder diffraction data we found that TCDAP crystallize in monoclinic of space group P
21/n, a=17.0302(17), b=12.1166(11), c=4.0236(2)Ǻ, beta=91.29(1), vol=930.06(9), Z=2. The
unit cell is indexed by DICVOL. Structure determination from powder diffraction data wascarried out using monte carlo simulation of DASH program. The final Rietveld refinement by
GSAS program gave Rwp= 0.0675, Rp=0.0425, and X2= 1.56. The powder structure of
TCDAP fit well to its thin film diffraction pattern. Some other powder structures of pentacene
derivatives will also reported in the meeting.

P05-124

PREPARATION, PROPETIES, AND STRUCTURAL STUDIES OF[MCl(diphosphine)]2 (M = Rh, Ir; diphosphine = BINAP)
Tsuneaki Yamagata,a Aika Iseki,a Kazunori Hoshida,a Hiromitsu Nagata,a Kazuhide Tani,a,b,
and Kazushi MashimaaaDepartment of Chemistry, Graduate School of Engineering Science, Osaka University,

Machikaneyama 1-3, Toyonaka, Osaka, 560-8531, Japan, bHigashiosaka College, Nishitutumi
Gakuen-chou 3-1-1, Higashiosaka, Osaka 577-8567, Japan

Recently, we have reported the isolation and characterization of [IrCl(binap)]2 1{BINAP = 2,2'-bis(di-phenylphosphino)-1,1'-binaphthyl}. Complex 1 reacted easily with
MeOH, H2O, PhSH, RCOOH (R = Me, Ph, p-tolyl), and HX (X = Cl, Br, I) to give theoxidative addition products ([{IrHCl(binap)}(μ-Cl)2(μ-OMe)]Cl 2, ([{IrHCl(binap)}(μ-Cl)2(μ-OH)]Cl 3, [{IrHCl(binap)}(μ-Cl)2(μ-SPh)]Cl 4, OC-6-23-A-[IrCl(H)(O2CR){(S)-binap}](R = CH3, Ph, p-tolyl, etc.) 5, and [{Ir(H)-[(S)-binap]}2(μ-X)3]X (X = Cl, Br, I) 6. These
complexes were efficient for transfer hydrogenation of alkynes and alkenes with methanol asa hydrogen source (2), hydration of nitrile (3), and asymmetric hydrogenation of prochiralimines (5 and 6). However, [RhCl(binap)]2 7 does not react with protic molecules orBrönsted acid at ambient temperature.
We will discuss the structures of 1 and 7 and the different reactivity of them for protic
molecules or Brönsted acid.

P05-125

HIGH RESOLUTION CRYSTAL STRUCTURE OF A BLUECOMMERININ PIGMENT
Naohiro Matsugaki,a Masaaki Shiono,b and Kosaku TakedacaPhoton Factory, High Energy Accelerator Research Organization, Oho 1-1, Tsukuba 305-0801,

Japan; b Department of Physics, Graduate School of Science, Kyushu University, Hakozaki 6-10-1,
Fukuoka 812-8581, Japan; c Department of Biology, Tokyo Gakugei University, Koganei, Tokyo
184-8501, Japan.

The structure of commerinin, a pigment of a blue dayflower, was solved by Kondo et al.
in 1992 [1]. The authors reported that the pigment was composed of six anthocyanin and six
flavone molecules with two Mg ions, based on the crystal structure analysis at 1.0Å resolution.
However, our recent research on the structure of protocyanin pigment [2] indicated that thecommerinin complex pigment has other metal constituents.
We investigated the crystal structure of the commerinin pigment at the resolution of 0.7
Å using a large CCD area detector at BL-5A of the Photon Factory. The structure reveals two
additional Mg ions bound to outer side of the complex pigment. The positions of Mg ionsroughly corresponded to those of Ca ions in the protocyanin structure. The high resolution
structure including the positions of hydrogen atoms will be presented.

P05-126

SOLID-STATE PHOTODIMERIZATION OF 6-METHYLCOUMARIN
AND IT’S INCLUSION COMPLEXES, INVESTIGATED BY Ab INITIOPOWDER CRYSTAL STRUCTURE ANALYSIS
Kotaro Fujii,a Hidehiro Uekusa,a Shunsuke Tanigawa,b Shinji Toyota,b Fumio Toda,baDepartment of Chemistry and Materials Science, Tokyo Institute of Technology; bDepartment ofChemistry, Okayama University of Science

The photoreaction of 6-methylcoumarin in solid-state produces four stereoisomeric
dimers in different raitio (the major product is syn-Head-to-Head dimer). However, in the
inclusion complex with trimesic acid, only syn-Head-to-Head dimer is obtained byphotoreaction. In order to investigate this difference of photoreactivities, the crystal structuresof each phase were analyzed.
Since 6-methylcoumarin crystal (1) has high tendency to crystallize in twin form, thecrystal structure was successfully determined by ab initio powder crystal structure analysis. In
the crystal structure, 6-methylcoumarin aligned by 4.73Å parallel translation and dimerization
to the major product of syn-Head-to-Head dimer is well expected(Fig. 1).
The inclusion complex of 6-methylcoumarin and trimesic acid (2) was obtained as
single crystalline form from the ethanol solution. The single crystal analysis revealed thecomplex consists of 1:2:2 of 6-methylcoumarin, trimesic acid, and ethanol molecules. While
the alignment of 6-methylcoumarin in the inclusion complex is favorable for theanti-Head-to-Tail dimer by photoreaction(Fig. 2), however, it is not consistent with the actual
photo-product of syn-Head-to-Head dimer. Desolvation of ethanol from this crystal and thefollowing crystal structure change may explain this inconsistency of photo-reactivity.

P05-127

GUEST EXCHANGE MECHANISM OF ORGANIC INCLUSIONCRYSTAL INVESTIGATED BY POWDER X-RAY DIFFRACTIONANALYSIS
Yasunari Ashida,a Hidehiro Uekusa,a Natsuki Amanokura,b and Masami KanekobaDepartment of Chemistry and Materials Science, Tokyo Institute of Technology, Japanb

Nippon Soda Co., Ltd.

1,1,2,2-tetrakis(4-hydroxyphenyl)ethane, TEP, is an commercially used host molecule
which crystallizes with small guest molecules such as organic solvents. By application ofwater vapor, inclusion crystal of TEP with methanol (1) showed guest exchange phenomenon
and was transformed into TEP with water inclusion crystal (2). Interestingly, TEP is
insoluble to water; therefore the inclusion crystal of 2 is obtained only through the guest
exchange of methanol for water in powder crystalline state. Thus the crystal structure was
successfully determined directly from powder diffraction data (SDPD technique) using direct
space method. The crystal structure has a solvent channel structure and also it is very
similar to that of 1, which are the reason of the easy guest exchange. Heating of bothinclusion crystals of 1 and 2 transformed them into apohost crystal (3), however, the reverse
process, vapor absorption of the apohost, was observed only for methanol inclusion crystal.
The crystal structure of apohost of 3 was also determined from powder diffraction data
indicating that the SDPD technique is very powerful for investigation of this kind of phasetransition process in which single crystal is usually disintegrated.

H2O vapor
MeOH vapor

Methanol (1)Water (2)

heat

heat

MeOH
vapor

Apohost (3)P05-128

HYDROGEN BONDING DYNAMICS OF THE STRUCTURE
4,5-DIMETHYL-N-(2-METHYL PHENYL)-2-{[(1E)-3,4,5-TRIMETHOXYPHENYLMETHYLENE] AMINO} THIOPHENE-3-CARBOXAMIDE.
Vasu,a K. A. Nirmala,b Deepak Chopra,c S. Mohand and J. Saravanan daVivekananda Degree College, Bangalore 560 055, Karnataka, India,
Department of Physics, Bangalore University, Bangalore 560 056, Karnataka, India,c
Solid State and Structural Chemistry Unit, Indian Institute of Science, Bangalore 560 012, Karnataka,
India,dPES College of Pharmacy, Hanumanthanagar, Bangalore 560 050, Karnataka, Indiab

The title compound shows promising antibacterial activity against subtilis aureus,
Escherichia coli compared with Ampicilin. The molecular structure is primarily stabilized byintra-molecular N-H...O interactions forming pseudo-six membered S(6) ring forminghydrogen bonded pattern. The crystal packing is governed by a diverse set of C-H...O
head-tail interactions and π...π interactions. These dimers connected another C-H…O
dimers.
The structure was determined by direct methods using SHELXS-97 and refined to a
final R-value0.045. In the title compound, the geometry of the thiophene ring is planar andis good agreement with the data obtained for thiophene by electron diffraction.
Theortho-toluidine is in the gauche position. The angle between thiophene and ortho-toluidine
is 59.24(2)o. The S-C bond distances are not equal due to π-delocalisation. The methylgroup of the p-methoxy connected to oxygen is not in the plane and is deviated from thephenyl plane by 0.095(1)Ǻ. The methyl groups attached at m-positions point away fromeach other. The inclination angles in the methoxy parts are not equal due to stericenvironment. The bond distances in the methoxy groups agree with values observed in othermethoxy benzene derivatives. The non-planar part of the molecule i.e., ortho-toluidine ischaracterised by the torsion angle 72.84(2)o indicating the conformation of the ortho-toluidine
is bent in the compound.

Fig.

packing diagram.

The dotted lines show C - H…Oandπ-π hydrogen bonds

P05-129

THE PHICIAL PROPERTIES OF S DOPANT IN InP UNDERHIGH-PRESSURE BY ADX AND RAMAN METHDOS
1

1

Yen-Ting Liu , Chih-Ming Lin and Hwo-Shuenn Sheu

2

1

Department of Applied Science National Hsinchu University of Education, Hsinchu 30014,
2
Taiwan; Synchrotron Radiation Research Center, No. 1 R &D Road VI, Hsinchu
Science-based Indust. Park, Hsinchu 30011, Taiwan

Angle-dispersive x-ray diffraction (ADXD) and Raman scattering methods have been
performed for the Sulphur-dopand Indium Phosphide (InP:S) under high-pressure at ambient
temperature. The ADXD results show that possible structure transitions from zinc-blende (B3)
to rock-salt phase (B1) and rock-salt to Cmcm phase for InP:S occur at 8.1 and 22.3 GPa,
respectively. The ambiguous regions in which the B3 and B1 phases and B1 and Cmcm
phases mixed together, exists from 8.1 to 11.3 GPa and from 22.3 to 35.0 GPa for InP:S,
respectively. The unloading run reveals that a reversible phase transition exists in the InP:S
bulk. Raman scattering results show that the structure transitions from zinc-blende to rock-salt
and rock-salt to Cmcm phase occur at 8.3 and 23.0 GPa. The ambiguous regions exists from
8.3 to 15.2 GPa and from 23.0 to 34.4 GPa for InP:S. Those two methods were matched verywell.

P05-130

DIMERIZATION IS IMPORTANT FOR THE GTPASE ACTIVITY OF
CHLOROPLAST TRANSLOCON COMPONENTS ATTOC33 AND
PSTOC159
Yi-Hung Yeh,a,b Muppuru M. Kesavulu, a Hsou-min Li, a Shu-Zon Wu, a Yuh-Ju Sun, b
Emadeldin H. E. Konozy a and Chwan-Deng Hsiao a
School of Molecular and Microbial Sciences and Institute for Molecular Bioscience, University of
Queensland, Brisbane, Australia.

As part of our program on high-throughput crystallography of macrophage proteins, wehave carried out a comprehensive structural and functional characterisation of mouseacyl-CoA thioesterase 7 (Acot7). Acots catalyse the hydrolysis of fatty acyl-CoA to free fatty
acid and coenzyme A and thereby regulate lipid metabolism and cellular signalling. Whileprokaryotic homologues possess a single thioesterase domain, mammalian Acot7 contains apair of domains in tandem. We determined the crystal structures of both the N- andC-terminal domains (1.8 and 2.5 Å resolution, respectively) of the mouse enzyme, and thestructure of the full-length enzyme using a combination of chemical crosslinking, mass
spectrometry, and molecular modelling. The novel quaternary arrangement features a trimerof hotdog fold dimers. We show that both domains of Acot7 are required for activity, that
only one of two possible active sites in the dimer is functional, and identify Asn24 andAsp213 (from N- and C-domains, respectively) as the catalytic residues through site-directedmutagenesis. We also designed an enzyme with higher activity than wild-type Acot7 by
mutating the residues in the non-functional active site. Because Acot7 shows the highest
activity towards arachidonoyl-CoA (a precursor of eicosanoids), is highly expressed inmacrophages and upregulated by pro-inflammatory factors, and its over-expression in
macrophages alters the production of prostaglandins D2 and E2, we propose a role in
inflammatory processes. Together, our results provide a foundation to relate the molecularand cellular functions of Acot7 in macrophages and other mammalian tissues.
Forwood JK, Thakur AS, Guncar G, Marfori M, Mouradov D, Meng W, Robinson J,
Huber T, Kellie S, Martin JL, Hume DA and Kobe B (2007). Structural basis for recruitmentof tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation. Proc Natl
Acad Sci USA 104: 10382-10387

P05-131

EFFECTS OF TERMINAL SUBSTITUENTS AND SEED CRYSTALS ON
THE MODE OF POLYMORPHIC TRANSITION INDUCING
PREFERENTIAL ENRICHMENT
Masahiro Horiguchi, Shinichiro Okuhara, Eiji Shimano, Daisuke Fujimoto, Hiroki Takahashi,
Hirohito Tsue, and Rui Tamura
Graduate School of Human and Environmental Studies, Kyoto University, Kyoto 606-8501, JapanOH
MeIn 1996 we reported the first instance in
H
X
SO
Me
N
O
O R
N
3
which enantiomeric resolution by simple
Merecrystallization of a racemic crystal fromO(±)-2a, X=Me, R=Ph(±)-1a, X=NO2, R=Ph
organic solvents was feasible; this unusual(±)-1b, X=NO2, R=p-FC6H4 (±)-2b, X=Me, R=p-FC6H4
symmetry-breaking enantiomeric resolution(±)-3, X=Cl, R=Ph(±)-4, X=Br, R=Ph
phenomenon regarded as an event of(±)-5, X=I,
R=Ph
complexity system was referred to as
Preferential Enrichment [1].
Crystal, ± 0.0% ee, 1.020 g
Recently we have found a new type of(1st recrystallization)polymorphic transition (γ to α1-form) inducing
Preferential Enrichment for (±)-3~(±)-5 having a 7.2% ee, 0.940 g Crystal, R
Solution, S
phenoxy group at the terminal position of the(2nd recrystallization)
86.1% ee, 0.075 g
ammonium cation (Figure 1) [2]. Here we report(i) the mode of polymorphic transition with respect
Crystal, S 3.8% ee, 0.829 g
Solution, R
to the novel terminal phenoxy derivatives (±)-1a(3rd recrystallization)and (±)-2a and the p-fluorophenoxy ones (±)-1b 89.8% ee, 0.108 mg
and (±)-2b, and (ii) the effects of seed crystals of 6.9% ee, 0.740 g Crystal, R
Solution, S(±)-2a and (±)-2b on the Preferential Enrichment(4th recrystallization)
89.1% ee, 0.085 g
of (±)-1 and (±)-2 (Table 1). (±)-1a, (±)-1b, and(±)-2b showed Preferential Enrichment, whereas
Crystal, S 3.6% ee, 0.654 g
Solution, R(±)-2a failed to do so. In this case, addition of the
α1-form seed crystals of (±)-2b to the 91.2% ee, 0.077 g
supersaturated EtOH solution of (±)-2a induced Figure 1. Preferential Enrichment of (±)-4 in EtOH.
the Preferential Enrichment of (±)-2a.
Table 1. Induction or inhibition of Preferential
Enrichment by seeding for (±)-1 and (±)-2.
Seed crystal b
Solubility
Withoutain EtOH (mg/mL)
seeding(±)-2a (μ-form)(±)-2b (α1-form)ceyes
inhibition
restraint f(±)-1a6.1(μ) g(γ to α1 and μ) d
(α1) gceyesinhibition
restraint f(±)-1b1.9dg(γ to α1)(μ)(α1) ghhno effect
induction ino(±)-2a2.0(γ to μ) d(μ) g(α1) gceyesinhibition
inhibition e(±)-2b4.9dg(γ to α1)(α1) g(μ)
ab
Recrystallization was carried out without
seed crystals. 5 wt% of seed
crystals were added. cdePreferential Enrichment occurred. Modeof polymorphic transition. Preferential Enrichmentg
was completely inhibited by seeding. f Preferential
Enrichment was restrained by seeding.
Polymorphic form of the deposited crystals. h Preferential Enrichment did not occur. i
Preferential Enrichment was induced by seeding.

Reference:[1] Top. Curr. Chem. 2007, 269, 53-82.
[2] Cryst. Growth Des. in press.

P05-132

STRUCTURE-ASSISTED DISCOVERY OF HELICOBACTER PYLORISHIKIMATE KINASE (HpSK) INHIBITORS
Wen-Chi Chenga, Yen-Fu Chenb, Jinn-Moon Yangb and Wen-Ching Wangaa

Institute of Molecular and Cellular Biology and Department of Life Science, National Tsing Hua

University; bDepartment of Biological Science and Technology, Institute of Bioinformatics, National
Chiao Tung University, Hsinchu, Taiwan, 300, R.O.C.

Helicobacter pylori, a Gram-negative bacterium, colonizes in approximately half ofhuman population, induces chronic inflammation in gastric epithelial cells, and may further
develop into various gastrointestinal diseases such as peptic ulcers and gastric cancer.
Shikimate pathway plays an important role in aromatic amino acid biosynthesis in bacteria,
fungi, and plants, but not mammals, in which enzymes of this pathway represent attractive
targets for the development of new antimicrobial agents, herbicides and antiparasitic agents.
We have determined the structure of the fifth enzyme, shikimate kinase (HpSK) that catalyzes
the specific phosphorylation of the 3-hydroxyl group of shikimic acid in the presence of ATP
in its apo form (1.8 Å) and the HpSK·shikimate·PO4 (2.3 Å) binary complex structures. The
binary structure reveals induced fit movement on substrate binding and the detailed
enzyme-substrate interactions. Several highly conserved charged residues including Asp33 (ina conserved Asp31Thr/Ser32Asp33 motif), Arg57, and Arg132 (interacting with shikimate)
are identified, guiding the development of novel inhibitors of shikimate kinase. We havecurrently conducted virtual drug screening utilizing the DOCK4.0 and GEMDOCK moleculardocking tool among compounds of ZINC database which is a free database from University ofCalifornia, San Francisco. Top hits obtained from DOCK4.0 were additionally filtered with
GEMDOCK. Several molecules were identified that inhibited the HpSK activity with IC50
values in the micromolar range.

P05-133

AB INITIO STRUCTURAL DEFERMINATION OF
PHARMACEUTICAL COCRYSTAL FROM POWDER X-RAY
DIFFRACTION DATA
Chihiro Itogaa, Kotaro Fujiia, Hidehiro Uekusaa, Noriyuki Takatab, Koji ShirakibaDepartment of Chemistry and Materials Science, Tokyo Institute of Technology, bChugai

Pharmaceutical Co.Ltd .

The solubility and other properties of pharmaceutical compounds can be controlled byforming cocrystals with small molecules. Because the solubility of compounds relates to themolecular structure and interactions in the crystal, the crystal structure information is the mostimportant to control the solubility and other properties. Also, pharmaceutical compounds
usually obtained and handled in poly-crystalline form. Thus the crystal structure analysis
should be performed to the powder crystals without recrystallization using ab initio structure
determination from powder X-ray diffraction data.
The powder cocrystal of spironolactone (a), which is hypotensive and diuretic medicine,and the saccharin (b), which is artificial sweetener, was obtained from water solution. Powder
X-ray diffraction data were collected in SPring-8, BL19B2, and the structure determination
was performed by direct space method, using simulated annealing optimization. The
crystallographic data for the cocrystal are monoclinic, space group C2 with a=25.2550,
b=6.4045, c=23.4824Å, β=126.1552°, and V=3066.73Å3, T=298K. Rietveld refinement was
performed using the best solution of the simulated annealing calculation. The bond length andangles are restrained to it’s own crystal structure reported in CSD.
There is an intermolecular H-bond, N-H…O in cocrystal between N atom in Saccharin
and O atom in spironolactone carbonyl. Both N-H…O and C-H…O H-bond make eachmolecule stacked along b axis to form a column structure. Because of these intermolecularinteractions, the solubility was decreased in cocrystal comparing with spironolactone crystal.

(a)(a) spironolactone ,(b)(b) saccharin

crystal structureP05-134

PROBING INTER MOLECULAR INTERACTIONS IN
FUNCTIONALISED THIOPHENES
K.A.Nirmala a, Vasu baDepartment of Physics, Bangalore University, Jnanabharathi, Bangalore-560056.

b

Department of Physics, Vivekananda Degree College, Malleshwaram west, Bangalore-560055.

Probing inter molecular interactions in functionalised 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 conformational studiesof 2-amino thiophenes, and Schiff bases of thiophenes, which serves as a starting materials
for number 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 experimental steps consist of growing single crystals by slow evaporation methodby selecting the right solvents. After careful examination under polarising microscope(for transparent crystals) suitable crystal is selected which is free from defects such as
twinning or cracks and it is mounted on the single crystal diffractometer equipped with
SMART APEX CCD. The crystal structures were solved using SHELXS97 program, andrefined using SHELXL97 program. Molecular and packing diagrams were generated by
ORTEP32. The geometric calculations were done using PARST.
The structural comparisons of all the thiophene compounds are as follows: There arecertain similar and dissimilar molecular and crystal packing features are described among
2-amino thiophene derivatives and Schiff bases of thiophene derivatives. The thiophenemoiety is planar in all the compounds. It is noticed that from the comparative study that theconformation of the six-membered ring does not make any change from the half-chairconformation with different substituents. Strong intra-molecular interations which locks themolecular conformation is observed in all the compounds. In addition to this the presenceof intermolecular interactions within the crystal lattice is influencing the packing of themolecules which modifies the properties.

P05-135

MOLECULAR RECOGNITION OF SYNEPHRINE BY CHIRALORGANIC ACIDSTaira Kimino,a Yukio Takahashi, b and Isao FujiiaaDepartment of Biological Sci. and Tech., Tokai Univ, Japan,b Daito Chemical Co., Ltd, Japan

Production of optically active aminoalcohols and amines, such as ephedrine and1-phenylethylamine [PEA], has a great importance in the pharmaceutical industry. PEA is
one of intermedicines and ephedrine has a variety of potent bioactivities, e.g. adrenergic
activity. On the other hand, an aqueous solution of racemic compound and optically pure
ephedrine has been widely applied in the diastereomer salt separation. One of such alkaloids,
synephrine [SYN], systematic name: 4-(1-hydroxy-2-(methylamino)ethyl)phenol, is lower
toxic and natural product without law control. The racemic compound was also found in
citrus commonly. 1),2) The enantiomers were considered to be potentially chiral resolution
agents.
In this study, we focus on the molecular-recognition mechanism of SYN and
optically-active organic acids. The complexes of rac-SYN and (1R, 2R)-tartrate [R-TART],and rac-SYN and S-ibuprofen [S-IBU] were examined by X-ray analysis. From the limited
information, the SYN molecules recognize the chiral carboxy groups by its amino-ethernol
group and p-hydroxy group in the columnar hydrophilic region with intermolecular hydrogenbonds. Two independent S-IBU molecules in the asymmetric unit are almost identical, but
the difference between the enantiomers of rac-SYN mainly existed at the torsion angles ofaminoethane moiety. This tendancy was also found in R-TART complex. It reveals that themolecular recognition system of chirality differs in the diastereomer.
Reference:
1) M. Datta et. al, Acta Cryst. (1994), C50, 1132-1135.
2) M. Sajid et. al, Acta Cryst. (2005), E61, o2534-o2536.

OH
∗

Me

COOH

NH

HO

OH
∗

S-IBU

HO

rac-SYN

COOH

NH
HOCO

HO

rac-SYNMeOH

R-TARTP05-136

CRYSTAL STRUCTURE OF
2-PHENYL-2,3-DIHYDRO-4H-CHROMEN-4-ONE
Nongnaphat Khosavithitkul,a Kenneth J. Hallerbab

The Centre for Scientific and Technological Equipment; School of Chemistry, Institute of Science,
Suranaree University of Technology, Nakhon Ratchasima 30000 Thailand
E-mail: nkhosavithitkul@yahoo.com

Flavonoids are a group of polyphenolic compounds of low molecular weight that
present a common benzo-γ-pyrone structure. They occur naturally in fruits, vegetables, nuts,
seeds, flowers, and bark. They are categorized into various subclasses including flavones,
flavonols, flavanones, isoflavanones, anthocyanidins, and catechins. Their various properties
make them attractive for applications in the pharmaceutical, cosmetic and nutrition fields.
They are pharmacologically active, and some are currently used in a wide range of medical
preparations, including antibacterial, antiviral, anti-inflammatory, and vasodilatory
preparations.
The crystal structure of the title compound was determined by single crystal X-ray
analysis. Data were collected on a Nonius KappaCCD diffractometer equipped with a fine
focus molybdenum X-ray source, and a 0.3 mm ifg capilliary collimator. Structure solution
and refinement utilized SIR97, MaXus, and the SHELXTL system.
Crystal data: C15H12O2; Mr = 224.26 Daltons; transparent colorless; monoclinic; P21/n(No.14); a = 10.611(5), b = 5.531(5), c = 19.362(5) A, V = 1136.32 A3; Z = 4; Dcalc = 1.230
Mgm-3; λMoKα = 0.71073 A; μ = 0.9 cm-1; T = 298(2) K. 16,476 data collected, Rint = 0.0752
1068 unique data.

P05-137

CRYSTAL STRUCTURE OF‘N-(4-METHOXYPHENYL)-2-{[(1E)-(4-METHYLPHENYL)
METHYLENE]AMINO}-4,5,6,7-TETRAHYDRO-THIENO[2,3-C]PYRIDI
NE-3-CARBOXAMIDE’
G. N. Anilkumar a, M. K. Kokila b, Puttaraja b, S. Mohan C and J. Saravananc.
aDepartment of Physics, M. S. Ramaiah Institute of Technology, MSRIT Po, Bangalore, Karnataka.

560054. b Department of Physics, Bangalore University, Bangalore, Karnataka.

560056.

c

PES

College of Pharmacy, Hanumanthanagar, Bangalore, Karnataka. 560050.
e-mail: anilkumargn@gmail.com

The title compound, is one of the series of is one of a series of 3-arylcarboxamides andwas found to exhibit antibacterial and antifungal activities. Various derivatives of thiophenes
and Schiff bases are known to possess different biological activities, such as antitubercular,
bacteriostatic and antifungal activities. Sulfur containing Schiff bases are the most effective.
The compound C24H25N3O2S, crystallizes under Triclinic system, Pī space group, a =8.3905 (11) Å, b = 9.9883 (13) Å and c = 12.9549 (17) Å, α = 91.375 (2)º, β = 94.789 (3)º, γ =96.121 (2)º, V = 1075.2 (2) Å3, Z= 2, µ = 0.18 mm−1, & D= 1.296 Mgm-3.
The three dimensional intensity data were collected using Bruker Smart CCD
diffractometer using graphite monochromated MoKα radiation. The data of the compound wascorrected for LP factors and used for structure solution. The structure was solved using
SHELXS-97 program and and refined using full-matrix least squares on F2 to an R value of
0.085 using SHELXL-97 Program for 2645 reflections with I>2σ(I). The geometry, modeof packing and the hydrogen bonds of the compound will be presented and discussed.

P05-138

CRYSTAL STRUCTURE OF‘N-(4-METHOXYPHENYL)-2-{[(1E)-(4-METHYLPHENYL)
METHYLENE]AMINO}-4,5,6,7-TETRAHYDRO-THIENO[2,3-C]PYRIDI
NE-3-CARBOXAMIDE’
G. N. Anilkumar a, M. K. Kokila b, Puttaraja b, S. Mohan C and J. Saravananc.
aDepartment of Physics, M. S. Ramaiah Institute of Technology, MSRIT Po, Bangalore 560056,

Karnataka, India. b Department of Physics, Bangalore University, Bangalore 560056 Karnataka,
India.

cPES College of Pharmacy, Hanumanthanagar, Bangalore 560050, Karnataka, India.

e-mail: anilkumargn@gmail.com

The title compound is one among the series of 3-arylcarboxamides and was found to
exhibit antibacterial and antifungal activities. Various derivatives of thiophenes and Schiffbases are known to possess different biological activities, such as antitubercular, bacteriostaticand antifungal activities. Sulfur containing Schiff bases are the most effective.
The compound C24H25N3O2S, crystallizes under Triclinic system, Pī space group, a =8.3905 (11) Å, b = 9.9883 (13) Å and c = 12.9549 (17) Å, α = 91.375 (2)º, β = 94.789 (3)º, γ =96.121 (2)º, V = 1075.2 (2) Å3, Z= 2, µ = 0.18 mm−1, & D= 1.296 Mgm-3.
The three dimensional intensity data were collected using Bruker Smart CCD
diffractometer using graphite monochromated MoKα radiation. The data of the compound wascorrected for LP factors and used for structure solution. The structure was solved by Patterson
technique using SHELXS-97 program and refined using full-matrix least squares on F2 to an
R-value of 0.085 using SHELXL-97 Program for 2645 reflections with I>2σ(I).
The
conformation, mode of packing and the hydrogen bonding geometry of the compound will bepresented and discussed.

P05-139

CRYSTAL CHEMISTRY OF CYCLODEXTRINS AND THEIRINCLUSION COMPOUNDS WITH BIOLOGICALLY-ACTIVE GUESTS
Mino R Caira
Department of Chemistry, University of Cape Town, Rondebosch 7701, South Africa

Results of our recent studies of the crystal chemistry of cyclodextrins (CDs) and their
inclusion compounds are described under three headings, namely structures andconformations of sterically crowded host compounds, the isolation and structuralcharacterization of multiple crystalline forms of individual CD inclusion complexes, andnovel modes of inclusion of biologically-active molecules in both native and derivatised CDs.
Chemical modification of native CDs (e.g. alkylation/acetylation of their hydroxyl
groups) has a dramatic effect on their structures and conformations. ‘Self-inclusion’ ofsterically bulky substituents may render these modified hosts unsuitable for inclusion of
sizeable guest molecules. The structures of representative examples of such host molecules
are compared with those of previously reported analogues and their limited extent of guest
inclusion is illustrated.
Variation of crystallization conditions can give rise to different crystal forms of a CD
inclusion complex. This was reported earlier for the β-CD inclusion complex of methyl
paraben, where a triclinic and a monoclinic crystal form with the same 1:1 host-guest
stoichiometry were isolated and structurally characterized. An important feature of thesecomplexes is the significant difference in their thermal stabilities. This has obvious
implications for crystallization control in the production of CD inclusion complexes,
especially those of pharmaceutical relevance. Our recent studies indicate that, as in theconventional generation of polymorphs, the chances of isolating multiple forms of a given
inclusion complex may be significantly enhanced by systematic variation of thecrystallization conditions,
Accurate prediction of the mode of inclusion of a given guest in a CD host molecule is
not yet possible and the empirical approach often yields novel findings in this regard.
Representative structures of CD inclusion complexes containing antibacterials,
anti-hypertensives and potential anti-cancer agents are described to illustrate some of thediversity of inclusion modes observed in the solid state. Guest disorder may prevent
satisfactory structural elucidation even from X-ray data recorded at relatively low
temperatures. However, examples are presented in which more than two disordered guest
components have been successfully modelled within their CD host cavities.
While the focus in this presentation is on single crystal X-ray studies, the utility ofcomplementary techniques such as powder X-ray diffraction and thermal analysis in theinvestigation of these compounds is also illustrated.

P05-140

CRYSTAL STRUCTURE OF‘2-AMINO-N-(2-METHOXYPHENYL)-5,6,7,8-TETRAHYDRO-4H-CYC
LOHEPTA[B]THIOPHENE-3-CARBOXAMIDE’
K. Chandra Kumar a, M. K. Kokilab, Puttaraja b, S. Mohan C and J. Saravananc.
aDepartment of Engineering Physics, HKBK College of Engineering, Nagawara, Bangalore 560 045,

Karnataka, India. b Department of Physics, Bangalore University, Bangalore 560056, Karnataka,
India.

cPES College of Pharmacy, Hanumanthanagar, Bangalore 560050, Karnataka, India.

Schiff bases and various derivatives of thiophenes are known to possess different
biological activities, such as antitubercular, bacteriostatic and antifungal activities. Sulfur
containing Schiff bases are the most effective. The title compound shows above mentioned
properties.
The compound C17H20N2O2S, crystallizes under Monoclinic system, P21/n space group,a = 9.228(2) Å, b = 8.413(2) Å and c = 20.839(5) Å, β = 95.798(4)º, V = 1609.5(6) Å3, Z= 4,µ = 0.210 mm−1, & D= 1.306 Mgm-3.The three dimensional intensity data were collectedusing Bruker Smart CCD diffractometer using graphite monochromated MoKα radiation. The
data of the compound was corrected for LP factors and used for structure solution. The
structure was solved using SIR92 program and refined using full-matrix least squares on F2
to an R value of 0.0510 using SHELXL-97 Program for 2238 reflections with I>2σ(I).
The structural details of the compound will be presented and discussed.

P05-141

HIGH RESOLUTION, HIGH THROUGHPUT X-RAY POWDERDIFFRACTION EXPERIMENTS AND DATA ANALYSIS
A. Stefanovic, D. Beckers, T. Degen, S. Prugovečki
PANalytical B.V., Almelo, The Netherlands

Advances in X-ray optics, detector technology and software enabled new application
areas that previously were not feasible on a laboratory powder diffractometer. Until recently,
e.g. XRPD experiments on small sample amounts were either time consuming or needed to be
performed with compromises in resolution, limiting the information content that could be
extracted from the data.
New optical modules - like the focusing X-ray mirror - and new stages that can be
added to modular systems now allow to optimize the optical configuration for a particularsample – and not vice versa. With these new options in particular high resolution, highthroughput X-ray powder diffraction comes within reach of laboratory instrumentation.
Samples coming from high throughput crystallization experiments, typically only
available in small amounts, can now be measured with drastically enhanced speed withoutcompromising the resolution. High quality data can be obtained either in transmission orreflection geometry. Optimal instrument configurations, measurement strategies and data
treatment tools will be discussed on pharmaceutical examples.

P05-169

RNA DEGRADATION BY ESCHERICHIA COLI POLYNUCLEOTIDEPHOSPHORYLASE
Zhonghao Shi,a,b Wei-Jen Yang,b Kin-Fu Chaka and Hanna S. YuanbaInstitute of Biochemistry and molecular Biology, National Ying-Ming UniversitybInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan

RNA degradation is an important biological process in regulating mRNA levels in cells.
In eukaryotes, a protein complex, exosome, plays a major role for mRNA degradation incytoplasm. The bacterial trimeric polynucleotide phosphorylase (PNPase) shares similar
sequence and domain organization and bears similar function in mRNA degradation to that ofeukaryotic exosome. We determined the crystal structure of E. coli PNPase at a resolution 2.7
Å. PNPase, containing two RNase PH domains and a S1/KH domain, forms a trimer. The six

RNase PH domains of the trimeric PNPase fold into a ring-like structure containing a central
channel for RNA binding and degradation. This ring-like architecture of bacterial PNPase issimilar to those of archeal and human exosomes, supporting the hypothesis that a common
mechanism for RNA degradation is used in all kingdoms of life. We also found that thewild-type PNPase produces a final end product of 4-nucleotide RNA.

However, a R106A

mutant and a S1/KH domain truncated PNPase produce different RNA end products,
indicating that R106 located inside the channel and S1/KH domain are likely involved in
RNA recognition.

P05-170

UNDERSTANDING OF D-STAGGER IN COLLAGEN FIBERS BASEDON THE 7/2-HELICAL STRUCTURE AND AMINO ACID SEQUENCE
Koichi Masakiyo, Tatsuya Kawaguchi and Kenji Okuyama
Department of Macromolecular Science, Graduate School of Science, Osaka University,
Toyonaka, Osaka, 560-0043, Japan
Collagen is the most abundant protein in animals, responsible for structural integrity intheir bodies. It is composed of three polypeptide chains containing more than 1000 aminoacid residues, and has a triple helical structure. Since each polypeptide chain requires Gly at
every third position, the amino acid sequence of collagen can be designated by (Gly-X-Y)n, in
which the X and Y positions are frequently occupied by Pro and Hyp, respectively. During
these five decades, the molecular structure of collagen was believed to be the 10/3-helicalstructure (the Rich & Crick model). Recently, we reported that both the 7/2- and 10/3-helicalmodels could explain quantitatively the fiber diffraction data from native collagen (Okuyama,
et al., Biopolymers 2006). On the other hand, all the conformations found in single crystalsof collagen-model peptides showed 7/2-helical symmetry rather than 10/3-helical one(Okuyama, et al., Biopolymers 2006). Based on these evidences it is now clear that the
average conformation of collagen is the 7/2-helical structure.
In the fiber-forming collagen, like type I, II and III collagen, molecules spontaneously
associate in a specific way to form fibers in the extracellular matrix. These fibers exhibit
cross striations every 670 Å (= D) in electron microscopic observations and also a series of
meridional Bragg reflections in X-ray small angle diffraction based on this period. Although
this period was explained by the D-stagger of collagen molecules along the molecular axis
(Figure 1), there is no clear explanation why they assemble with this stagger based on theamino acid sequence. In other words, we do not know the specific interaction between
adjacent molecules which cause this D-stagger. In this study we examined electrostaticinteractions between source and target molecules to understand the origin of the D-stagger.
The amino acid sequence of α1(II) chain of the human type II collagen was used in thisanalysis. Charged residues were supposed to have +1 or -1 charge on their Cβ atom as a first
approximation. Collagen molecules were constructed from three such peptide chains byapplying 7/2-helical symmetry. Staggering the source molecule 5 residues at a time,electrostatic energy between source and target molecules was calculated. The local minimumof energy was found at the 1D-stagger (= 235 amino acid residues), which showed that theelectrostatic interaction is one of important driving forces for the D-stagger in collagen fiber.

D

3000 Å

P05-171

X-RAY CRYSTAL STRUCTURE ANALYSIS OF HEMOGLOBIN FROMDOMESTIC PIGEON (COLUMBA LIVIA) AT 1.44Å RESOLUTION
P.Charles1, K.Neelagandan1, S.Sundaresan1, Jürgen J. Müller2, Udo Heinemann2 and
M.N.Ponnuswamy1*
1

Department of Crystallography and Biophysics, University of Madras

Guindy Campus, Chennai-600 025, India,
e-mail: mnpsy2004@hotmail.com1*
2

Max-Delbrück-Center for Molecular Medicine,Department of Crystallography

Robert-Rössle-Straße 10, D-13122 Berlin, Germany

Hemoglobin is an oxygen carrier protein in the red cells of the blood in mammals andother animals. The oxygen binding properties of hemoglobin are regulated by binding ofallosteric effectors. The data were collected at 1.44 Å resolution using synchrotron radiation
at BESSY, Germany. Crystals of pigeon hemoglobin belong to the orthorhombic space group
P212121 with cell dimensions: a = 81.086 Å, b = 81.543 Å, c = 79.214 Å. The structure
solution was carried out by molecular replacement method using graylag goose hemoglobin
as the starting model (PDB id: 1FAW) using the program AMORE implemented in CCP4 suite.
The structure refinement was done using REFMAC 5.0. About 5% of the reflections wereused for the test set. The resultant model obtained from the structure solution was subjected to
20 cycles of rigid body refinement, which led to an R-factor of 37.7% (R free=38.1%). At thisstage restrained refinement was carried out and the final R-factor converged to 19.6% (Rfree=
23.4%). The detailed results will be presented.

P05-172

SMALL-ANGLE X-RAY SCATTERING EXPERIMENTS TO
DETERMINE THE STRUCTURAL TRANSITIONS IN THE INSULIN
RECEPTOR ECTODOMAIN UPON INSULIN BINDING
Andrew E. Whitten,1 Jill Trewhella2, Colin W. Ward3 and Michael C. Lawrence3
1

Bragg Institute, ANSTO, Australia, 2Department of Biochemistry, University of Sydney, New South

Wales, Australia; 3Walter and Eliza Hall Institute of Medical Research, Parkville, Australia.

The human insulin receptor (hIR) is a disulphide-linked homodimeric tyrosine kinase(TK) receptor. The crystal structure of the apo form of the hIR ectodomain has recently been
determined to 3.8 Å resolution (McKern et al., Nature, 2007) and revealed the ectodomain tohave an inverted “V” structure with two-fold symmetry. Each leg of the inverted “V” iscomposed of the L1, CR and L2 domains of one monomer juxtaposed against the FnIII-1,
FnIII-2 and FnIII-3 domains of the other monomer (domain nomenclature is described in
Adams et al., Cell Mol. Life Sci., 2000). The C-termini of the FnIII-3 domains lie at base of
the legs of the inverted “V”, poised to extend through the cell membrane towards theintracellular TK domains. The structure revealed, importantly, that the L1 and FnIII-1
domains, both known to be involved in hormone binding, are juxtaposed in such a way that
insulin can bind with its dimer-forming face interacting with L1 and elements of its
hexamer-forming face interacting with the C-terminal loops of FnIII-1.
However, nothing is known about the conformational changes that occur in hIR uponinsulin binding and how these effect signalling, and we are thus seeking to investigate theseby small-angle X-ray scattering (SAXS) from the hIR ectodomain in solution. As part of thisstudy, we are investigating the extent to which simulated, one-dimensional SAXS data
derived from the crystal structure of the ectodomain is capable of yielding an adequately
unique reconstruction of the three-dimensional shape of the particle. We have shown that theectodomain particle is mono-dispersed in solution and have thus begun SAXS studies of thehIR ectodomain to investigate whether the solution structure agrees with the crystal structure.
The final task is to determine from SAXS data the structural transitions in the hIR ectodomain
upon complexation with insulin. Progress towards these goals will be presented.

P05-173

CRYSTAL STRUCTURE OF THE HUMAN FOXO3A-DBD/DNACOMPLEX SUGGESTS THE EFFECTS OF POST-TRANSLATIONALMODIFICATION
Kuang-Lei Tsai,a,b Yuh-Ju Sun,b Cheng-Yang Huang,a Jer-Yen Yang,c Mien-Chie Hungc andChwan-Deng HsiaoaaInstitute of Molecular Biology, Academia Sinica, Taipei, 115, TaiwanbInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300,

Taiwanc

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
in multiple 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.

P05-174

CRYSTAL STRUCTURE OF HUMAN TUDOR-SN AND IMPLICATIONOF ITS ROLES IN RNA INTERFERENCE
Chia-Lung Li and Hanna S. Yuan
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan, R.O.C.

The human Tudor-SN (also called p100) is a multiple function protein. So far Tudor-SN
has been reported to function as a transcriptional co-activator, participate in RNA interference
silencing complex assembling and hyper-edited microRNA cleavage. Although extensivefunctional studies have been carried out, the structure and domain arrangement of Tudor-SN
is unknown. The structural based analysis of Tudor-SN is thus imperious for better
understanding of the role of this protein in RNA interference and transcription activation.
We crystallized a stable 70-kD truncated form of human Tudor-SN and solved thestructure by MAD method at a resolution of 1.9 Å. X-ray diffraction data were recorded at the
Taiwan beamline BL-12B in SPring-8. The overall Tudor-SN structure contains three intact
SN domains (SN3, SN4 and SN5) and one Tudor domain which is a insertion domain between
second and third β-strands of SN5. Superposition of Tudor-SN with staphylococcal nucleaseshows that some of the important active site residues of SN3 and SN4 domains are missing,indicating that some of the SN domains, including SN4, may not be active in RNA cleavage.
Structural superposition of the OB fold in the SN domain of Tudor-SN with the OB-foldstructure of Sac7d/DNA complex reveals a substrate binding cleft located between SN3 andSN4 interface. We suggest that SN3 domain is likely responsible for RNA cleavage and SN4
domain is likely involved in substrate binding but not in cleavage. These results are consistent
with the activity assays for different truncated forms of Tudor-SN in RNA cleavage. In
conclusion, the structural analysis of Tudor-SN suggests a coordination between two SN
domains in RNA binding and cleavage and provides some clues for further functional
investigations.

P05-175

CRYSTAL STRUCTURE OF DNAC REPLICATIVE DNA HELICASEREVEALS THE MECHANISM OF HEXAMERIZATION AND
POSSIBLE PROTEIN-PROTEIN INTERACTIONS NETWORKCheng-Yang Huang, Kuang-Lei Tsai, Wei-Ti Chen, Chwan-Deng Hsiao
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan, Republic of China

Helicases are motor proteins which play an essential role in DNA replication,
recombination, and transcription. The GK3476 gene encoding a replicative DNA helicase(GkDnaC helicase) of Geobacillus kaustophilus HTA426 is a hexameric ring helicase
belonging to the AAA+ family. DnaC helicase can interact with several proteins required for
DNA replication, such as DnaA initiator protein, DnaI helicase loader protein, and DnaG
primase. Here, we cloned, overexpressed, purified, crystallized, and determined the crystal
structure of DnaC helicase at 3.6 Å resolution. Unlike other crystal structures of hexamerichelicase, the six monomers of the DnaC helicase adopt predominantly a 3-fold symmetricmorphology (trimer of dimers) to the hexameric ring, made by forming a four-helix bundle inthe cooperation between the two N-terminal regions (residues 110-150) of the dimer, and thus
creates three significant holes on the surfaces of DnaC helicase. The orientation and positionof the RecA-like helicase domains are almost identical. However, the N-terminal domaininteracting modes with the helicase domain are different. Based on this crystal structure of fulllength version of DnaC helicase, we renew the hexamerization mechanism of replicative
helicase and propose the interaction regions of DnaC helicase for DnaA, DnaI, and DnaG
binding. This study provides a molecular insight into why DnaC helicase can not unwind
double-stranded DNA in the absence of the N-terminal domain and may contribute to anunderstanding of the protein-protein interactions map in DNA replication.

P05-176

PYROCOCCUS HORIKOSHII ARGINYL-TRNA SYNTHETASELACKING ADDITIONAL N-TERMINAL DOMAIN WITH
AMINOACYLATION ACTIVITY
Emiko Uchikawa,a Shun-ichi Sekine,b Shigeyuki Yokoyama,b and Michiko KonnoaaDepartment of Advanced Sciences, Chemistry and Biochemistry course, Graduate School of
Humanities and Sciences, Ochanomizu University, 2-1-1 Otsuka, Bunkyo-Ku, Tokyo 112-8610, Japan;b
The Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo,
Hongo, Bunkyo-Ku, Tokyo 113-0033, Japan.

Since there are six kinds of codons (CGX (X stands for U/C/A/G), AGA, AGG) for
arginine, and arginyl-tRNA synthetase (ArgRS) has the additional N-terminal domain, ahypothesis that the recognition of tRNAArg is determined mainly by the interaction between
20th base of D-loop of tRNA and N-terminal domain on ArgRS has been believed. On theother hand, in the aminoacylation reaction for tRNA of N106A and G111A mutants yeast
ArgRS substituted to Ala of Asn106 and Gln111, which D20 base of the D-loop of tRNA
(ICG) was observed to have contacts with in crystal structure, it was revealed that Km andkcat values of these mutant ArgRSs are the same as that of wild type ArgRS and theinteraction between the N-terminal domain and D loop of tRNA is not required in theaminoacylation reaction [1]. The main codon usages of Arg are CGX for E. coli, CGG/AGG
for T. thermophilus and CGX/AGA/AGG for yeast and distribution of usage is broad for these
species, whereas for Pyrococcus horikoshii (Ph), codons of AGA and AGG occupy 98 % of
Arg codon usage. Therefore, we selected tRNA with anticodon CCU and determined the
crystal structure of the ternary complex of Ph ArgRS, Ph tRNAARG (CCU) and AMP-PNP
with Rfactor = 0.22 (Rfree = 0.26) at 2.0 Å resolution. It was observed that in this complex, thebase of A20 of D loop of tRNA stacks on the aromatic ring of the side chain of Tyr85 andforms hydrogen bonds with Asn87 in the last β-strand in the N-terminal domain. In order toclarify the role of the N-terminal domain, we constructed Ph ArgRS (92-629 residues) lacking
the N-terminal domain and measured kinetic parameters in the aminoacylation reaction formutant ArgRS and wild type ArgRS. For wild type ArgRS, kcat and Km values for tRNA are
0.075 s-1 and 3.3 μM at 100 mM HEPES-NaOH buffer pH 7.5, respectively and for mutant
ArgRS, those are 0.006 s-1 and 13 μM at the same buffer and 0.013 s-1 and 5.1 μM at 100 mM
trisHCl buffer pH 8.0, respectively. This indicates that the fixing of tRNA by the N-terminal
domain is not essential in the aminoacylation reaction. We obtained also sensitive crystals of acomplex of mutant ArgRS and tRNA from solution containing 2 % PEG and 2.0 M
ammonium sulfate.
Reference:[1] R. Geslain, G. Bey, J. Cavarelli & G. Eriani, Biochemistry 2003, 42, 15-92-15101.

P05-177

CRYSTAL STRUCTURE OF 5-METHYLTHIORIBOSE 1-PHOSPHATEISOMERASE PRODUCT COMPLEX FROM BACILLUS SUBTILIS:IMPLICATIONS FOR CATALYTIC MECHANISMHaruka Tamuraa, Yohtaro Saitob, Hiroki Ashidab, Tsuyoshi Inouea, c, Yasushi Kaia, Akiho
Yokotab, and Hiroyoshi Matsumuraa, caDepartment of Applied Chemistry, Osaka University, Suita, Japan; bDepartment of Molecular biology,

Nara Institute of Science and Technology (NAIST), Ikoma, Japan; cCREST (Sosho Project), JST, Suita,
Japan

Methionine salvage pathway (MSP) plays an important role in recycling the methylthio
moiety of methylthioadenosine into methionine. Recently, the genes and reactions in MSP
from Bacillus subtilis have been identified, where 5-methylthioribose 1-phosphate isomerase(MtnA) catalyzes a reversible conversion of 5-methylthioribose 1-phosphate (MTR-1-P) to
5-methylthioribulose 1-phosphate (MTRu-1-P). According to Pfam database, MtnA belongs
to a superfamily of translation initiation factors.
Herein, we report the crystal structures of B. subtilis MtnA (Bs-MtnA) in complex with
its product MTRu-1-P, and a sulfate at 2.4 and 2.7 Å resolution, respectively. The electron
density clearly shows the presence of each compound (MTRu-1-P and sulfate) bound to theactive site. Bs-MtnA exhibits a Rossman-fold (αβα-sandwich) and forms a homo-dimer.
The three-dimensional structure of MtnA product complex and the structuralcomparison with MtnA homologous proteins suggest an open/close transition as well as novel
catalytic mechanism. The several highly conserved residues in the active site, namely Arg94,
Cys160 and Asp240 are most likely involved in catalysis. The details of the catalytic
mechanism will be proposed and discussed.

P05-178

STRUCTURAL DIFFERENCE BETWEEN RICE AND RED ALGARUBISCO COMPLEXED WITH SULFATE
Yasuhiro Komuraa, Hiroyoshi Matsumuraa, d, Hiroyuki Ishidac, Hiroki Ashidab, Eiichi
Mizohataa, Tsuyoshi Inouea, d, Amane Makinoc, Tadahiko Maec, Akiho Yokotab, Yasushi Kaiaa

Department of Applied Chemistry, Osaka University, Suita, Japan; bDepartment of Molecular biology,

Nara Institute of Science and Technology (NAIST), Ikoma, Japan; cDepartment of Applied Plant
Science; Tohoku University, Sendai, Japan, dCREST (Sosho Project), JST, Suita, Japan

Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1.39) catalyzes the
addition of gaseous CO2 to ribulose 1,5-bisphosphate (RuBP) and produces two molecules of
3-phosphoglycerate (3-PGA). The carboxylation of plant Rubisco is the rate-limiting step ofphotosynthesis due to the following reasons. First, Rubisco has an extremely slow rate ofcatalysis with a very low turnover rate (3-4 / seconds per active site). Second, the enzyme
cannot exert its maximum ability to fix CO2, since the concentration of CO2 in the stroma issmaller than the Michaelis constant (Km) for CO2. Third, the carboxylation and oxygenation
reactions are catalyzed in the same active site on the enzyme, with CO2 and O2 being
competitive substrates. Compared to plant Rubisco, Rubisco from a red alga Galdieria partite
catalyzes its carboxylation with high affinity to CO2, but with low maximum turnover
number.
In order to investigate the difference in enzymatic properties, rice and Galdieria
Rubiscos were crystallized in presence of sulfate. The two crystal structures complexed withsulfate show the apparent structural difference of their catalytic loop. The details of structural
analysis and structure-function relationship of the two Rubiscos will be presented anddiscussed.

P05-179

CRYSTAL STRUCTURE OF IcaR, A REPRESSOR OF THE TetR
FAMILY IMPLICATED IN BIOFILM FORMATION IN
STAPHYLOCOCCUS EPIDERMIDIS
Wen-Yih Jeng,*, 1, 2 Tzu-Ping Ko,*, 1, 2 Rey-Ting Guo,1, 2, 3 Chien-Liang Liu,1, 4 Chia-I Liu,1, 2, 3
Hui-Lin Shr1, 2 and Andrew H.-J. Wang1, 2, 3*

These authors contributed equally to this work. 1Institute of Biological Chemistry, 2Core Facility forProtein Crystallography, Academia Sinica, Taipei 115, Taiwan; 3Institute of Biochemical Sciences,
National Taiwan University, Taipei 106, Taiwan; 4Structural Biology Program, Institute of
Biochemistry and Molecular Biology, National Yang-Ming University, Taipei 112, Taiwan

Expression of the gene cluster icaADBC is necessary for biofilm production in S.
epidermidis. The ica operon is negatively controlled by the repressor IcaR. Here, the crystal
structure of IcaR was determined by multiple anomalous diffraction methods, using aseleno-methionine derivative. It revealed a homodimer comprising entirely α-helices, typicalof the tetracycline repressor protein family for gene regulations. The N-terminal domain
contains a conserved helix-turn-helix DNA-binding motif. Conformational variation indicates
flexibility in this region. The C-terminal domain shows a complementary surface charge
distribution about the dyad axis, ideal for efficient and specific dimer formation. The resultsof electrophoretic mobility shift assay suggest that a 28-base-pairs core segment of the ica
operator is implicated in cooperative binding of two IcaR dimers on opposite sides of theDNA. Computer modeling based on the known DNA-complex structure of QacR showed that
direct protein-DNA interactions are mostly conserved, but with slight variations forrecognizing the different sequence. By interfering with the binding of IcaR to DNA,
gentamicin and other antibiotics may elicit biofilm production in S. epidermidis, as a defense
mechanism.

P05-180

STRUCTURAL BASIS FOR THE DISTINCTIVE SUBCHLOROPLAST
LOCATION OF THREE MAIZE LEAF FERREDOXIN:NADPHOXIDOREDUCTASES
N. Muraki,a G. T. Hanke,b T. Shiba,a T. Hase,b and G. KurisuaaDepartment of Life Sciences, University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo 153-8902, Japan,bInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

Ferredoxin:NADPH oxidoreductase (FNR) catalyzes reduction of NADP+ in the final
step of linear photosynthetic electron transport and is also implicated in cyclic electron flowthat facilitates H+ pumping for ATP production without producing new reducing species. In
higher plants, it has been reported that FNR is localized on the stromal side of thylakoide
membranes through association with membrane protein complexes. We have identified that
there were three leaf FNR isozymes (LFNR1, LFNR2, and LFNR3) in maize chloroplasts at
approximately equivalent concentration and they varied in subchloroplast location (Okutani etal., 2005). LFNR1 was only found at the thylakoide membrane, LFNR3 was exclusively
soluble and LFNR2 had a dual location, although three FNRs showed high (>80%) aminoacid sequence homologies. In addition, LFNR1 and LFNR2 were found to associate with thecytochrome b6f complex as a result of its partial purification. Since no one has succeeded in
crystallizing the FNR:cytochrome b6f super complex from higher plants, we crystallized andanalyzed the structures of three FNR isozymes, to elucidate the structural basis for their
distinctive localization in chloroplast. Main-chain structures of functional domains were very
similar (rmsd = 0.58-0.92 Å). A significant structural difference was found at the N-terminal
region consisting of about 20 residues. A protruding N-terminal region from the globular
domains of LFNR1 seemed to be suitable for interaction with membrane proteins, while the
N-terminal of LFNR3 was folded globular across the catalytic domains. These results are
discussed in terms of the functional differentiation of maize LFNR isozymes.

P05-181

PREPARATION, CRYSTALLIZATION AND PRELIMINARYCRYSTALLOGRAPHIC ANALYSIS OF OLD YELLOW ENZYMEFROM TRYPANOSOMA CRUZINaoki Okamotoa, Shigeru Sugiyamab, Keiji Tokuokaa, Nahoko Uchiyamac, Yousuke Okanoa,
Hiroyoshi Matsumuraa, Yasushi Kaia, Koji Inakad, Yoshihiro Uradec and Tsuyoshi InoueaaDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1

Yamadaoka, Suita, Osaka 565-0871, Japan;
332-0012, Japan;c565-0874, Japan;dbCREST, JST, Honcho, Kawaguchi-shi, Saitama

Department of Molecular Behavior Biology, Osaka Bioscience Institute, Osaka
Maruwa Foods Co., Ltd., Tsutsui-cho 170-1, Yamatokoriyama, Nara 639-1123,

Japan

Trypanosoma cruzi (Tc) is the etiological agent of Chagas’ disease which is a major
public health and economic problem in South America. The development of new
chemotherapeutic agents becomes an urgent need because the anti-chagasic drugs in use havebeen shown to have undesirable side effects in addition to the emergence of parasite
resistance.
Old yellow enzyme (OYE) is an NADPH oxidoreductase that contains flavinmononucleotide as prosthetic group. The OYE from Tc (TcOYE) produces prostaglandin (PG)
F2α from PGH2 as a potent mediator of various physiological and pathological processes.
However, the detailed mechanism has remained obscure.
In order to investigate the relationship between structure and function of TcOYE, therecombinant enzyme was expressed and purified from Escherichia coli and crystallized by thehanging-drop vapor diffusion method. The crystal belongs to the monoclinic space group of
P21 with unit-cell parameters of a = 56.3 Å, b = 78.8 Å, c = 78.8 Å, and β = 93.4° showingthat there are two molecules per asymmetric unit. The crystals diffracted up to 1.7 Å
resolution, and were suitable for X-ray crystallographic studies. A Patterson search method
using the structure of OYE from Pseudomonas putida, as a starting model, is in progress.

P05-182

CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF THE
CERAMIDASE FROM PSEUDOMONAS AERUGINOSA
Hiroyuki Okanoa,Koji Kambayashia, Nozomu Okinob, Hatsumi Monjusyob, Yoshimitsu
Kakutac Makoto Itob and Tsuyoshi InoueaaDepartment of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1

Yamada-oka, Suita, Osaka 565-0871, Japan, bDepartment of Bioscience and Biotechnology, Graduate
School of Bioresource andBioenvironmental Sciences,Kyushu University, 6-10-1, Hakozaki,

Higashi-ku, Fukuoka 812-8581, Japan, cLaboratory of Biochemistry, Department of Bioscience andBiotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka 812-8581,
Japan

Ceramidase (CDase, EC 3.5.1.23) is an enzyme that catalyzes the hydrolysis of the
N-acyl linkage of ceramide to generate sphingosine and fatty acids. Based on optimal pH andprimary structure, CDases are classified into three groups: acid, neutral, and alkaline enzymes.
Bacterial CDases cloned from Pseudomonas aeruginosa are classified as neutral CDases
based on the primary structure.
In this study we performed the overexpression, purification and crystallization of aneutral CDase from Pseudomonas aeruginosa. Crystals grew with PEG1000 and PEG8000 as
the precipitant at 293 K. They diffracted up to 2.6 Å at 100 K using synchrotron radiation andwere found to belong to an orthorhombic space group of P212121, with unit-cell parameters of
a = 127.7, b = 206.6,and c = 204.8 Å. The asymmetric unit contains twelve molecules ofCDase, showing the VM value of 2.4 Å3 Da-1 and a solvent content of 49%. The search forheavy atom derivatives is in progress.

P05-183

WHY DO NITRILASES NEED TO FORM HELICES TO BE ACTIVE?
Trevor Sewella, Serah Kimanib and Muhammed SayedcaElectron Microscope Unit; bDepartment of Molecular and Cell Biology, University of Cape

Town;cDepartment of Biotechnology, University of the Western Cape, South Africa.

We have recently solved the crystal structure of the amidase from Geobacillus pallidus
RAPc8. The structure of this enzyme, which has approximately 20% identity to the fibre
forming, cyanide hydratases, cyanide dihydratases and nitrilases gives a series of previously
inacessible insights. Firstly the extended C-terminus is forms an interlock on at the “A
surface” which we have described previously - giving the reason for the stability of thisinterface. Furthermore a hydrogen bond across this interface stabilises the position of the 310
helix on which the catalytic cysteine is located. The most interesting obsevation arises fromthe very small active site of the amidase. Because of this it can be seen that the oxygen of theacyl intermediate restricts access to glu59 thought to be the general base catalyst responsible
for assisting the hydrolysis of the acyl intermediate. An alternative choice for general basecatalyst is glu142 which is located in a loop which we have previously identified as being partof the “C surface” which together with the “A surface” form the interactions along the
one-start left handed helix. We postulate, based on a series of cryo and negative stain
structures, that the formation of the “C surface” moves glu142 into position so that it canperform a catalytic role in the nitrilases.

P05-184

THE PRESENT STATUS OF ACCURATE STRUCTURE
REFINEMENTS FOR MACRO MOLECULES BY THE MAXIMUMENTROPY METHOD
Makoto Sakata,a Eiji Nishibori,a , Takahiro Nakamura,a Masanori Arimoto,a Shinobu
Aoyagi,a Hideo Ago,b Masashi Miyanob and Toshikazu EbiszakicaDepartment of Applied Physics, Nagoya University;Chikusa-ku, Nagoya, 464-8603 Japan, bMiyano

Structural Biophysics Laboratory, RIKEN SPring-8 Centre, Harima Institute, 1-1-1 Kouto, Mikazuki,
Sayo, Hyogo, 679-5148 Japan, , cEbisuzaki Computational Astrophysics Laboratory, RIKEN 2-1
Hirosawa, Wako, Saitama, 351-0198 JapanIt seems very obvious that the Maximum Entropy Method (MEM) has a great potential
to improve the accuracy of crystal structure refinements for macromolecules, e.g. proteins. In
a sense, protein crystals are open system, for which unknown number of water molecules is
included. Therefore, it is absolutely necessary to determine the structure of water molecules
included in protein crystals.
Conveniently, such determination of water molecules is replaced by bulk solvent
correction, which assumes homogeneous distribution of water among protein molecules. This
assumption should become crude as the accuracy of structure refinements increases. For betterrefinements, every water molecules has to be assigned in a unit cell of the crystal structure.
It would be not difficult to understand that MEM has essential superiority to theconventional Fourier method. MEM never produces physically meaningless negative density
region and hence positive region due to termination effects in resolution. Such positive regionof electron density map could be easily misinterpreted as water molecules in protein crystals.
Although MEM has an essential advantage of accurate structure analyses for
macromolecules, there are very few examples of actual structure analyses of protein crystals
by the MEM. A part of reasons is MEM requires a huge computation loads. The purpose ofthis study is to demonstrate how accurately a protein crystal can be analysed by taking
advantage of MEM in the case of relatively a small protein crystal from extreme thermopile(TT189) using near atomic resolution diffraction data set. It was possible 1) to determine
probably all water molecules in a protein crystal, 2) to find out disordered structures in manycases, 3) to detect hydrogen atoms and 4) to refine anisotropic thermal parameters if necessary.
However, it was not possible to find out all the atoms in a crystal. The small number of atoms,
which seemed severely disordered, could not be detected.

P05-185

CRYSTALLIZATION OF THE COLD-ADAPTED ARABINANASEFROM PENICILLIUM CRYSOGENUM
Kyoko Ikoma,a Yuri Sogabe,a Asako Yamaguchi,b Tetsuko Nakaniwa,a Takayoshi Kinoshita,aTatsuji Sakamoto,b Hideshi Iharaa and Toshiji TadaaaDepartment of Biological Science, Graduate School of Science, Osaka Prefecture University, Osaka,

Japan; bDepartment of Applied Life Sciences, Graduate School of Life and Environmental Sciences,
Osaka Prefecture University, Osaka, Japan

Arabinanase hydrolyzes the α-1,5-L-arabinofuranoside linkage of arabinan distributed inhemicelluloses, which comprise a large fraction of plant cell walls. An endo-arabinanase(Abnc) from Penicillium crysogenum 31B showed optimal activity at 303 to 313 K andretained about 40% of its optimal activity at even 273 K. We have initiated an X-ray structure
analysis of Abnc to clarify the structural features that participate in having activity at low
temperature. Here we report the expression system, purification and crystallization of Abnc.
The recombinant Abnc was overexpressed in E. coli as fusion protein with maltose
binding protein (MBP-Abnc). MBP-Abnc purified by affinity chromatography was cleaved by
Factor Xa. The resulting mixture was chromatographed on UNO Q and Superdex 75 columns.
The purity of Abnc was confirmed by SDS-PAGE. Prior to crystallization trials, the purified
protein was concentrated to 6 mg ml-1 in 0.02 M Tris-HCl buffer, pH 8.0, containing 0.1 M
NaCl. Crystallization were performed using the sparse matrix screening kit Crystal Screen Іfrom Hampton Research by the sitting drop vapor diffusion method at 277 K. Small crystals
were obtained from a drop containing ammonium sulfate as a precipitant at pH 8.5. The
optimization of crystallization conditions is currently under way.

P05-186

RIETVELD ANALYSIS SOFTWARE FOR J-PARC
Ryoko Oishi,a Masao Yonemura,b Shuki Torii,c Akinori Hoshikawa,d Toru Ishigaki,b Yuichiro
Nishimaki,a Takahiro Morishimac and Takashi KamiyamacaVisible Information Center Inc., Tokai-mura, bIbaraki University; Hitachi-city, cHigh Energy

Accelerator Research Organization; Tsukuba-city,dJapan Atomic Energy Agency, Tokai-mura,Japan

As a part of the project creating the world brightest pulsed neutron beam facilty in Japan
Proton Accelerator Research Complex(J-PARC), we are developing software for dataacquisition, data handling, analysis and visualization.
Here we report on the present status of structure analysis software for J-PARC,
especially development of the Rietveld analysis code whose provisional name is Z-Rietveld.
The features of this software and results will be presented.

P05-187

VISUALISING AND QUANTIFYING INTERMOLECULAR
INTERACTIONS WITH HIRSHFELD SURFACES AND
CRYSTALEXPLORER
Joshua J. McKinnon,a Mark A. Spackman,a and Dylan JayatilakaaaSchool of Biomedical, Biomolecular & Chemical Sciences, The University of Western Australia,

Crawley, WA, Australia.

The Hirshfeld surface [1] and associated 2D-fingerprint plot [2] encourage a new kindof understanding of intermolecular interactions in molecular crystals by emphasising awhole-of-structure approach. The Hirshfeld surface is determined by the full local
environment - the combination of intermolecular contacts - rather than concentrating on thosecontacts perceived to be important.
The latest release of CrystalExplorer [3] incorporates our recent developments[4] whichenable the Hirshfeld surface and fingerprint plot to focus on specific interaction types (forinstance, O•••H, C–H•••π, etc.) by highlighting regions of the molecule or fingerprint
involving those specific types of interaction.
By dividing the Hirshfeld surface into regions involved in different types of interaction,
CrystalExplorer allows the user to quantify the contribution of these interactions based on
their contribution to the Hirshfeld surface area. Quantifying intermolecular interactions in thisway provides a truly novel tool for comparing related structures such as polymorphs.
Reference:
1. McKinnon, J. J., Spackman, M. A. & Mitchell, A. S. (2004). Acta Crystallographica Section B, 60,
627-668.
2. Spackman, M. A. & McKinnon, J. J. (2002). CrystEngComm 4, 378-392.
3. Wolff, S. K., Grimwood, D. J., McKinnon, J. J., Jayatilaka, D. & Spackman, M. A. (2007).
CrystalExplorer. Version 2.0. http://hirshfeldsurface.net/CrystalExplorer
4. McKinnon, J.J., Jayatilaka, D., Spackman, M.A., Chem. Commun., 2007, DOI: 10.1039/b704980c

P05-188

THE EFFECT OF AMINO ACIDS AND AMINO ACID DERIVATIVESON PROTEIN CRYSTALLIZATION
L. Ito1, T. Kobayashi1, K. Shiraki2, T. Narukawa1, A. Oosuka1 and H. Yamaguchi1
1

Sch of Sci and Tech, Univ of Kwansei Gakuin, 2-1 Gakuen, Sanda, Hyogo 669-1337,

2

Inst of Appl Phys, Univ of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573

Protein crystallography is an indispensable technique for biological, biotechnological,
and pharmaceutical researches. The structure determination by X-ray crystallography has
been dramatically developed by progress in sample preparation, data collection andcomputation. To obtain high quality single crystals, however, still remains as the great
problem. The difficulty depends on the many parameters that influence protein
crystallization, including protein concentration, pH, ionic strength and precipitantconcentration. Recently, many researchers adopt the sparse-matrix including different
mother liquors that cover many chemical factors, in order to determine the primary
crystallization conditions. Single crystals suitable for X-ray diffraction experiment are notalways obtained by the procedure. Such screening procedures are not effective enough.
Prevention of protein aggregation plays a key role in the formation of single crystals
in the aggregation-prone solution condition. Guanidine and urea are well known as
aggregation suppressors that weaken the hydrophobic intermolecular interaction of proteins.
Such denaturants are contained in a commercially available additive-screen kit, but
decrease the stability of the native state. Recently, amino acids and amino acid derivatives,
which are non-denaturating reagents, such as arginine have been used for additives todecrease the aggregation during a refolding process and a heat treatment process. In thisstudy, we investigated the effect of amino acids and amino acids derivatives on protein
crystallization.
As a result, protein crystals were obtained in expanded concentration range of the
known precipitant in the presence of some kind of these reagents. Especially, crystals wereobtained from many conditions including precipitants that crystal did not appear in theabsence of the reagents. For example, in the presence of arginine, HEWL crystals wereobtained from ammonium sulfate solution. It is considered that the basic additive andamino acid derivatives promote the crystallization of positively charged HEWL. These
results show that these reagents are very effective for crystallization and promote successratio of it and suggests a new strategy to improve the performance of the protein
crystallization by addition of amino acids.

P05-189

COMPUTATIONAL METHODOLOGY TO ANALYZE VARIOUS
DEFECTS IN CUBIC CRYSTALS
S. T. Nakagawa
Material Science, Graduate School of Science, Okayama Univ. of Science, Okayama, JAPANIn the field of crystal engineering, an important issue is the innovative synthesis with a
new effect. In order to make a breakthrough in the material design, it has been confirmed thatthe key is hidden in the sequence of time-developed intermediate processes following certain
disturbances. In experiments, the sign of such an intermediate process emerges occasionallyas imperfections in a perfect crystal. To the contrary, computation can thoroughly trace thetime-dependent processes in principle, and we can see the detail of the response mechanismof materials. For such computation, Molecular dynamic (MD) simulation is often used.
Unfortunately for the same event or quantity, we cannot always compare experimental andcomputational results with same accuracy, while those two means are rather complementary.
We have developed a computational methodology to analyze atomistic defects in cubic
crystals based on crystallography under the name of Pixel Mapping (PM). An empirical MD
monitors the atomic configuration under annealing or ion bombardment. PM method canidentity various types of atomistic defects from microscopic to macroscopic scale including
long-range-order (LRO) parameters. The essential difference of the PM from other analyses isin the coarse-grained recognition of atoms. Crystalline space is segmented into cubic pixels
and atoms are identified by integer address of its belonging cubic pixel. This definition makes
it possible to identify Miller indices of atomic planes and indicate crystallographic directions
for atoms in crystals, even at higher temperatures than absolute 0 K. This coarse-grained
viewpoint is a breakthrough that our computational analysis can identity planar defects with
Miller index as is observed by microscopes.
The PM is available for 24 prototype cubic crystals listed in a crystallographic databasecalled StrukturBericht. The classification of prototypes arranges crystals based on theligand-field of composite atoms in a crystal. For MD simulations, such a classification has the
merit that the same formula of interatomic potentials can be expected for crystals belonging to
the same prototype. We have defined the set of LRO parameters for each prototype group.
Judging from LRO information, we can identify structure changes as amorphization ortransformation from one cubic crystal to another. Applications of PM are to be shown in thepresentation.

P05-190

DDLM: A NEW DICTIONARY LANGUAGE SUBMITTED TOCOMCIFS FOR APPROVAL
Nick Spadaccini,a John Westbrook,b and Syd HallcaSchool of Computer Science and Software Engineering, The University of Western Australia,

AUSTRALIA;b

Protein Data Bank, Rutgers Univ., New Jersey, USA;c

School of Biomedical,

Biomolecular and Chemical Sciences, The University of Western Australia, AUSTRALIA

DDLm is a data definition language that provides a rich but simple syntax forconstructing data definitions. It includes facilities for relating derivative data via method
expressions that are symbolic, easy to read as text, but are computer interpretable andexecutable [2]. DDLm provides a wider range of data types and allows for lists, arrays,
tuples and tables. DDLm also provides for real-time merging of dictionaries, thus allowing
for the greater modularisation of discipline dictionaries and the avoidance of definition
duplication. A long-term aim of DDLm is to provide a common syntax and structure to all
crystallographic dictionaries. It is currently available for examination and comment by all
members of the crystallographic community [3]. The community is invited to review andcomment on the proposed definition language as part of the approval process.
The paper will describe the major features of DDLm and their importance in the morecomprehensive definition of all data used our discipline.
Reference:[1] International Tables for Crystallography Volume G: Definition and Exchange of
Crystallographic Data. (2005) Editors Sydney Hall and Brian McMahon. Springer, Dordrecht.
[2] Spadaccini, N., Hall, S.R., & Castleden, I.R. (2000) J. Chem. Inf. Comput., Sci. 40.
1289-1301.
[3] www.iucr.org/iucr-top/cif/ddlm/

P05-191

MULTIPLE STRATEGIES IN HIGH-THROUGHPUT CLONING,
EXPRESSION AND PRODUCTION OF RECOMBINANT PROTEINSFOR STRUCTURAL PROTEOMICS
Hao Xu, Jin-Yi Zhu, Mervin Zhao, Quentin Florence, James Tucker Swindell II, Bret
Dillard, Dayong Zhou, Angela Yang, John Rose, and Bi-Cheng Wang
Southeast Collaboratory for Structural Genomics, Department of Biochemistry and Molecular Biology,
University of Georgia, Athens, GA 30602, USA

The determination of “three-dimensional protein structures with unique chemicalsequences” has been an emphasis of the Southeast Collaboratory for Structural Genomics(SECSG) in target selection.
Six biologically important organisms have been chosen as initial genome resources inour studies and more than 3,000 pfam or non-pfam ORFs have been cloned. We have foundthat recombinant protein yield and solubility of these ORFs is highly dependent on thespecific sequence, as well as on the vector, fusion construct, host cell, and culture conditions
used. For high-throughput processing, initial efforts have focused on soluble (Tier-1) andinsoluble (Tier-2) purification strategies using the cost-effective His-tag. In Tier-1
processing ~50% of the cloned targets are expressed and ~25% of the expressed proteins aresoluble and have been purified for crystallization. In the Tier-2 process, insoluble Tier-1
targets are salvaged using a variety of cloning and production strategies in parallel. For
difficult yet biologically important targets including membrane proteins, HIV-related humanproteins, or protein complexes, new technologies have been developed to improve expression
and explore high throughput production.
Work is supported in part with funds from the National Institutes of Health (GM62407),
the Georgia Research Alliance and the University of Georgia Research Foundation.

P06-004

PERFORMANCE OF THE HIGH-THROUGHPUT PROTEIN
CRYSTALLOGRAPHY BEAMLINE BL13B1 AT THE NSRRC
Chun-Hsiung Chao,a Yuch-Chen Jean,a Yu-Shan Huang,a Chien-Chang Tsenga, Cheng-Hung
Chianga, Chun-Jung Chena, Shih-Chun Chung,a Ching-Shiang Hwang,a King-Long Tsanga
and Chien-Te ChenaaNational Synchrotron Radiation Research Center, Hsinchu 30077, Taiwan, ROC

A high-throughput Protein Crystallography facility was constructed for the National
Synchrotron Radiation Research Center (NSRRC) super-conducting super-wiggler beamline
BL13B1. This 28-pole wiggler, with a magnetic field of 3.2 Tesla, increases the criticalenergy from 2.14 keV for a 1.25 Tesla normal conducting magnet to 4.82 keV, and is capableto provide an intensive X-ray beam up to 19 keV, which made it possible for hard x-ray
experiments to be conducted at the relatively low energy NSRRC ring (1.5 GeV).
BL13B1 covers an energy range from 6.5 keV to 19 keV, which is suitable for both
MAD and monochromatic diffraction experiments. The major optical components of thisbeamline include a front end, a cylindrical vertical collimating mirror, a double-crystal Si(111) monochromator, and a toroidal focusing mirror. The end stations is equipped with an
ADSC Quantum315 CCD area detector, with a high precision single-phi axis goniometer, asample cooling system, a robotic sample changer for automatically sample mounting andcentering. BLU-ICE and HKL2000 provides user-friendly interfaces to the data acquisitionand data processing tasks. The design and performance characteristics of this beamline will be
described.

P06-005

STANDARD OPERATION SYSTEM FOR STRUCTURAL BIOLOGYBEAMLINES AT SPRING-8
Go Uenoa, Kazuya Hasegawab, Nobuo Okazakib, Kunio Hirataa, Takashi Kumasakaa, b and
Masaki Yamamotoa, ba

RIKEN SPring-8 Center, Kouto, Sayo, Hyogo, Japan., bJapan Synchrotron Radiation ResearchInstitute, Kouto, Sayo, Hyogo , JapanThe standard operation system for structural biology beamlines at SPring-8 has been
first developed at RIKEN Structural Genomics Beamlines (BL26B1 & BL26B2) [1], where
the high throughput data collection with sample auto-changer SPACE (SPrign-8 Precise
Automatic Cryo-sample Exchanger) is carried out with automatic beamline operation. The
control system is designed based on the client-and-server architecture in which each device iscontrolled by distributed server programs. User interface BSS (Beamline Scheduling
Software) provides the centralized control of entire beamline instruments with an intuitive
GUI. The hardware components in the end station such as x-ray shutter, crystal goniometer,
equipment stage etc. are controlled by VME bus modules through MADOCA device control
framework [2], which is commonly used for beamline and storage ring operation of SPring-8.
By communicating with MADOCA system, as well as other equipment servers such as area
detector, sample changer etc., BSS realizes the all-in-one and automatic operation of thebeamlines. Successive data collections for multiple samples can be easily scheduled andexecuted by utilizing BSS, starting with setting x-ray wavelength, exchanging sample, setting
up detector, and taking diffraction photos with monitoring the storage ring status.
Since this control system is scalable and configurable to other hardware, the samearchitecture has been similarly implemented to many of other structural biology beamlines atSPring-8, providing users a common look and feel at all beamlines.
Presently, development of some new features, such as automatic crystal screening,real-time monitoring of radiation damage, automatic crystal centering etc. are attempted byassociating the beamline operation with the automatic diffraction image analysis.
Reference:[1] Ueno, G., et al., (2006). J. Struct. Funct. Genomics. 7, 15-22.
[2] Tanaka, R. et al., Proc of ICALEPCS ’95, Chicago, USA, 1995 p.201.

P06-006

HOMELABS VS. SYNCHROTRONS: THE FACTS WILL SURPRISEYOU
Joseph D. Ferrara, Cheng Yang
Rigaku Americas Corporation, The Woodlands, USA

This presentation will be divided into two parts. The first part will comprise a review of
the current state-of-the-art in home lab x-ray sources from both performance andenvironmental impact perspectives. In the second part will present the results of data miningof the RCSB PDB (H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig,
I.N. Shindyalov, P.E. Bourne: The Protein Data Bank. (2000) Nucleic Acids Research. 28,
235-242) , and will compare and contrast the productivity of home labs and synchrotrons.
The results of the survey will surprise you.

P06-007

NEXT GENERATION X-RAY DETECTOR FOR IN-HOUSE XRDSYSTEM
Takeyoshi Taguchi,a Christian Broennimannb and Eric F. Eikenberryba

X-rayResearch Laboratory, Rigaku Corporation, 3-9-12 Matsubara-cho, Akishima-shi, Tokyo, Japan;b

DECTRIS Ltd., 5232 Villigen PSI, Switzerland

A novel type X-ray detector, called PILATUS, has been developed at the Paul Scherrer
Institut (PSI) during the last decade. PILATUS detectors are two-dimensional hybrid pixel
array detectors, which operate in single-photon counting mode. The PILATUS detectors havea very wide dynamic range (1:1,000,000), very short read out time (< 3.0msec), and very highcounting rate (> 2 x 106 counts/sec/pixel). Additionally, the PILATUS detector can set energy
threshold individually for each pixel. Thus the PILATUS can suppress fluorescencebackground. These features are superior to existing area detectors and PILATUS is the next
generation X-ray detector.
The PILATUS detector systems have a few different configurations. A single module of
PILATUS detector, or the PILATUS 100K, has 487 x 195 pixels with a pixel size of 172 x
172µ2. The active area is 83.8 x 33.5mm2. Large area systems consist of 20 to 60 modules
and can cover up to 424 x 435mm2 area. Such systems are mainly used for macromolecule
analysis, i.e. protein crystallography. The single module detector is small and easy to handle
and can be adapted to many systems with small modification. The PILATUS 100K detector is
integrated to an in-house X-ray diffraction system and demonstrates superior performance.
Some examples of XRD measurements with the PILATUS 100K detector will be given.

P06-008

STRUCTURAL BIOLOGY BEAMLINES AT SPring-8
Masaki Yamamotoa,b, Go Uenoa, Takaaki Hikimaa, Atsushi Nisawaa, Kunio Hirataa, Tetsuya
Shimizua, Nobutaka Shimizu a,b, Masahide Kawamoto b, Kazuya Hasegawa b, Hisanobu Sakaib, Seiki Baba b, Nobuo Okazaki b, Aik Hong Teh b, Takashi Kumasaka a,ba

RIKEN SPring-8 Center, Kouto, Sayo, Hyogo, Japan., bJapan Synchrotron Radiation ResearchInstitute, Kouto, Sayo, Hyogo , Japan

In the third generation synchrotron radiation, structural biology research is one of the
major subjects in the past decade. At SPring-8, eight beamlines are operating for protein
crystallography (PX). We have been constructing and developing the beamlines with the viewof two objectives. One objective is improvements of the applicable crystal size and the data
quality, and the other is the high throughput protein crystallography. After the completion of
the Human Genome Project, structural genomics research projects have been progressing
worldwide. At SPring-8, the Protein 3000 project, a Japanese structural genomics project, hasbeen progressing rapidly owing to high-throughput PX beamlines.
BL41XU is an undulator beamline with the high brilliance of 4.8 × 1014
photons/sec/mm2. The new K/B mirror system was installed for micro crystals (~ 25 μm)
using a micro beam. The beam size at sample position is controllable from 25 × 25 to 70 ×
100 μm2 using two quadrant slits. SAD measurements of Se-methionine samples with the
crystal size from 15 to 50 μm were performed using multiple positions on a crystal, and wesolved the initial phase at the resolutions from 2.7 to 3.9 Å. A new micro focus beamline,
aimed at the target beam size of 1 × 1 μm2, is planning.
BL26B1&B2 have been constructed for Structural Genomics research. The beamline
operation is automated cooperating with the sample changer robot named SPACE, theoperation software BSS and beamline management database D-Cha. Combination of BSS,SPACE and D-cha also enables Mail-in data collection, and the Web interface of D-Cha
allows users to deposit measurement condition or to observe recorded images from distantplace.
We will present the present status and the future plan of protein crystallography
beamlines at SPring-8.

P06-009

STATISTICAL PROPERTIES OF X-RAY INTENSITY MEASURED
WITH A COUNTING SYSTEM WITH FINITE DEAD-TIME
Takashi Ida, Akihisa Oya, Hisashi Hibino
Ceramics Research Laboratory,Nagoya Institute of Technology, Tajimi, Gifu, 507-0071, JapanCounting method is widely used to measure the intensity of X-ray. Independently
generated signal pulses are expected to obey the Poisson distribution, which predicts theprobability for the number of pulses n during the measurement period T is given by
PPoisson(n) = (n!)-1 (rT)n exp(-rT) ,where r is the average rate of generated pulses. The mean μ and variance σ2 of thenumber of the Poisson pulses are simply given by
μ = σ2 = rT
The statistical errors of the intensity measured by a counting method can naturally bemodelled by the square root of the measured count, if the Poisson distribution of the pulses isassumed.
The probability for the number of counted Poisson pulses m based on the non-extended
dead-time model can be expressed as
Pnon(m) = (m!)-1 (1+rτ) [r(T - mτ)]m exp[-r(T - mτ)]where τ is the dead-time of a detector and/or the electronic circuits of the detection
system. The mean μnon and variance σnon2 of the counted pulses are given by
μnon = rT / (1 + rτ)
σnon2 = μnon / (1 + rτ)2
Recently, Laundy & Collins [1] have reported analytical expressions about thestatistical properties of a pulse-overlap model for the counting loss, which includes theextended dead-time model as a special case. According to their results, the mean μext andvariance σext2 for the extended dead-time model are given by
μext = rT exp(-rτ) ,σext2 = μext [1 - 2rτ exp(-rτ)] .
The above expressions for the non-extended and extended dead-time models forcounting loss applied to the Poisson pulses has been validated by a Monte Carlo simulation
with simple computer algorithm. Variance of pulses counted with a detection system on the
powder diffraction beam-line BL-4B2 at the Photon Factory in Tsukuba, evaluated byrepeated measurements of the beam diffracted from mica standard powder (NIST SRM675),
will be compared with the theoretical prediction.
Reference:[1] Laundy, D. & Collins, S. (2003). J. Synchrotron Rad. 10, 214-218

P06-010

MAIL-IN DATA COLLECTION AT SPRING-8 STRUCTURAL
BIOLOGY BEAMLINES
Seiki Babaa, Kazuya Hasegawaa, Go Uenob, Nobuo Okazakia, Hisanobu Sakaib, Hironori
Murakamib, Takashi Kumasakaa and Masaki Yamamotoa,baJapan Synchrotron Radiation Research Institute, Kouto, Sayo, Hyogo , Japan,b

RIKEN SPring-8

Center, Kouto, Sayo, Hyogo, JapanThe mail-in data collection at SPring-8 structural biology beamlines makes use of
automated beamline operation system using the sample changer SPACE, the beamline control
software BSS and the web interface D-Cha. Data collection can be readily carried out without
visiting SPring-8 by following procedures: 1) Target crystals are stored in the sample tray atlaboratory. 2) The tray is sent to the beamline via home-delivery service. 3) The informationof the tray such as sample name, experimental conditions of content samples is input into
D-Cha by users. 4) Diffraction data is collected at the beamline utilizing automatic systemwith SPACE and BSS. 5) Collected data is downloaded via the Internet using D-Cha.
At the beamline, all crystals are once screened by using synchrotron radiation. In thisprocess, crystal centering is carried out by beamline operator. Users can monitor theexperimental results via D-Cha at their laboratory in real time. The complete data set iscollected only for crystals qualified by users. Since SPACE has the special feature to assure
the reproducibility of the crystal mount position, the data sets can be automatically collectedonce the crystal centering is performed.
By following the screening process on our system, users can definitely select the best
crystal to collect the data set and also can make an efficient experimental schedule, whichleads to the improvement of the throughput.
At BL26B1, BL26B2 and BL38B1, mail-in data collection system has been operated
since September 2005. Currently, the commercial mail-in service has started in July 2006, as
the joint project among JASRI, RIKEN and analysis service companies.

P06-011

HIGH THROUGHPUT PROTEIN CRYSTAL EXCHANGE ROBOTS OF
THE PHOTON FACTORY BEAMLINES
Masahiko Hiraki, Shokei Watanabe, Nobuo Honda, Yusuke Yamada, Naohiro Matsugaki,
Noriyuki Igarashi, Yurii Gaponov and Soichi Wakatsuki
Structural Biology Research Center, Photon Factory (PF), Institute of Materials Structure Science,High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki, 305-0801, Japan

In order to execute diffraction experiments of protein crystals by remote-control,
process of sample exchange must be automated. In addition, the sample exchange robots canliberate users from slavish work at the beamlines. Therefore, we have developed sample
exchange robots that can exchange protein crystals according to the instructions from out of
the experimental hutches. The robots were designed based on the SAM system (SSRL
Automated Mounting system) with cooperation of SSRL (Stanford Synchrotron Radiation
Laboratory) macromolecular crystallography group. In order to reduce the required time forthe sample exchange, we modified the single-tongs of the SAM system and developed adouble-tongs system that can hold two cryo pins at the same time. The robot withdouble-tongs can move to the goniometer head holding the next cryo pin by one of the tongs,
dismounts the used cryo pin with the other tongs and mounts the next pin onto the goniometerhead without leaving the diffractometer area.
Two different types of tongs have been installed; the single-tongs at the beamlines
BL-5A and AR-NW12A, and the double-tongs at the BL-17A. The same GUI software for theoperation of the sample exchange robots is used at all beamlines, however, so that the users
do not need to consider the differences of the tongs. An intermediate computer works forcommunication between the GUI and the robot controller. When it receives "exchange"command from the GUI, it translates suitable commands for the type of tongs and sends themto the robot controller.
We will introduce our sample exchange robot system including the beamline computer
network, and report on the state of the user operation.

P06-012

UPGRADE OF THE STRUCTURAL BIOLOGY BEAMLINES AT THE
PHOTON FACTORY
Noriyuki Igarashi, Naohiro Matsugaki, Yusuke Yamada, Masahiko Hiraki and Soichi
Wakatsuki
Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research
Organization 1-1 Oho, Tsukuba, Ibaraki 305-0801, Japan

Structural Biology Research Center at the Photon Factory currently operates four
structural biology beamlines. The AR-NW12A, BL-5A and BL-17A are the insertion device
beamlines, while the BL-6A is a conventional bending magnet beamline. The micro-focus
beamline BL-17A was newly constructed and opened for general users in 2006. In the next
two years, two more construction plans of a pharmaceutical beamline and anothermicro-focus beamline are scheduled.
The BL-17A was designed for micro-crystal structure analysis. In addition, the intenselower energy beam at around 6 keV is used for structure determination by SAD phasing withlight atoms. The source of the beamline is a newly developed short-gap undulator installed in
one of four short straight sections of PF 2.5GeV ring. The measured focused beam size
(FWHM) with the K-B mirror system was about 0.03mm (V) x 0.23 mm (H). The photon flux
at 12 keV collimated by 100 and 20 µm2 were 8 x 1010 and 7 x 109 photons/sec, respectively.
Further optimization and stabilization of the optics have been executed; suppressing vibrationof the optical elements, fixing beam position by feedback control, etc. In this June, abrand-new CCD detector ADSC Quantum 270 was installed and used for experiments.
Automation of the beamlines is facilitated by installing sample changers, automatic
sample centering system and beamline control software. The changers, modified from theoriginal SSRL-SAM system, have been operated at all the insertion device beamlines. The
automatic sample centering system, including diffraction-based evaluation algorithm, is underdevelopment. The beamline control software based on a relational database allows secure
remote access and automatic scheduled experiments together with the sample changer. All theinformation stored in the database during experiments can be easily tracked and managed.
A pharmaceutical beamline will be built at the PF-AR NE3A in the summer of FY2008
and opened to users from April, FY2009. The beamline is expected to show a higher
performance than the high-throughput beamlins AR-NW12A and BL-5A. The beamline will
be mainly dedicated to drug design.
Construction of a new micro-focus beamline at the PF ring in FY2009 is scheduled. The
goal is to deliver brilliant lower energy beam at around 4-5 keV (dedicated to sulphur SAD
experiment) and more photon flux at around 12keV than that of BL-17A.

P06-013

THE SIDE LINE OF TAIWAN CONTRACT BEAMLINE BL12XU ATSPRING-8 FOR HIGH ENERGY PHOTOEMISSION
Chi-Yi Huang, Ku-Ding Tsuei, Yong Q. Cai, Cheng-Chi Chen, Yen-Fang Song and Shih-Chun
Chung
National Synchrotron Radiation Research Center, Hsinchu, Taiwan, 300, R.O.C.

High energy photoemission spectroscopy presents new opportunities in the study of theelectronic structure of novel materials with increased bulk sensitivity. This characteristic isparticularly useful to study strongly correlated systems with different bulk properties fromsurface, and the properties of berried interface of devices. For these experiments, we areconstructing a new side beamline branching off from the main line of BL12XU at SPring-8. A
single bounce diamond monochromator (DM) will be used to deliver monochromatic X-rays
to the side beamline from 6 keV to 12 keV. After the DM, we have designed a high resolution
monochromator to reduce the energy resolution to 60 meV (FWHM). The total flux will be
2x1011 photons/sec at 6 keV. Finally, the X-ray is focused to 30 x 30 μm2 (HxV) (FWHM) at
the sample position. The whole beamline except the DM will be supported on a platform thatswings with photon energy. We intend to start commissioning this beamline by the end of2007.

P06-041

RATIOS OF ELASTIC CONSTANTS OF CdTe DERIVED FROM X-RAY
THERMAL DIFFUSE SCATTERING UNDER HIGH PRESSURE
Daisuke Ohtsu,a Maki Okube,a Takahiro Kuribayashi,b Yasuhiro Kudoh,b Taiki Nakanishi,aHiroyuki Katsuragawa,a Akiko Nakao,c and Satoshi SasakiaaMaterials and Structures Laboratory, Tokyo Institute of Technology, Yokohama, 226-8503;b

Institute of Mineralogy, Petrology and Economic Geology, Tohoku University, Sendai, 980-8578;c

Photon Factory, Institute of Materials Structure Science, KEK, Tsukuba, 305-0801, Japan

Cadmium telluride (CdTe) has attracted to various applications to optoelectronic
devices. The II-VI semiconductor has the zinc-blende structure at ambient pressure andtransforms to the intermediate cinnabar phase in a pressure range of about 2.5 to 4 GPa,
before reaching the rock-salt structure. An accurate description of the elastic property for
CdTe is important because it provides a link between the mechanical and dynamical
behaviours of crystals in concerning the nature of phase transition. The elastic constants canbe related to the X-ray intensity of thermal diffuse scattering (TDS), which arises from thescattering of the incident beam by phonons. The TDS approach is useful even for a small andopaque crystal loaded in a diamond-anvil cell (DAC). In this study, the pressure dependenceof the elastic constant of CdTe is investigated on the basis of the observation of TDS.
At each experiment, a single crystal of CdTe was loaded in a modified
Merrill-Bassett-type DAC with a gasket made from stainless steel. The pressure wasmeasured using the ruby-fluorescence method. Only zinc-blende phase was investigated in thepressure range close to the phase boundary. The TDS intensity was measured with avertical-type four-circle diffractometer at the BL-10A of Photon Factory. A wavelength of λ =0.7 Å was selected by a Si(111) monochromator. The TDS intensities were measured in
two-dimensional reciprocal area with two of [100], [010] and [001] passing through 004, 220
and 111 reciprocal lattice points at room temperature. Based on the diffuse intensity measured
at each point of the grid, the shape of curves of isodiffusion surrounding the Bragg point wereobtained and compared with the theoretical isodiffusion surfaces (Jahn, 1942). The shape of
the isodiffusion surface was examined whether to change by the pressure. Then, the ratios ofelastic constants of c11/c44 and c11/c12 were determined from the relative diffuse intensities as afunction of pressure. The presentation will be made in the context of the merits and demeritsof the TDS method.

P06-042

SITE OCCUPANCY AND MAGNETIC STRUCTURE OF BaTiMnFe10O19
HEXAFERRITETaiki Nakanishi,a Maki Okube,a Hiroyuki Katsuragawa,a Daisuke Ohtsu,a Takeshi Toyoda,bAkiko Nakao,c and Satoshi SasakiaaMaterials and Structures Laboratory, Tokyo Institute of Technology, Yokohama, 226-8503, Japan;bIndustrial Research Institute of Ishikawa, Kanazawa, 920-8203, Japan;cPhoton Factory, Institute of Materials Structure Science, KEK, Tsukuba, 305-0801, JapanM-type barium hexaferrite, BaFe12O19 is ferrimagnetic below Tc = 723 K. The magnetic
structure can be described with the spin collinear model, where all the magnetic moments areordered parallel or antiparallel to c axis. Ti4+ and Mn2+ substitution for Fe3+ results the
reduction of the strong uniaxial magnetic anisotropy. In the solid solution including Ti4+ andCo2+ ions, the neutron and synchrotron X-ray diffraction studies have revealed the existenceof a magnetic helix propagated along the hexagonal c axis in BaTi0.8Co0.8Fe10.4O19. Therefore,
in this study, another hexaferrite of BaTiMnFe10O19 has been examined with the ion-size
effect to study crystallographically the mechanism of the magnetic anisotropy change.
The powder crystals were prepared by the conventional solid-state reaction using
appropriate molar mixtures of BaCO3, TiO2, MnCO3 and Fe2O3 as starting materials. The
products preheated at 1073 K for an hour were ground again and heated at 1473 K for 2 hours.
A flux method was used for single crystal growth. The chemical analysis was made using a
Horiba XGT-2000 X-ray fluorescence spectrometer. The cell dimensions are a = 5.902(3), c =23.209(4) Å (P63/mmc). Conventional and synchrotron X-ray diffraction experiments werecarried out using Rigaku AFC-7R and PF-BL10A four-circle diffractometers, respectively.
The X-ray magnetic circular dichroism (XMCD) experiments were performed at the Fe K
absorption edge with a diamond(001) phase retarder and rare-earth magnets at the BL-6C.
The structural parameters of BaTiMnFe10O19 were determined using full-matrix
least-squares software RADY with the Mo K data. The site occupancies of Fe ions in fivedifferent sites were determined with the anomalous scattering effects of synchrotron X-rays ata wavelength λ = 1.7485 Å. Then, site occupancies of Ti ions were determined within two
selective sites with the Mo K data. The final result on the cation distribution is: 100% Fe in
Fe(1) [2a site]; 100% Fe in Fe(2) [2b]; 58.0% Fe, 35.1% Ti and 6.9% Mn in Fe(3) [4f1]; 100%Fe in Fe(4) [4f2]; 80.7% Fe, 5.0% Ti and 14.3% Mn in Fe(5) [12k]. In XMCD measurements,
a negative peak was clearly observed near E = 7.120 keV, having a similar pattern to that oftypical M-type ferrites. Progress on the determination of the magnetic structure will bepresented.

P06-043

VALENCE AND SPIN STATE OF Co IONS IN La1-XCaXCoO3
Hiroyuki Katsuragawa,a Maki Okube,a Takayasu Hanashima,b Taiki Nakanishi,a Daisuke
Ohtsu,a and Satoshi SasakiaaMaterials and Structure Laboratory, Tokyo Institute of Technology, Yokohama, 226-8503;b

Organization for Promotion of COE, Ritsumeikan University, Kusatsu, 525-8577, Japan.

Broad magnetic-electronic transition of LaCoO3 above 90 K can be interpreted with theexistence of the intermediate spin (IS) of Co3+. It is known in La1-xSrxCoO3 that the IS statewith hole doping or a superexchange of Co3+-O-Co4+ gives the magnetic moments such as
spin glass when Sr2+ is substituted for La3+. Ca2+ substitution for La is expected to have thehole doping with weak lattice distortion because of resemble ionic radii (rLa = 1.32 Å, rCa =1.35 Å, rSr = 1.44 Å). A careful comparison of magnetic and electronic state is needed forLa1-xCaxCoO3 and La1-xSrxCoO3.
Powder crystals of La1-xCaxCoO3 were synthesized from appropriate molar mixtures of
Co2O3, La2O3 and CaCO3. The mixtures were ground in an agate mortar, prepared in analuminum crucible, and heated up to 1273 K and maintained for 36 hours. The products wereground again and heated at 1273 K for 12 hours and quenched. X-ray powder diffraction
measurements were performed to confirm a single. The effect of Ca doping on the magnetic
structure of La1-xCaxCoO3 (x = 0, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.5, 0.6, 0.65 and 0.8)
was examined by measurements of SQUID and X-ray magnetic circular dichroism (XMCD).
The XMCD experiments were carried out at the Co K absorption edge on the BL-6C(3A). The
Si(111) double-crystal monochromator and a diamond(001) phase retarder were used with
X-rays of 3(H) x 2(V) mm2. The powder samples were mounted on several sheets of transparent
tape, which were used in the Faraday arrangement with a pair of rare-earth magnets in amagnetic field of 0.4 T. Two ionization chambers were used for absorption experiments,
where the second one is 300 mm in length and filled with 75% N2 + 25% Ar gas. A
completely standard transmission setup was used with the
The XMCD signal was observed in a difference of absorption coefficients with the rightand left circularly polarized X-rays. It reflects the local spin and orbital polarization of the
final states at the inner core absorption edges. A negative peak of XMCD was clearlyobserved at E = 7.719 keV within the threshold region, suggesting the existence of the IS stateof Co3+. By Ca substitution for La, a positive peak appeared at E = 7.723 keV of the mainedge. The presentation will discuss the electronic state of Co ions.

P06-044

MIXED-VALENCE STATES OF TRANSITION-METAL ATOMS IN A
SOLID SOLUTION BETWEEN Fe3O4 AND Co3O4
Yoshihiro Yamamoto,a Norio Shimizu,a Maki Okube,a Atsuko Ohnoa and Satoshi SasakiaaMaterials and Structures Laboratory, Tokyo Institute of Technology, Yokohama, 226-8503, Japan;

The spinel structure has the geometrical frustration of a pyrochlore type, which isimportant in the superexchange interaction between tetrahedral A and octahedral B sites. The
valence states of iron and cobalt atoms are a key factor to control the conductivity andmagnetism in ferrites and cobaltites. A combination study of single-crystal X-ray diffraction(SCXD), X-ray absorption near edge structure (XANES) and X-ray magnetic circulardichroism (XMCD) is useful to clarify the valence and spin states in the mixed-valencecompounds.
Synchrotron experiments for FexCo3-xO4 (x = 0, 0.8, 1.0, 1.1, 1.4, 1.8, 2.0, 2.1 and 3.0)
were carried out at BL-10A and BL-3A/6C of Photon Factory. The horizontally polarized
X-rays were monochromatized by Si(111) monochromators to select the wavelengths near Fe
K and Co K absorption edges. Diffraction intensities for some single crystals were measured
by a ω-2θ step-scan technique in a vertical-type four-circle diffractometer. The cation
distribution between iron and cobalt atoms was determined with a large difference inanomalous scattering factors. The XMCD experiments were made to use a phase retarder of asynthetic diamond crystal, ionization chambers and rare-earth magnets. The difference in theabsorption coefficients for right- and left-circularly polarized X rays can be used with spins
parallel and antiparallel to the direction of light travel.
XANES and XMCD spectra of FexCo3-xO4 gave the following results on thecompositional dependence of the valence states: (1) iron ions are trivalent for the samples
having x ≤ 2, (2) trivalent cobalt ions exist at least for x ≤ 2 and (3) Fe3+, Co2+ and Co3+ ionsequally occupy the B sites in Fe4/3Co5/3O4. The samples for x ≤ 1.4 have the split XMCD
peaks at E = 7707 and 7715 eV of the Co K edge, suggesting the change of the spin state ofcobalt atoms. The presentation will discuss the electronic states of iron and cobalt atoms inthe solid solution of Fe3O4 and Co3O4.

P06-045

X-RAY SCATTERING STUDY OF YTTRIUM-DOPED HfO2 THIN
FILMS
C.-H. Hsua, Z. K. Yang,a,b K. L. Yua,, M.-T. Tang,a M. L. Huang,a,b W. C. Lee,b Y. J. Lee,b P.
Chang,b M. Hong,b and J. Kwoca

National Synchrotron Radiation Research Center; bDepartment of Materials Science and Engineering,

National Tsing Hua University; cDepartment of Physics, National Tsing Hua University, Hsinchu,
Taiwan, 300, ROC

We have successfully converted the structure of monoclinic HfO2 thin films to a cubic
one by yttrium doping. These yttrium-doped HfO2 (YDH) ultra-thin films were grown
epitaxially on GaAs (001) and Si (111) substrates by molecular beam epitaxy (MBE). The
electric measurements of a film of 7.7 nm thick yielded an enhanced dielectric constant κ~32,
close to the theoretical value of cubic phase HfO2. We have performed x-ray scattering andtransmission electron microscopy measurements to thoroughly investigate the structure andsurface morphology of the YDH thin films. The interfaces between YDH and both kinds ofsubstrates are atomistic sharp and free of reacted interfacial layer. The surface of YDH layersgrown on Si (111) are rather flat but well resolved {111} facets were observed on those grown
on GaAs (001). We have also determined yttrium content of YDH films to be 19% by using
anomalous x-ray diffraction (AXD) across Y k-edge and angle resolved X-ray photoelectron
spectroscopy (AR-XPS). The agreement between the AXD and AR-XPS results manifests thatthe incorporated Y atoms indeed homogeneously substitute Hf atoms in the crystalline lattice
and form a substitutional solid solution.

P06-046

STUDIES ON FERROMAGNETIC CARBONS
Prabal Dasgupta
Department of central scientific services
Indian Association for the cultivation of science
2A&2B, Raja S.C. Mullick Road
Kolkata-700032
India

The structure of commerinin, a pigment of a blue dayflower, was solved by Kondo et al.
in 1992 [1]. The authors reported that the pigment was composed of six anthocyanin and six
flavone molecules with two Mg ions, based on the crystal structure analysis at 1.0Å resolution.
However, our recent research on the structure of protocyanin pigment [2] indicated that thecommerinin complex pigment has other metal constituents.
We investigated the crystal structure of the commerinin pigment at the resolution of 0.7
Å using a large CCD area detector at BL-5A of the Photon Factory. The structure reveals two
additional Mg ions bound to outer side of the complex pigment. The positions of Mg ionsroughly corresponded to those of Ca ions in the protocyanin structure. The high resolution
structure including the positions of hydrogen atoms will be presented.

P06-047

CRYSTAL STRUCTURE AND MAGNETIC PROPERTIES OF
NaFe(WO4)2 AND NaCr(WO4)2
D.Sangaaa , L.Nyam-Ochira,b, H.Ehrenbergb,c, D.Mikhailovab, H.FuessbaNational University of Mongolia, Ikh Surguuli1, Ulaanbaatar, MongoliabDarmstadt University of Technology, Petersenstrasse 23, 64287 Darmstadt, GermanycInstitute forComplex Materials, IFW Dresden, Helmholtzstrasse 20, 01069 Dresden, Germany

Powder samples of NaFe(WO4)2 and NaCr(WO4)2 were prepared and studied by X-ray
diffraction and SQUID measurements at low temperature. The structure of sodium iron andchromium tungstate, NaFe(WO4)2 and NaCr(WO4)2, is similar to the structure ofwolframite-type FeWO4 with the same space group P2/c, but with doubled a parameter [1,2].
Therefore, less magnetic coupling paths between M3+O6-octahedra exist in
NaM3+(WO4)2 because of additional diamagnetic units in the structure. Nevertheless,magnetisation data show that NaFe(WO4)2 and NaCr(WO4)2 are antiferromagnetic at low
temperature. A maximum in the temperature dependence of magnetisation is observed at
11(1)K for NaFe(WO4)2 and for NaCr(WO4)2 at 32(1)K, which is an upper estimate of the
Néel temperature.
This system provides a suitable test for the proposed dominance of supersuperexchange
couplings M3+-O-O-M3+, with M3+-O-O and O-O- M3+ angles close to 180° and both bridging
oxygens belonging to the same coordination polyhedra of a diamagnetic ion [3].

Reference:[1] P.V.Klevtsov and R.F.Klevtsova, J. Solid State Chem. 2, 278-282 (1970)[2] R.F.Klevtsova and N.V.Belov, Soviet Physics-Crystallography Vol.15, No.1 July-Aug., 1970
[3] H.Ehrenberg, K.G.Bramnik, E.Muessig, T.Buhrmester, H.Weitzel, C.Ritter, J. Magn. Magn. Mater. 261,
353-359 (2003).

P06-048

THE METHOD OF DETERMINATION OF STRUCTURAL IN
STRETCHED POLYMERSAida Martirosyan
Physical department,Yerevan

State University , Yerevan, Armenia

The suggested method has high sensitivity towards structural changes occurring insubstances ; it allows us to observe particularly supramolecular changes in stretched or
textured polymers.In the given work, by the example of stretched polychloroprens (300%), it
is shown the regularity of intercristalline distance changes along and across the stretched axes,
depending on the medium density of the stretched sample. If in the three – blockinterferometer we put a stretched polymeric film on the way of one of the split X-ray beams
and get moir patterns in two positions – along and across the stretching axes, according to the(l − l0 ) λformula δ =+ δ 0 ( l and l0 are the distances between moiré stripes, received froml0 D
the interferometer with and without the sample, accordingly; D- is the sample thinckness; λis the wave length of the falling X-ray radiation; δ is the decree-ment of the refractive index
of air), it will be possible to determine the decrement of
X-ray beams, and to calculate thedensity alond and across the stretching axes of polymer. The density was defined according
to the formula ρ = 3,67 ⋅ 10 −11Aδ, where A and Z are the atomic weigt and the fullZλnumber of electrons in the atom, accordingly .
The relation of the calculated densities is back proportional to intercrystalline
distances along and across the stretching axes of the polymeric film ( irradiated volumes are
N m + N 1 mam N 1 mkr + N 2 mamequal in both cases) : V1 = V2 = 1 kr=
, where N1 and N2 are

ρ1

ρ2

the numbers of crystalline and amorphic fields in the irradiated area, along and across thestretching axes, accordingly, mkr and mam are the masses of crystalline and amorfic unit
sections, accordingly, ρ1

and

ρ2

are the medium densities along and across thet,stretching axes. Taking into account the fact that the intercrystalline distance is d =Niwhere i= 1,2,… , and it is the length of the irradiated section, from here it follows thatgd1 ρ 2=. In the given method the accuracy of the density definition is 10-4-10-5 cm 3 .
d 2 ρ1

P06-049

CRYSTAL ENGENEERING OF NEW 4,4’-BIPYRIDINES AND
RELATED COMPOUNDS
Olexii V. Gutov, Eduard B. Rusanov, Alexander N. Chernega, Mark I. Povolotskii
Institute of Organic Chemistry NAS Ukraine, Murmanska st. 5, 02094, Kyiv-94, Ukraine(AVGutov@mail.ru)

4,4’-bipyridine derivatives are widely used on the practice as the electrochromic
materials, electron transfer mediators, biosensors, matrices of molecular electronic devices etc.
The viologens, 4,4’-bipyridine tertiary salts (I), are the most useful of them.
2A

+

+

R N

N R

I
2A

+

N R
R N

II +

R = Alk, -(CH2)n-X. X – functional group.
We have recently synthesized new substituted viologens contained various functionalgroups (amide, amino, urea, carboxylic etc), conjugation-extended viologen analogues (II)bearing stilbene motif as a spacer between the pyridine moieties and some other4,4’-bipyridine derivatives. Single-crystal X-ray diffraction was used for the determination of
the molecular and crystal structure peculiarities of these compounds. It was found that in themost cases pyridine moieties of viologens and their analogues are coplanar. But there are also
some exceptions that demonstrate twisted bipyridine structures. X-ray diffraction has showedthat the viologens bearing hydrogen-contained functional groups usually formate
intermolecular chains, helices or nets by different types of hydrogen bonds.
Spectral and optical properties of the all new compounds were studied. It was found thatthe extended viologen-analogues demonstrate strong luminescence properties in contrast to
the corresponding original viologens.

P06-050

COCRYSTALS OF OXALIC ACID WITH DERIVATIVES OF
TRICYCLIC QUINAZOLONE-4
Akmal Tojiboev,a Kambarali Turgunov,a Bahodir TashkhodjaevaaInstitute of Chemistry of Plant Substances, Academy Sciences of Uzbekistan, Tashkent, Uzbekistan.

The design of organic solids by crystal engineering is presently of high interest [1].
Tricyclic quinazoline derivatives are potentially valuable synthons in crystal engineering:
their electron donating nitrogen atom holds out the promise of different complexes with arange of electron acceptors.
Recent x-ray investigations of crystals obtained by cocrystalization of tri-, tetra- andpentamethylene-3,4-dihydroquinazolin-4-one homologues with oxalic acid shows that in thecase of first two homologues cocrystal structures is formed without protonation ofquinazolin-4-one molecule in the ratio 2:1, in contrast to first crystallization ofpentamethylene-3,4-dihydroquinazolin-4-one with oxalic acid gives salt type crystals in the
1:1 ratio. In this case protonation occurs through nitrogen atom of quinazolone molecule andit reflects in changing of some bond lengths in the molecules of quinazoline and oxalic acid.
Forcomparison
tofirststructures
also
thecrystalsof
2,3-pentamethylene-3,4-dihydroquinazolone-4 hydrochloride oxalic acid is obtained andstructure is investigated.
Such research of a structure of this cocrystals of biologically active tricyclic derivativesof quinazoline [2] are important in crystal engineering terms since they offer the possibility ofdesigning new materials through control of hydrogen bonding
Reference:[1] Desiraji, G.R. Crys.Engineer. The Design of Organic Solids, Elsevier: Amsterdam, 1989.
[2] Shakhidoyatov, Kh.M. Quinazolin-4-one and their application. Tashkent: Fan, 1989.

P06-051

CRYSTAL STRUCTURES OF TWO ALIPHATIC AMIDASES AmiE
AND AmiF FROM HELICOBACTER PYLORI REVEAL A CONSERVEDCATALYTIC TRIAD
Wen-Ching Wang, Chiu-Lien Hung, Cheng-Yu Chen, and Yu-Wen Hua
Institute of Molecular and Cellular Biology and Department of Life Science, National Tsing Hua
University, Hsinchu, Taiwan

Helicobacter pylori AmiE and AmiF are two aliphatic amidases and belong to membersof the nitrilase superfamily. The crystal structure of AmiF was solved to 1.75 Å resolution
using single-wavelength anomalous dispersion methods. The structure consists of ahomohexamer related by 3-fold symmetry in which each subunit has an α-β-β-α four-layerarchitecture characteristic of the nitrilase superfamily. One exterior α layer faces the solvent,whereas the other one associates with that of the neighbor subunit, forming a tightα-β-β-α-α-β-β-α dimer. The apo and liganded crystal structures of an inactive mutant C166S
were also determined to 2.50 and 2.30 Å, respectively. These structures reveal a small
formamide-binding pocket that includes C166, E60, and K133 catalytic residues, in which
C166 acts as a nucleophile. The crystal structure of AmiE was also solved to 2.38 Å
resolution with molecular replacement methods. The AmiE structure also reveals thehomologous architecture and conserved catalytic residues (C165, E59, and K133). Molecular
dynamic simulations show that the conserved triad has minimal fluctuations, catalyzing thehydrolysis of a specific nitrile or amide in the nitrilase superfamily efficiently.

P06-052

POLYTYPE TRANSFORMATION DURING NITROGEN DOPING OF
SiC CRYSTALS
Jinli Chena and Zhe Chuan Fengb,*aPhysics Department, National University of Singapore, Singapore 117542; b Institute of Photonics &Optoelectronics and Department of Electrical Engineering, National Taiwan University, Taipei,
Taiwan 106-17, ROC.
* E-mail: zcfeng@cc.ee.ntu.edu.tw

SiC, because of its excellent properties, is very attractive in high power, high frequency,
and high temperature electronic and optoelectronic device applications, including as
substrates for III-Nitrides materials and devices. It has been noticed recently that polytypetransformation in SiC crystals has large impact on the quality of SiC-based materials andmicroelelctronic devices. The occurrence of stacking faults (SF) and the polytypetransformation in SiC thin films or bulk wafers will cause severe problems in the devices. In
deed, the polytype transformation is also a type of stacking fault - periodical stacking fault.
The uncontrolled polytype transformation in SiC wafers could degrade micro-electronic
device properties. On the other hand, if polytype transformation can be controlled, it may leadto new devices based on the heterojunction between different polytypes.
In this paper, we study the structural variations of a set of SiC bulk crystal wafers
prepared by Physical Vapore Deposition (PVD), with different Nitrogen (N) doping levels.
The initial growth conditions were used to produce 6H-poly type SiC, which has been
approved by high resolution X-ray diffraction (HR-XRD), Raman scattering (RS) and highresolution transmission electron microscopy (HR-TEM). However, when extreme highN-dopants were applied, the obtained wafer was found with 4H-polutype features.
Experimental results from HRTEM, RS and HR-XRD measurements are presented in details
for above observations. We propose a mechanism for the experimental findings. A possible
reason of the polytype transformation is that the introduction of N enhanced the formation ofclusters on the growing surface which act as nucleation centers of other polytypes or affects
the reaction surface C/Si ratio.

P06-053

FORMATION OF LARGE LANTHANIDE CLUSTER HAVING CHIRAL
LIGANDS AND THEIR MOLECULAR ASSEMBLY IN THE
CRYSTALLINE STATE
Chizuko Kabuto a), Kenji Omata b), Kuninobu Kabuto b), and Yoichi Sasaki c)a)Research and Analytical Center for Giant Molecules and b)Graduate School of Science, Tohoku

University, Aramaki, Aoba-ku, Sendai, 980-8578, c)Graduate School of Science, Hokkaido University,
Kita-ku, Sapporo, 060-0810

It is well known that the structures of lanthanide-based supramolecular systems are
hardly predictable and often quite peculiar. Recently we reported an unprecedented
tetrahedral cage-like of lanthanide cluster [LaIII18(D-bpba)18(H2O)36]Cl18 {D-bpba =N,N’-bis(2- pyridylmethyl)-N,N’-1,2-ethanediyl-bis(D-alaninate)} 1, revealed by X-ray
crystallographic study. To the best of our knowledge, 1 is the largest lanthanide cluster so far
reported not only in the number of metal ions but in the size of cluster (Figure 1). This
octadecamer cluster is built up with twelve cis- and six trans-complexes, where the bpba
ligands coordinate in the cis and trans position with respect to the two pyridines, respectively.
Another interesting feature is the formation of the trinuclear core in 1, being thesmallest assembled unit utilizing the carboxylate-bridging mode. Very recently we found outthat the similar trinuclear core is formed in various kinds of M+[Ln(pdta) (H2O)2]- complexes
2 {pdta = propylenediamine-N,N, N’,N’-tetraacetate}. Furthermore the trinuclear core of 2
forms a hexamer unit via M+ ion, eventually forming a two-dimentional network architecturein the crystalline state (Figure 2). Since no such assembly has been observed in Ln(etda) {edta= ethylenediamine-N,N, N’,N’-tetraacetate}, we consider that the chirality of the ligand might
be essential for the formation of the trinuclear core and for the large cluster formation.
We wish present and discuss here the details about the crystal structures of lanthanide
complexes 1 (X = Cl, Br) and 2 (M = Na, K; Ln = PrIII, SmIII, EuIII, GdIII)

P06-054

HOST FRAMEWORK OF INCLUSION CRYSTAL OF
1,1,2,2-TETRAKIS(4-CARBOXYPHENYL) ETHANE
Michiko Iriyamaa, Natsumi Sakumaa, Hidehiro Uekusaa, Natsuki Amanokurab, Masami
Kanekoba

Department of Chemistry and Materials Science, Tokyo Institute of Technology, Japanb

Nippon Soda Co.,Ltd.

Tetrapodal organic host molecule, 1,1,2,2-tetrakis (4-carboxyphenyl) ethane,
TEP-COOH (Fig.1), is expected to form inclusion host framework via strong hydrogenbonding (carboxylic dimer motif) and also weak π-π interaction (phenyl group). In order toinvestigate the dimensionality of the host framework, the crystal structures of inclusioncompounds of TEP-COOH with small solvent molecules and amines were determined bysingle crystal X-ray structure analysis.
As expected, methanol inclusion crystal shows two-dimensional framework with large
cavity (Fig.2). The methanol molecules are connecting the TEP-COOH hosts by O-H…O
hydrogen bonds. Interestingly, the TEP-COOH molecules also form a one-dimensional
linear chain using carboxylic dimer hydrogen bond (Fig.3) and fill the host cavity. As seenin this structure, the connections between TEP-COOH hosts are not always directly (dimrmotif), but have “joints” by guests. These structural elements of “chain”, “net”, and “joint”
form variety of host-frameworks in TEP-COOH inclusion crystals.

Fig. 1 TEP-COOH

Fig. 2 net framework

Fig. 3 one-dimensional liner chainP06-055

CRYSTAL STRUCTURE ANALYSIS OF
1,1,2,2-TETRAKIS(3-METHYL-4-HYDROXYPHENYL)ETHANEINCLUSION CRYSTALS
Kazuyuki Toyotaa, Hidehiro Uekusaa, Natuki Amanokurab, and Masami KanekobaDepertment of chemistry and materials science, Tokyo institute of technology, Tokyob

Nippon Soda Co.,Ltd

Enclosed in the host frameworks, physical properties of guest molecule such assolubility or guest release speed can be controlled by inclusion mode. 1,1,2,2-tetrakis(4-hydroxyphenyl)ethane, TEP, is known as a tetrapodal flexible host molecule which
crystallizes with small guest molecules such as organic solvents.
In our previous study, three characteristic host frameworks were recognized in TEP
inclusion crystal, which governed guest release properties. We focused on a TEP derivative,
1,1,2,2-tetrakis(3-methyl-4-hydroxyphenyl)ethane, TEOC (Fig.1), in which the methyl groupnext to hydroxy group deteriorates the hydrogen bonding capability. It is of interests toinvestigate the effect of methyl group to the framework structure and guest inclusion ability of
TEOC comparing with TEP inclusion crystal.
Unexpectedly, crystal structure analysis revealed that TEOC-acetone and TEP-acetone
inclusion crystals have similar structure. Also, in the case of TEOC-methanol (Fig.2) andcorresponding TEP crystal, same 1D chain framework with guest joints was observed.
Although the TEP-methanol has flat chain structure, the TEOC chain was zigzag shape due tosteric effect of methyl group, and additional host molecules were attached to the chain. Fromthese results, the influence of methyl substitution would be limited if the host framework hasenough cavity around itself.
CH3
HO

OH

CH3
H3C

HO

OH
CH3

Fig. 1

Fig. 2

P06-056

STRUCTURAL DIVERSITY OF [M(SCN)2] FRAGMENTS WITH
N,N’-BISPYRIDINE-TYPE LIGANDS, 4-BPD (4-BPD =1,4-BIS(4-PYRIDYL)-2,3-DIAZA-1,3-BUTADIENE)
Chih-Chieh Wang,a* Wei-Zeng Lin,a Yu-Ruei Guo,a Wei-Ting Huang,a Shuen-Jie Dai,a
Mei-Ju Ke,a Gene-Hsiang Leeba

Department of Chemistry, Soochow University,; bInstrumentation Center, National Taiwan

University, Taipei, Taiwan, R.O.C.

The Schiff base ligand, 1,4-bis(4-pyridyl)-2,3-diaza-1,3-butadiene (4-bpd), was used in
the synthesis of six new coordination polymers, [Fe6(NCS)12(4-bpd)11(H2O)]⋅(4-bpd)⋅3(H2O)(1),[Fe(NCS)2(4-bpd)2](2),[Ni(NCS)2(4-bpd)2]⋅3(EtOH)⋅(H2O)(3),[Ni(NCS)2(4-bpd)2]⋅2(EtOH)⋅2(H2O) (4), [Zn(NCS)2(4-bpd)2] (5) and [Cd(NCS)2(4-bpd)](6), each of them adopting a different structural topologies. Synthesis, X-ray structural
determinations and thermogravimetric analyses are presented. The reaction of FeCl2⋅4H2O,
KSCN and 4-bpd afforded compounds 1 and 2, in which the former one shows a
two-dimensional (2D) [Fe6] interpenetrating structure constructed by two T-shape terminal
Fe(II) and four central square-grid Fe(II) building units and the latter one shows a 2D 44
square grid framework. Three symmetrically identical layers in 2 are mutually interpenetrated
with a repeating ABCABC--- sequence. The reaction of NiCl2⋅6H2O, KSCN and 4-bpd wasfound to be solvent-sensitive and resulted in the formation of two supramolecular isomers,
compound 3, which adopts a 2D square-grid MOF and [Ni(NCS)2(4-bpd)2]⋅2(EtOH)⋅2(H2O)
and compound 4, which adopts a 3D 65⋅8 CdSO4 MOF, respectively. The 2D layered MOF in
3 adopts an ABAB-- arrangement forming a 3D network with two 1D channels intercalatedwith solvent molecules. In 4, the much larger intra-framework spaces of the3D NbO MOF areoccupied by two other identical but independent networks, which interpenetrate the first andeach other forming 1D channels intercalated with solvent molecules. The reaction of
ZnCl2⋅6H2O or Cd(NO3)2⋅6H2O with KSCN and 4-bpd afforded compound 5 with a
one-dimensional zigzag chain and compound 6 with a 2D rectangle-grid layer, respectively.
The rotational freedom of the diaza group of 4-bpd ligand plays an important role on the
structural diversity of theses MOFs.

P06-057

STRUCTURAL DIVERSITY OF [M(SCN)2] FRAGMENTS WITH BPHD
(BPHD = 2,5-BIS(4-PYRIDYL)-3,4-DIAZA-2,4-HEXADIENE)
Chih-Chieh Wang,a* Yi-Tzu Lin,a Yu-Hsuan Lee,a Gene-Hsiang Leeba

Department of Chemistry, Soochow University,; bInstrumentation Center, National Taiwan

University, Taipei, Taiwan, R.O.C.

Five metal coordination polymers with interesting supramolecular architectures,(1),[Mn(bphd)2(NCS)2]n(2){[Zn(bphd)2(NCS)2][Zn0.5(bphd)(NCS)(H2O)]}n{[Mn0.5(bphd)0.5(NCS)(H2O)](H2O)(bphd)}n(3),[Fe(bphd)2(NCS)2]n (4),and[Co(bphd)2(NCS)2]n (5), (bphd=2,5-Bis(4-pyridyl)-3,4-diaza-2,4-hexadiene), have beensynthesized and structurally determined by X-ray diffraction method, each of them adopting a
different structural metal-organic frameworks (MOFs). Compound 1 are divided into twoparts, the first part is a hexa-coordinated Zn(II) center bonded with two NCS− and fourbridging bphd ligands. A 2D layered MOF is constructed by a square-grid as the basic
building unit. The second part is a five-coordinated Zn(II) center bonded with two bridging
bphd, two NCS− and one water molecule forming a 1D chain-like MOF Adjacent 2D layers
are parallel arranged and penetrated by 1D chains. In compound 2, the Mn(II) ion ishexacoordinated by two NCS− and four bphd ligands. The bphd acts a bridging ligand toconnect the metal ions forming a 2D square-grid wave-liked layer. Three identical but
independent layers are mutually interpenetrated. In compound 3, the Mn(II) ion is
hexa-coordinated bonded with two NCS−, two water molecules and two bridging bphd ligands
to form 1D chains. A 3D supramolecular architecture is constructed by hydrogen-bonds
among the free bphd ligand and water molecules and π−π interactions between the pyridyl
rings of the bphd ligands. In compound 4 and 5, the metal centers are bonded with two NCS−
and four bridging bphd ligands to afford a 2D noninterpenetrating square-grid layered MOF.
These 2D layered MOFs adopt an ABAB arrangement forming a 3D network with two 1D
channels intercalated with solvent molecules. The rotational freedom of the diaza group of
bphd ligand plays an important role on the structural diversity of theses MOFs.

P06-058

CRYSTAL STRUCTURE AND VIBRATIONAL SPECTRA OF
μ-OXO-BIS[TETRA(p-METHOXYPHENYL)PORPHYRINATOIRON(III)]
Ratchadaporn Puntharod,a,b Bayden Wood,b Don McNaughton,b andaKenneth J. Hallera

School of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima,

Thailand, 30000;bSchool of Chemistry, Faculty of Science, Monash University, Melbourne,

Australia, 3800.

The compound, μ-oxo-bis[tetra(p-methoxyphenyl)porphyrinatoiron(III)] was preparedfollowing the method of Cheng (include the reference), and recrystallized by vapor diffusionof acetonitrile into a dichloromethane solution. The structure was determined fromsingle-crystal X-ray data collected at 123 K. The space group is monoclinic C2/c: a =17.1330(6), b = 27.1339(10), c = 18.0900(11) Å, β = 98.2980(10)º, V= 8321.7(7) Å3, andcontains four molecules of the title compound with iron atoms located on 2-fold axes. The
Fe−N distances are 2.072(8), 2.078(8), 2.080(9), and 2.087(8) Å; the Fe−O distance is
1.7624(13) Å; and the Fe−O−Fe angle is 179.7(6)º. The domed five-coordinate geometryaround each iron atom is entirely typical for a high-spin ferric porphyrin, and correspondswith the resonance Raman spectra which shows the oxidation state marker band (ν4) at ∼1359
cm−1 for high-spin iron(III) porphyrin. The ATR/infrared spectrum displays the μ-oxo
Fe−O−Fe absorption at 871 cm-1.

P06-059[H2en]2+ CATION DISORDER IN A NETWORK OF VANADIUMPOLYBORATE CLUSTERS
Aungkana Chatkon,a Kenneth J. Haller,a and Ian D. WilliamsbabSchool of Chemistry, Suranaree University of Technology, Nakhon Ratchasima 30000 Thailand

Department of Chemistry, Hong Kong University of Science & Technology, Hong Kong

Hydrothermal reaction of vanadium pentoxide, boric acid, ethylenediamine, andhydrofluoric acid (1:10:3:3) at 180 °C for 3 days gave the anionic vanadium polyborate
cluster, [V6B20O50H8]10- which has been characterized by single crystal X-ray crystallography.
Charge balance is maintained by conversion of amine groups to ammonium groups on theassociated ethylenediamine molecules. The approximately S6 cluster, which consists of acentral V6O18 band of six square-pyramidal vanadyl groups capped top and bottom throughthe basal oxygen atoms by triangular raft-like B10O16H4 polyborate ligands, was easily locatedby conventional direct methods using SIR97. Electron density difference maps based on thispreliminary model showed a plethora of peaks in the intercluster region. Some peaks wererational for the organic amine component, but several regions were not recognizable due todisorder of cations and solvent water molecules. Successful solution of this structure waspossible through an iterative process of examination/interpretation of electron density maps
followed by model building and constrained/restrained refinement. The resulting three
dimensional supramolecular array of cations, anions, and solvent water molecules,
interconnected by extensive hydrogen bonding will be described.
Crystal data: {[H2en]2+}5 [V6B20O50H8]10- •7H2O; Mr = 1766.6; light green; 0.20 x 0.25
x 0.32 mm; monoclinic; C2/c (No. 15); a = 20.0513(2), b = 13.4444(1), c = 21.6003(2) Å, β =97.332(1)°, V = 5775.34(9) Å3; Z = 4; λMoKα = 0.71073 Å; T = 200 K. Data collection: Nonius
KappaCCD; 16,769 data collected; Rmerge = 0.019; 8425 unique data; 7105 observed data (Io >4σ(Io)); R = 0.048.

P06-060

A THREE-DIMENSIONAL SUPRAMOLECULAR STRUCTURE OF
ZINC VANADATE: Zn(2-EtIm)2(VO3)2
Orrasa In-noi,a Samroeng Krachodnok,a Kenneth J. Haller,a Herman H.-Y. Sung,b Fanny L.-Y.
Shekb and Ian D. WilliamsbaSchool of Chemistry, Suranaree University of Technology, Nakhon Ratchasima 30000 Thailand;b

Department of Chemistry, Hong Kong University of Science and Technology, Hong Kong.

Pale yellow crystals of the title compound were obtained from the hydrothermal
synthesis of vanadium pentoxide, zinc acetate, and 2-ethylimidazole in the mole ratio 1:1:4 at
110°C for 2 days, and structurally analyzed by single crystal X-ray diffraction. The compound
crystallizes in monoclinic space group P21/c with a = 10.8319(10), b = 14.7575(14), c =10.8554(10) Å, β = 92.821(2)°, and V = 1733.15 Å3, T = 298(2) K. Intensity data werecollected on a Bruker-Nonius Smart Apex CCD diffractometer using graphite monochromated
Mo Kα X-radiation.
The structure contains polyoxovanadate chains parallel to the b axis, interconnectedwith corner-sharing ZnN2O2 tetrahedra to form 2D networks in the bc plane, with 6-membered[Zn2V4O6] rings and 10-membered [Zn2V8O10] rings. The strength of the layers is reinforced
by strong N–H···O and weak C–H···O hydrogen bond interactions. Adjacent layers are held
together via strong N–H···O hydrogen bond interactions (d[N···O] = 2.776(7) Å, d[H···O] =1.95(5) Å) to generate a 3D supramolecular framework (Fig. 1).
Crystal data: C10H16N4O6V2Zn; Mr = 455.52 Daltons; pale yellow crystals 0.10 x 0.15 x0.20 mm; monoclinic; space group P21/c (No. 14); a = 10.8319(10), b = 14.7575(14), c =10.8554(10) Å3, β = 92.821(2)°, and V = 1733.25; Z = 4;T = 298(2) K; μ = 2.460 mm-1; dcalc =1.746 Mgm-3; 10642 data collected; θmax = 28.31°; 4145 unique (2/m), Rint = 0.0696; R1=
0.0574 and wR2=
0.1028for2519
observed Fo > 4σ(Fo);Δρmax, min = 0.50, -0.44-3eA .

Fig. 1 Strong N–H···O hydrogen bond interactions forming a 3D network.

P06-061

LAYERED AND NETWORK STRUCTURES OF HYBRID ZINCVANADATES CONTAINING BRIDGING AZOLE LIGANDS
Samroeng Krachodnok,a Kenneth J. Haller,a Herman H-Y. Sung,b Fanny L-Y. Shekb and Ian
D. WilliamsbabSchool of Chemistry, Suranaree University of Technology, Nakhon Ratchasima 30000 Thailand;
Department of Chemistry, Hong Kong University of Science and Technology, Hong Kong

Vanadium oxide and hybrid organic-inorganic vanadate compounds have been thesubject of extensive study in the past decade with a wide range of applications in catalysis,
Liion batteries, magnetism, and medicine. Hybrid zinc vanadates remain relatively
unexplored when compared with hybrid cobalt, manganese, nickel, and copper vanadates with
their demonstrated rich structural chemistry.
Herein, we report three hybrid zinc vanadates synthesized with three different types ofbridging azole ligands, namely 2D Zn4(μ-3,5-Me2pz)4(3,5-Me2pzH)4(V4O12) (1)from 3,5-dimethylpyrazole, 3D Zn(Im)(μ -Im)VO3 (2) from imidazole, and 3D Zn( μ3-1,2,4-tz)V2O5(OH) (3) from 1,2,4-triazole. All compounds were synthesized underhydrothermal conditions from mixtures of vanadium pentoxide and zinc acetate dihydratewith the different azole bases in the mole ratio 1:1:1 at 140°C for 2 days. 1 consists of the[V4O12]4- tetracyclovanadate sharing the corners with four dimeric zinc tetrahedra, formed by
two doubly bridged μ-3,5-Me2pz, through μ-O oxygen atoms lying across inversion
centers to generate 2D layers parallel to the ac plane. The layer and neighbors are held
together via weak C–H···X (X = O and π) hydrogen bond interactions into a 3D network. 2,
presenting imidazolate-doubly bridged binuclear zinc units and the complexes are alternately
linked to disordered polyoxovanadate chains by sharing the corners. Finally, 3 shows thetriply bridged μ3-1,2,4-triazolate to zinc centers to build up cationic polymeric layers. The
cationic layers are connected to the anionic polyoxovanadate layers by μ-O oxygen atoms
into a 3D network. Strong D–H···O (D = N and O) and weak C–H···X (X = O and π)hydrogen bond interactions in 2 and 3 will be presented and discussed.

Fig. Perspective view of the cationic polymeric layers of triply bridged μ3-1,2,4-tz in 3

P06-062

OPEN COPPER TARTRATE BIPYRIDINE 3D FRAMEWORKS WITH
VARYING WALL CHIRALITIESPokka K-C. Pang, Herman H-Y. Sung and Ian D. Williams
Department of Chemistry, Hong Kong University of Science and Technology,
Clear Water Bay, Kowloon, Hong Kong, China.

Email: pokka@ust.hk

Hydrothermal synthesis has been carried out for the chiral porous lanthanide tartrates[Ln2(L-TAR)3(H2O)2]3H2O [1] as well as open framework indium tartrates [2]. In order tofurther extend this we have examined the possibility for transition metals of combining
tartrate with other neutral ligands which may act as spacers to create larger channels.
Reaction of copper acetate, 4,4-bipyridine and L-, D/L- or meso-tartaric acids leads to a
related set of 3D network polymers [Cu( 3, 3-TAR2-) (bipy)], in which sheets of copper
tartrate are connected by the bipyridine spacer groups. The inherent chirality of L-tartrateleads to rectangular chiral 1D channels, of dimension 4 x 6Å which can contain further
uncoordinated bipyridine (left). In D/L and meso-tartrate cases similar network polymers arealso formed in which the chirality of the uncoordinated C(2) and C(3) -CH(OH)- alcohol
centers are varied. Furthermore differentiation of the faces of the copper tartrate sheets cancreate two alternating channel types, through head-to-head and tail-to-tail ordering, shown
best in the case of [Cu(meso-TAR)(bipy)] (right) which has been crystallized with thealternating channels containing oxalic acid and water. The sorption selectivity of thesechannels in these novel porous solids is now under investigation. The Research Grants
Council (HKSAR) is thanked for financial support of this work, grant 603307.

Reference:
1. S. Thushari, J.A-K. Cha, H. H-Y. Sung, S. S-Y. Chui, I. D. Williams, Chem.Commun., 2005, 5515.
2. A. S-F. Au-Yeung, J.A-K. Cha, H. H-Y. Sung, S. S-Y. Chui, I. D. Williams, Inorg. Chem. Commun., 2006, 9,507.

P06-063

FLUX SYNTHESIS OF NEW TARTRATOBORATE POLYMERS ANDCYCLIC OLIGOMERSAlex S-F. Au-Yeung, Herman H-Y. Sung and Ian D. Williams
Department of Chemistry, Hong Kong University of Science and Technology,
Clear Water Bay, Kowloon, Hong Kong, China.

Email: alexwill@ust.hk

Molten boric acid 'flux' synthesis was initially developed by us for the preparation of
borate-rich clusters [1], recently we found these conditions can lead to newbis(salicylato)borates through direct reaction of boric and salicylic acids with either inorganicor organic bases.[2] We were interested to see whether this could be extended to otherchelating ligands involving carboxylate and alcohol groups. The use of chiral ligands is offurther interest since their bis-chelation leads to new stereogenic center at boron. Reaction of
L-tartaric acid with boric acid and KOH yields either the known monomeric salt K[B(L-TAR2-)2]nH2O or the new chiral chain polymer K[B(L-TAR4-)] H2O depending onreaction stoichiometry. The chain polymer has a novel 3-fold helical structure. If
meso-tartaric acid is used an analogous chain polymer K[B(meso-TAR4-)] H2O is formed,
which has 2-fold screw translational symmetry. Different reaction conditions in this case
can lead to phase-pure isolation of the novel cyclic oligomer K4[B4(meso-TAR4-)4], shown
below. This has a central cavity which binds a potassium ion in the solid state, which
presumably assists its supramolecular formation. The meso-polymers and oligomers arechiral since the stereochemistry of the boron centers is the same within each molecule. The
integrity of these tartratoborate chains and rings in solution and their use in further
preparation of chiral solids is under investigation. The Research Grants Council (HKSAR) is
thanked for financial support of this work (grant 6043-05)

Reference:
1.

I. D. Williams, M. Wu, H. H-Y. Sung, X. X. Zhang and J. Yu, Chem. Commun., 1998, 2463.

2.

A. S-F. Au-Yeung, H. H-Y Sung, M. G. Lesley, I. D. Williams

Mol. Cryst., Liq Cryst submitted

P06-064

CRYSTAL STRUCTURE OF COMPLEX BIMETALLIC SALTS OF
NICKEL(II): [Ni(ter)2(H2O)4][Ni(4-CNpy)2(H2O)4].H2O AND [Ni(H2O)6][Ni(ter)(4-CNpy)(H2O)4].(ter)Sanchay J. Bora and Birinchi K. Das*
Department of Chemistry, Gauhati University, Guwahati – 781 014, India

Two supramolecularly aggregated Ni(II) compounds containing terephthalato (ter) and4-cyanopyridine(4-CNpy)asthecommonligands,viz.
[Ni(ter)2(H2O)4][Ni(4-CNpy)2(H2O)4].H2O (1) and [Ni(H2O)6] [Ni(ter)(4-CNpy)(H2O)4].(ter)(2) have been synthesized and structurally characterized. Compound 1 is triclinic (Pī) with= 90.342(2)˚,=unit cell parameters a = 6.3355(2)Å, b = 7.1529(3)Å, c = 20.3808(7)Å,3-3
96.227(1)°,= 114.980(2)˚, V = 830.89(5)Å , Z = 2, Dcalc.= 1.315g cm . The structure wassolved by direct method and refined by full-matrix least squares to final R1 = 0.0323, wR2 =0.0694 for 3991 reflections with I>2 (I)and 310 parameters. The asymmetric unitof 1 contains two Ni(II) centres having
different coordination spheres. One of the
ORTEP diagram of 1
Ni atoms contains two monodentate
terephthalate dianions and four water molecules whereas the other Ni centre contains two
4-cyanopyridine ligands and four water molecules.
Compound 2 is also triclinic (Pī) with unit cell parameters a = 6.2609(4)Å, b =12.1153(9)Å, c = 15.3239(11)Å, α = 78.479(1)˚, β = 86.865(1)°, γ = 79.698(1)˚, V =1120.36(14)Å3, Z = 2, Dcalc. = 0.942g cm-3. The structure refined to final R1 = 0.0291, wR2 =0.0774 for 5063 reflections with I>2 (I) and 409 parameters. Like 1, the asymmetric unit of
2 also contains two different Ni(II) centres. The neutral part which consists of a Ni2+ ion
surrounded by a monodentate terephthalate
dianion, an N-bound 4-cyanopyridine and fourwater molecules as ligands, while the positive
charge on the [Ni(OH2)6]2+ cation iscompensated by the presence of an
uncoordinated terephthalate dianion in the
ORTEP diagram of 2
crystal lattice.
Extensive hydrogen bonding interactions in both crystal structures lead to interestingsupramolecular architectures for 1 and 2 in the solid state.

P06-065

A NOVEL 3D INTERPENETRATING FRAMEWORK CONTAINING 1D
LADDERS COORDINATION POLYMERS WITH MIXED ORGANICLIGANDS: [Ni2(H2O)2(BDC)2(bpp)2]
Chia-Her Lin* and Tai-Hsing Tsao
Department of Chemistry, Chung-Yuan Christian University, Chungli 320, Taiwan*Corresponding author. Tel: +886-3-2653315; Fax: +886-3-2653399
E-mail address: chiaher@cycu.edu.tw (C. H. Lin).

A novel nickel (II) coordination polymer, [Ni2(H2O)2(BDC)2(bpp)2](1) (BDC = BDC= 1,4-benzene dicarboxylate anion; bpp = 4,4’-trimethylene dipyridine), was synthesized byhydrothermal reaction and structurally characterized. Single crystal X-ray diffraction showedthat 1 consists of a 3D framework contracture by interpenetrated 1D ladders. The luminescentand magnetic properties of 1 in the solid state were investigated.
Keywords:
Nickle, Crystal structure; Magnesium; Photoluminescence, hydrothermal Synthesis

P06-066

HYDROTHERMAL SYNTHESIS OF METAL HYDROXIDEIMIDAZOLIDE 3D FRAMEWORK POLYMERSFion T-Y. Yeong, Fanny L-Y. Shek, Herman H-Y. Sung and Ian D. Williams
Department of Chemistry, Hong Kong University of Science and Technology,
Clear Water Bay, Kowloon, Hong Kong, China.

Metal imidazolides [M(Im)2] are metal organic analogues of SiO2 and possess
tetrahedral metal centers with bent ligand bridges. They can be found in a variety of
topological networks similar to zeolites. (K.S. Park et al, Proc. Natl. Acad. Sci, 2006, 103,
10186) Little work has appeared on their hydrothermal preparation, however for zinc, cobalt
and cadmium facile preparation is possible under basic conditions. Other phase types havealso emerged from this work and we have now prepared three mixed imidazolide-hydroxides
with open 3D frameworks [Zn3(2-MeIm)5(μ-OH)] forms I and II (framework shown below)
and [Zn2(2-EtIm)3(μ-OH)]. Studies of the thermal stability and sorption character of these
new hybrid polymers and comparison with the [Zn(Im)2] parent materials are underway. The
Research Grants Council (HKSAR) is thanked for financial support of this work.

P06-067

SOLVING ZEOLITE STRUCTURES FROM POWDER DATA USINGDENSITY BUILDING FUNCTIONS AND HISTOGRAM MATCHING
Chris Gilmore, Gordon Barr, Wei Dong, Andrew Parkin, Duncan Sneddon, Chick Wilson
Department of Chemistry, University of Glasgow, Glasgow G12 8QQ,UK.

Cambridge Structural Database (CSD) searches can produce thousands of 'hits' especially
if a simple fragment is used, and as a result processing and interpreting the results becomes aconsiderable task, and one in which it is easy to make mistakes. Cluster analysis using
dendrograms, metric multidimensional scaling and suitable visualization tools can reduce theworkload to a few hours with minimal user intervention, and minimal user bias. The real beautyof the method is in its interactivity and scalability: it allows you to go from an overview of theentire dataset and easily spot any outliers or errors, to the ability to ‘drill down’ within a cluster,
looking at more and more detailed differences between different fragments. The computer
program we have developed to do this is dSNAP [1]. The formalism and the associated program
are also invaluable in a crystal engineering environment since it can readily identify the basic
motifs in a structure and how they pack in the unit cell. It is available free of charge to allinterested researchers from the web site http://www.chem.gla.ac.uk/snap
Reference:[1] G. Barr, W. Dong, C. J. Gilmore, A. Parkin and C. C. Wilson J. Appl. Cryst,. 2005, 38, 833-841.

P06-068

AN OBSERVATION ON THE WETTING PHENOMENON OFGALLIUM NANO DROPLETS BY X-RAY DIFFRACTION
Masanori Tanaka,a Takehiro Noda, aOsami Sakata,bHikaru Terauchi,a and Isao Takahashi aaFaculty of Science and Technology, Kwansei Gakuin University Sanda, Japan; bJapan Synchrotron

Radiation Research Institute, Sayo, Japan.

Precise measurements of the contact angle of droplet provide us fundamental
information on wetting phenomenon. Instruments for macroscopic observation like an optical
microscope with digital view-recording devices have usually been adopted for determining
the “macroscopic” contact angle. However, wetting is a cooperative phenomenon associatedwith microscopic interaction between substrate and numerous atoms. In order to comprehend
this phenomenon, it is thus critical to study the average contact angle and its deviation from it
for many droplets which consist of a relatively small number of atoms. Size dependence ofcontact angle of metallic substance gives us the essential knowledge which would encompass
all the mechanical properties of electrons dispersed into anion-core gels. In the present
study, we evaluate the average contact angle of nano-sized Ga droplets formed on an inert
diamond substrate by surface-sensitive X-ray diffraction techniques. So as to avoid theoxidation of Ga surface, whole the process was performed in an ultra high vacuum chamber
installed on a multi-axis diffractometer BL13XU, SPring-8. After annealing the diamond(100)substrate at 500oC, gallium was evaporated onto the substrate to form a 3.5nm thick Ga layer.
As surface-sensitive X-ray diffractions, we exploited X-ray Reflectivity (XR) and Grazing
Incidence Small Angle X-ray Scattering (GISAXS). The combination of XR and GISAXS isquite useful to construct the average shape of nano-sized droplets, since electron density
profile normal to the substrate surface is precisely obtained by XR and that in lateral direction
is easily evaluated from GISAXS.
We carried out the measurements of XR and GISAXS at various temperatures up too
500 C, where X-ray wavelength was 0.08nm and degree of vacuum was maintained better
than 1.67X10-5Pa. From the fitting procedures on XR and GISAXS data, the average contact
angle of nano-sized Ga droplets shows about 110 degrees, which is substantially smaller thanthat of macroscopic Ga droplets. Considerable variation in electron density and size of thedroplets is also confirmed.

P06-069

BEAM COMPRESSION AND LATTICE-CONSTANT VARIATIONS IN
CURVED X-RAY CAVITY
S.-Y. Chen,a Y.-Y. Chang,a Y.-J. Liu,a M.-T. Tang,b Yu. P. Stetsko,b H.-H. Wu,a Y.-R. Lee,aM. Yabashi,c B.-Y. Shew,b and S.-L. ChangaaDepartment of Physics, National Tsing Hua University; bNational Synchrotron Radiation ResearchCenter, Hsinchu, Taiwan, 300, R.O.C.; cSpring-8/RIKEN Mikazuki, Hyogo 679-5148, Japan

We report the unusual optical effects for curved multi-plate x-ray crystal cavities
consisting of compound refractive lenses (CRL). X-ray (12 4 0) back diffraction from thesemonolithic silicon crystal devices clearly showed interference fringes due to cavity resonance.
However, the expected focusing effect from the CRL was not observed, but rather beamcompression was detected. That is, the incident x-ray beam size of about 90μm across the
CRL was reduced to 20μm. The beam size remained the same at different positions after thecavity. Namely, a small sized parallel x-ray beam was produced. The origin of this beamcompression mechanism is believed to due to the competition between the multiple backreflection of the crystal cavity and the focusing of the CRL, in addition to crystal absorption.
On the other hand, when the photon energy was close to the exact energy for cavity
resonance, the exact energy required for resonance became very sensitive to the irradiatedposition on the cavity crystal. By tuning the crystal position along the wafer surface-normal
for the back diffraction, the nominal exact energy could vary. This meant the variation of thelattice constant at different crystal positions came into play. In turn, the analysis of the change
in the crystal positions and nominal exact energy allowed us to determine the local lattice
deformation. The lattice-constant variation resolved is of the order of 10-7 A°.

P06-070

DETERMINATION OF LATTICE PARAMETERS OF FeSi2/Si
QUANTUM DOT NANO-STRUCTURES BY X-RAY BRAGG-SURFACEDIFFRACTION
Yi-Wei Tsai,a Chia-Hung Chu ,a Wen-Ching Sun,a and Shih-Lin ChangaaDepartment of Physics, National Tsing Hua University, Hsinchu, Taiwan, R.O.C.

The method of using Bragg surface diffraction (BSD) for structural investigation of thinfilm/substrate systems has recently been introduced and demonstrated successfully forinterfacial strain analysis. With the BSD method, the strain field can be determined bymeasuring the variations of lattice constants of iso-strained substrate layers at different
penetration depths. This method is now applied to investigate the strain field of quantum dots
nano-structures of FeSi2/Si. Choosing one secondary diffracted beam along the interface(parallel to the surface of the substrate) between the quantum dots and the Si substrate, thediffraction images of the secondary diffraction, recorded on a charge coupled device (CCD),
provide the information of the interfacial structures. A theoretical model of X-ray scattering inquantum dots at the Bragg-surface diffraction geometry will be also reported.

P06-071

CRYSTALLINE LAMELLAE IN THIN FILM OF BIODEGRADABLEPOLYMER POLY(HYDROXYBUTYRATE) STUDIED BY SURFACE
X-RAY DIFFRACTION
Shota Mukoyama,a Kazuhiro Yamasaki,a Hikaru Terauchi,a Harumi Sato,a Yukihiro Ozaki,aIsao Noda,b and Isao TakahashiaaFaculty of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo 669-1337, Japan ;b

The Procter & Gamble Company, 8611 Beckett Road, West Chester, Ohio 45069, USA

Much attention has been paid to biodegradable polymers due to its biodegradability andpresumably due to the anxiety for our society deeply relying upon the limited petroleum.
Poly(hydroxybutyrate) (PHB) is one of the most studied polymers which shows decent
thermo-plasticity, high crystallinity and prompt biodegradability. A PHB-based random
copolymer
Poly(hydroxybutyrate-co-hydroxyhexanote)(P(HB-co-HHx))
indicates
remarkable flexibility because of its lower crystallinity. Our recent study revealed that interand intra-molecular interaction of C-H…O type along the a-axis plays an essential role forcrystallization, melting and morphology of lamellae crystallites embedded in bulk matrix [1].
In the present study, we focus on crystalline lamellae in ultrathin films of PHB and that of therandom copolymer, formed on Si substrates. The thin films were prepared by spin-coating
method with hot chloroform solutions. We exploit two surface-sensitive X-ray diffractions tocharacterize the polymer layers: one is X-ray reflectivity which affords nano-meter level
information on surface morphology such as average thickness, surface roughness and electron
density; the other is the grazing incidence X-ray diffraction (GIXD) for investigating
crystalline objects in surface region e.g., crystallinity, average crystallites size and preferredorientations. PHB thin films with a smooth surface are abtained only for samples withthickness less than 60nm. For P(HB-co-HHx), we form a fairly flat surface even for the films
with 120nm thick. From the GIXD data collected at various temperatures up to 130oC, we
find that unstable-type lamellae which would be referred to as loosely packed lamellae
display a novel thermal behavior in the surface region. In addition to the measurements statedabove, we study surface morphology of atactic PHB in which no crystallite is grown. It would
afford a clue to understand the effects of crystallinity on surface morphology.
Reference:[1]H.Sato et al., Macromolecules, 39(2006) 1525-1531

P06-072

CORE-SHELL COMPOSITION AND ITS INFLUENCES ON THE
PROPERTIES OF MATERIALSVo Vong a, Luu Tien Hunga and Michael HietscholdbaLaboratory of Electron Microscopy,Institute of Materials Science,Vietnamese Academy of Scienceand Technology;b Institute of Physics , Technical University of Chemnitz,Germany
18 Hoangquocviet str. Caugiay

Hanoi Vietnam

In recent years, nano materials have been widely applied in many fields of hightechnology . Besides scientists have been using the nano materials,which have core-shell
composition, in order to treat the dangerours diseases such the cancer. In these materials there
are two parts : The core and the shell. The first is the main one, which is a medicament or achemical substance . The second plays the role of showing the way. In other words , it directs
the core (medicament) to target ( cancer cells).
The nano materials are fabricated by special method and we received many sorts ofmaterials,which have core-shell composition. They are : 1) the volume of the core and theshell is the same 2) the volume of the core is biger than of the volume of the shell 3)
vice versa ,the volum of the core is smaller than of the volum of the shell.
In the paper we will present the details about preparation of these nano materials anddiscuss application in high technology and the life .

TEM image of the Sn(y)Ox sensor –material,which have core-shell composition

P06-073

GLASS TRANSITION TEMPERATURE OF ULTRATHIN POLYMERUNDER ULTRASLOW HEATING: AN X-RAY REFLECTIVITY STUDYON POLYSTYRENE FILMS SUPPORTED ON Si
Chun-Ming Yang, Hikaru Terauchi, and Isao Takahashi
Faculty of Science and Technology, Kwansei Gakuin University, Gakuen 2-1, Sanda 669-1337, JapanFor glass-forming polymers, glass transition temperature (Tg) is known to vary withheating/cooling rate. According to the cooperative molecular motion theory, the possible
lowest glass transition temperature TgL for bulk sample can be as low as ( (Tg determined byexperiments with conventional cooling rates) – 50K ). Whole the picture of glass transition
phenomenon would finally be understood in a hyper-phase diagram spanned by a combinationof non-thermodynamic variables like “time” and conventional thermodynamic variables
including pressure and temperature. For thin polymer films, “thickness” and “substrate”
should emerge as additional non-thermodynamic parameters. In the present study, we perform
precise measurements on X-ray reflectivity (XR) of thin polystyrene (PS) films under various
heating rates. Atactic PS thin layers were prepared by spin-coating method with Si substrates
and toluene solutions. Before the XR measurements, samples were annealed above bulk Tg for
12 h. The range of film thickness investigated is between 4 nm and 60 nm, which arecomparable to radius of gyration. Typical heating rate is 0.05 K/min. and 0.5 K/min., both ofwhich fully elucidate the temporal character of glass transition of ultrathin PS layers
supported by Si(100) wafers. From the thickness vs. temperature curve obtained under various
heating rates, substantial reduction in Tg is clearly observed for the sample with 5.8 nm thick;the glass transition temperature is evaluated as 333K ( = Tg(Bulk) – 40 K ) with heating rateof 0.05K/min. Systematic variations in Tg with heating rate and thickness are also confirmed.

P06-074

CRYSTAL STRUCTURE OF β-LACTOGLOBULIN AND VITAMIN DCOMPLEX. IDENTIFICATION OF A SECOND BINDING SITE FOR
VITAMIN D: A THERMAL INDEPENDENT SITE.
Hong -Hsiang Guan2,3, Ming -Chi Yang1, Ming -Yih Liu2, Jinn -Moon Yang1,Wen -Liang
Chen1, Simon JT Mao1 and Chun- Jung Chen2
1

College of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan

2Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu,

Taiwan3Institute of Bioinformatics and Structural Biology, National TsingHua University, Hsinchu, Taiwan.

β-lactoglobulin (β-LG) is a bovine milk protein sensitive to thermal denaturation
belonging to the lipocalin family. It is predominantly a β-sheet configuration containing
nine antiparallel β-strands from A to I, strands A-D form one surface of the barrel (calyx)
while strands E-H form the other. The only α-helical structure with three turns is at the
C-terminus, which follows strand H lying on the outer surface of the calyx. A remarkableproperty of the calyx is its ability to bind hydrophobic molecules such as retinol, fatty acids,
and vitamin D. Whether there is another binding site for vitamin D is physiologicallyimportant, but remains controversial. The opening of calyx (located at the EF loop) is
responsible for the entrance of vitamin D and such binding ability of β-LG is
conformationally and pH dependent known as Tanford transition. In the present study, weobserved that the molar binding ratio between vitamin D to β-LG was 2:1 at pH above theTanford transition, but for retinol and palmitate was 1:1. However below the transition (pH2-6), only vitamin D was able to retain the binding with a ratio almost 1:1. We also
observed that heating β-LG above 80°C abolished its binding to retinol and palmitic acid,
while heated β-LG (heated at 100°C for 16 min) still binding to vitamin D3. Titration curveshows the maximal binding ratios of heated β-LG to vitamin D3 to be 1:1. Taken together,
the data suggest that there is a second binding site beyond the calyx that is specific only forvitamin D3, but not for retinol and palmitate. Using synchrotron X-ray diffraction on the
crystal of β-LG-vitamin D3 complex (at a resolution 2.4 Å, R = 0.2369, Rfree = 0.2989; spacegroup P3221 with unit-cell parameters a = b =53.78 Å and c = 111.58 Å), we demonstrate thatone vitamin D3 molecule bound to the calyx (central binding site) of β-LG and the otherbound to a specific remote exosite. It is located near the surface of C-terminal -helix(residues 130-141) and -strand I (residues 146-151), where the OH group of vitamin D3
interacts with 1 N of Arg-148. This binding domain provides strong van der waals forces
to stabilize vitamin D3 binding, whereas the charged group of Asp-137, Lys-138, and Lys-141
congregate and stick outside of the binding pocket and therefore enhance the hydrophobic
interaction between the exosite and vitamin D3. The significance and physiologic role ofthis additional binding site is discussed in the light of vitamin D supplemented milk.

P06-075

NANOSTRUCTURED FILMS CONSTITUTED OF TiO2 AND SnO2
PREPARED BY MEANS OF SPRAY PYROLYSIS
Pham-Van Nhoa, Pham-Hoang Nganb, Tran-Kim CuongcabApplied Physics Lab, Hanoi University of Science, and Faculty of Engineering Physics and NanocTechnology, College of Technology, Vietnam National University, Hanoi; Faculty of Physics, Dalat
University, Dalat City,Vietnam

Nano TiO2 is one of the perspective materials in nanoscience and nano technology. This
material has been effectively applied to photo catalysis for environmental purification, photoelectrochemical solar cell…However, in order to heighten efficiency, nano TiO2 is usuallyused in the form of as either dye sensitized or nitrogen doped materials...
In this work we present another way to enhance activities of TiO2 materials. That is the
preparation of TiO2 in conjugation with SnO2 using spray pyrolysis technique. The starting
materials are solutions from commercial TiCl4 and SnCl4, which were sprayed by help of theatomizer operated by pressed air. Solutions were sprayed onto glass slide substrates preheated
up to 400oC under open air condition. At high temperature pyrolysis of chloride salts weretook place resulting in the formation of the films of nano TiO2 crystalline and SnO2. Obtained
films were characterized by XRD and SEM and photoconductivity measurement. It was foundthat in this method TiO2 was deposited in anatase phase with average crystalline size of
15-20nm and photoelectrical properties of it strongly depends on both SnO2 concentration andmethod of spraying constituent solutions.
This is inexpensive method but obtained results have been successfully used for
manufacture of high performance UV detectors. They also can be applied to photoelectrochemical solar cell based on nano crystalline TiO2.
Corresponding Author: Pham Van Nho, nhopv@vnu.edu.vn

P06-076

STRUCTURAL STUDY OF ARSENATE INCORPORATION INTOCALCIUM PHOSPHATE HYDROXYAPATITE
Winya Dungkaew*, Weenawan Somphon**, Kenneth J. Haller**School of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon
Ratchasima,Thailand ** National Synchrotron Research Center (NSRC), Nakhon Ratchasima,
ThailandCalcium Phosphate Hydroxyapatite (Ca10(PO4)6(OH)2, CaHAP) is a naturally occurring
material as a major component of animal bones and teeth. Apatite structure[(AI4)(AII6)((BO4)6)X2] contains several exchangeable positions resulting in the apatite
structure being tolerant to ionic substitutions. Due to this property CaHAP has been widelyused as a host for heavy metal substitution for contaminant immobilization. CaHAP has also
been considered as an ideal adsorbent for long term storage due to its high sorption property,high stability under reducing and oxidizing conditions, low water solubility, and low cost.
The structural study of arsenate incorporated CaHAP structure was performed. The
effect of the amount of arsenate incorporation on the CaHAP structure was investigated using
XRD and Ca K-edge XAS (XANES and EXAFS) techniques at the Siam Photon Laboratoryof the National Synchrotron Research Center (NSRC). This study is useful in understanding
arsenate immobilization using CaHAP. Arsenate immobilization occurs by incorporating
arsenate into CaHAP structure at phosphate positions due to the similarity of arsenate andphosphate.

P06-077

STRUCTURAL STUDY OF COPPER INCORPORATION INTOCALCIUM PHOSPHATE HYDROXYAPATITE
Oratai Saisa-ard, a Winya Dungkaew, a Weenawan Somphonb and Kenneth J. Haller aaSchool of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasimab

30000 Thailand. Siam Photon Laboratory of the National Synchrotron Research Center (NSRC),
Nakhon Ratchasima 30000 Thailand.

Calcium phosphate with apatite structure [Ca10(PO4)6(OH)2, CaHAP] crystallizes in the
hexagonal space group P63/m. The CaHAP structure consists of a calcium/phosphate
framework surrounding a pseudo hexagonal channel as shown in the figure. The material can
accept a series of cationic and anionic substitutions in its structure, both in the framework
itself and inside the hexagonal channel. From this property CaHAP has been proposed for theremoval of heavy metal from wastewater.
Cu2+ ions can ions exchange with Ca2+ ions in the CaHAP structure resulting in copper
immobilization. Substitution of Cu2+ at Ca2+ positions affects the CaHAP structure due to theirdifferent sizes. This work studies the structure of copper incorporation into CaHAP based on
XRD and Ca K-edge XAS (XANES and EXAFS) techniques.
Acknowledgement: OS and WD thank the Thai government for supporting this work throughPh.D. scholarships.

P06-078

CHROMIUM AND CADMIUM IMMOBILIZATION BY PORTLAND
CEMENT SOLIDIFICATION
Weenawan Somphon, a Samroeng Krachodnok,b Angkana Kiatpichitpong caNational Synchrotron Research Center (NSRC), Nakhon Ratchasima 30000 Thailand; bSchool ofChemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000
Thailand; cThai Pride Cement Co., Ltd., Saraburi 18110 Thailand.

Cement-based solidification/stabilization (S/S) is an important technology used forheavy metal immobilization due to low water solubility, non-flammability, durability, and low
cost of the final materials. Ordinary Portland Cement (OPC) is the most common cementbinder in S/S technology. This research aims to improve understanding of the chromium andcadmium immobilization process. The mechanisms of S/S technology for toxic metal
immobilization are significantly controlled by surface, near-surface, and interfacial
phenomena. OPC was mixed with K2Cr2O7 (Cr6+), Cr2O3 (Cr3+), and Cd(NO3)2·4H2O (Cd2+).
The pH value of the cation solutions was varied between 6 and 8. The mixture was cured atroom temperature for 7 and 28 days, and the analyzed using XRD and SEM. X-Ray
Photoemission Spectroscopy (XPS) was used for chemical analysis on the cement surface.
X-Ray Absorption Spectroscopy (XAS) was then applied to powder samples to examine of
the hydration state of chromium and cadmium.

P06-079

NANOCRYSTALLINE COPPER SULPHIDE: SYNTHESIS AND ITS
CHARACTERIZATION
N.Vasumathi, B.B.Nayak and B.S.Acharya
Materials Characterization Dept., Institute of Minerals and Materials Technology, Bhubaneswar,
Orissa, India – 751013.

Copper chalcogenides have been studied for their use as optical filter, solar cellmaterials and superionic materials. Although several methods like templated assisted
sonochemical synthesis, hydrothermal synthesis and facile solution reaction in ethylene glycol
etc have been proposed, large scale preparation of copper monosulphide in nano regime has
not been successful so far. In the present investigation, the authors have modified techniqueproposed by Wu et al (J.Am.Chemical Soc.June-2006) to produce CuS nanospheres having
size in the range of the 10nm to 250nm.
The powders were characterized by x-ray diffraction, transmission electron microscopy
and laser raman spectroscopy. X-ray diffraction studies reveal the average crystallite size to be
14nm and the phase identified to be Cu1.8S (PDF card no 646) with hexagonal structure.
Morphological study of the powder was carried with a high resolution TEM (TechnaiG20 –200KV). Two types of particles were observed; one in the size range of 10nm to 60nm andanother in the range of 150nm to 250nm, also particles were spherical in nature. Selected area
diffraction pattern of these particles confirm the monophasic nature of CuS. The powder wastested for its stability at room temperature (≈ 27°C). The nano CuS powders kept at RT for 6
months show interesting result as regards the laser raman spectra are concerned. The raman
spectra observed for freshly synthesized CuS and 6 months stored CuS powders were 162,
275, 479, 1453 and 172, 494, 1262, 1444 cm-1 respectively. The sharp band observed at
479cm-1 for as prepared Cu1.8Scm-1 shifts to 494cm-1 when the sample was stored at RT for
180days. Although structurally, the sample remains the same, the size of the crystallites
reduces to 8.0nm. These observations have been confirmed from TEM photographs and size
distribution analysis. This indicates that surface oxidation plays an important role inamorphization of the sample thereby reducing the particle size and shifting the raman peak tohigh wavenumber side. These results will be presented and discussed in this paper.

P06-080

X-RAY DIFFRACTION STUDY ON THERMAL BEHAVIORS OF
SHAPE MEMORY ALLOY AU50.5CD49.5
Michinori Yoshikawa,a Genki Kikuma,a Takuya Ohba,b Hikaru Terauchi,a and Isao
Takahashi aaFaculty of Science and Technology, Kwansei Gakuin University, Sanda, Japanb

Interdiscipilinary Faculty of Science and Engineering Shimane University, Matsue Japan.

Martensitic transformation is a diffusionless transformation which is considered to servea substantial role for both of the shape memory effect and superelasticity in Shape Memory
Alloys (SMA). Although the Martensitic transformation is a cooperative phenomenon in solidstates, conventional thermodynamic variables e.g., temperature, pressure, are insufficient todetermine the physical properties of SMA; additional parameters like heating rate, coolingrate, ageing time, and thermal history etc., sometimes greatly affect them. Au50.5Cd49.5 is oneof the most intensively studied SMA which also exhibits superelasticity. The parent phase of
the CsCl-type is stable above 309K. Under cooling, it undergoes a transformation to thetrigonal phase (ζ’2 phase) at 303K. Theζ’2 phase consists of a multi-domain structure called
variant [1]. Despite the large number of published papers, information on spatial-temporaldevelopment of domain structure in bulk as well as in the surface region seems to be highly
limited. In the present study, we investigate the time & temperature dependent domain
formation of Au50.5Cd49.5 by exploiting X-ray diffraction techniques.
An electro-polished 112 surface of Au50.5Cd49.5 with 5mmX5mm in area was prepared tomeasure the (112) Bragg reflection and X-ray reflectivity. High resolution diffractometers
equipped with rotating-anode X-ray generators were used (Rigaku TTR-450,
SLX2000+UltraX). For measurements of temporal fluctuations, synchrotron radiation at
BL13XU, SPring-8 was also used. The temperature varied from the room temperature to350K within a precision of 0.1K. The (112) reflection is measured by longitudinal andtransverse scans, usually referred to as ω scan and θ-2θscan respectively. X-ray reflectivity iscollected with a very shallow angle of incidence close to the critical angle of total reflection.
A peak splitting of (112) Bragg reflection and that of X-ray reflectivity is clearly observed
throughout the transformation, indicating the domain formation. Inζ’2 phase, long-tailed
fluctuations in (112) reflection are observed, although the X-ray reflectivity does not show the
fluctuation of this type.
Reference:[1]T. Ohba and K. Otsuka, Jpn.J.Appl.Phys.Vol37 (1998) L64-L66

P06-081

OBSERVATION ON TRANSITIONS IN SURFACE REGION OF
COCOA BUTTER BY X-RAY DIFFRACTION
Yusuke-Hayashi,a Yoshihito-Uozaki,a Hikaru-Terauchi,a and Isao-TakahashiaaDepartment of Science and Technology, Kwansei Gakuin Universiy, Hyogo,Japan

Cocoa butter, which constitutes chocolate, is known to have at least six phases [1].
There are a lot of studies on phase transition of bulk cocoa butter, but little has been reported
on surface. In this paper, we perform comparison between phase transitions in bulk and thosein the surface region by combination of conventional wide angle X-ray diffraction (WAXD)
and surface sensitive X-ray diffraction techniques. As for the X-ray diffraction forinvestigating the surface region, we exploited X-ray reflectivity (XR) and grazing incident
X-ray diffraction (GIXD). XR gives us information on sample surface, e.g., thickness,
electron density, and roughness of surface. GIXD detects the crystal structure, crystallinity,
preferred orientations of crystalline in surface region.
Naturalcocoa
butteriscomposedofsomesimilaroils:
POP(sn-1,3-dipalmitoyl-2-oleoylglycerol), SOS (sn-1,3-dipalmitoyl-2-stearoyl-glycerol), POS(1,3-rac-palmitoyl-stearoyl-2-oleoylglycerol). Thin films of cocoa butter are formed on
Si(100) wafers by spin coating method. Since the melting points of polymorphisms of cocoa
butter are I: 17.3oC, II: 23.3oC, III: 25.5oC, IV: 27.5oC, V: 33.8 oC, and VI: 36.3 oC in bulk,
we measured XR and GIXD of thin film in this temperature range.
Figure1 shows XR at various temperatures. At 24oC, thickness of the cocoa butter layer
is estimated as 4.8 nm. With elevating the temperature, coverage of the layer increased from
80% to 100% indicating the formation of completely wetting layer. Increase in the thickness
was also recognized presumably due to the melting of residual cocoa butter particles which
incoherently scatter X-ray. Results on GIXD3 will also be discussed.
45℃

2
1

R eflectivity

0

36℃
24℃

-1
-2
-3
-4
-5

Fig.1

-6
0.0

0.5

1.0

θ [deg]Reference:[1] R.L. Wille and E.S. Lutton : J. Am. Oil Chem. Soc. Vol.43, 491 (1966)

1 .5

2 .0

2.5

P06-082

COMPARATIVE STUDY ON THE I-V CHARACTERISICS OF METALSTRING COMPLEXES EXPERIMENT VS THEORY
Liang-Yan Hsu, Bih-Yaw Jin, Chun-Hsien Chen, Shie-Ming Peng
Department of Chemistry, National Taiwan University, Taipei, 106, Taiwan.
Institute of Chemistry, Academia Sinica, Taipei, 115, Taiwan.
smpeng@ntu.edu.tw; Tel:(886)-2-2363-8305; Fax:(886)-2-8369-3765

I. Linear Metal String Complexes 1, 2, 3
＊ Synthesis, Structure, Bonding

X

N

N

N

N

M

M

M

M

N
m

M

4
X

M = Ni, Co, Crm = 0, 1, 2, 3
X = Cl, NCS

II. Potential Application as Molecular Metal Wires & Molecular Switches 4,5＊ STM Study on the Conductivity of Metal Strings＊ C-AFM Measurements of Single Metal String Molecules＊ Comparative Study on the I-V Characterisics (Theory V.S. Experiment)
III. Tuning of the Metal Strings 6＊ Naphthyridyl Amino Ligands: Low Oxidation Mixed Metal Strings＊ Asymmetrical Ligands: Toward Molecular Rectifier
IV. Conclusion
Reference:
1. C.-Y. Yeh, C.-C. Wang, Y.-H. Chen and S.-M. Peng, in Redox Systems Under
Nano-Space Control, Ed: T, Hirao, Springer, Germany, 2006, Ch. 5.
2. S.-Y. Lai, T.-W. Lin, Y.-H. Chen, C.-C. Wang, G.-H. Lee, M.-H. Yang, M.-K. Leungand S.-M. Peng, J. Am. Chem. Soc., 1999, 121, 250.
3. S.-J. Shieh, C.-C. Chou, G.-H. Lee, C.-C. Wang and S.-M. Peng, Angew. Chem. Int.
Ed. Engl., 1997, 36, 56.
4. S.-Y. Lin, I.-W. P. Chen, C.-H. Chen, M.-H. Hsieh, C.-Y. Yeh, T.-W. Lin, Y.-H. Chen
and S.-M. Peng, J. Phys. Chem. B, 2004, 108, 959.
5. I.-W. P. Chen, M.-D. Fu, W.-H. Tseng, J.-Y. Yu, S.-H. Wu, C.-J. Ku, C.-H. Chen, and
S.-M. Peng, Angew. Chem. Int. Ed. Engl., 2006, 5414.
6. (a) C.-H. Chien, J.-C. Chang, C.-Y. Yeh, G.-H. Lee, J.-M. Fang and S.-M. Peng,
Dalton Trans., 2006, 2106. (b) C.-H. Chien, G.-H. Lee, Y. Song and S.-M. Peng,
Dalton Trans., 2006, 3249.

P06-142

CRYSTAL STRUCTURES OF THE CYTOSOLIC DOMAIN OF THE
Mg2+ TRANSPORTER MgtE
Yoshiki Tanaka a, Motoyuki Hattori a, Shuya Fukai b, Ryuichiro Ishitania and Osamu NurekiaaDepartment of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo

Institute of Technology, Yokohama, Japan; bCenter for Biological Resources and Informatics, Tokyo
Institute of Technology, Yokohama, JapanThe magnesium ion, Mg2+, is one of the most abundant divalent cations in biologicalsystems and is vital for all living organisms. Three distinct classes of Mg2+ transporters havebeen identified from eubacteria and archaea. The MgtE Mg2+ transporter, which is
ubiquitously conserved in all of the kingdoms of life, has not been thoroughly characterized,
and it is not even clear whether MgtE acts as a channel or an active transporter. MgtE consistsof an N-terminal cytosolic domain and a C-terminal transmembrane domain. The cytosolic
domains include a cystathionine-β-synthase (CBS) domain, which reportedly plays aregulatory function in other transporter proteins, e.g. human chloride channels and theosmoregulated ABC transporter, OpuA. Therefore the cytosolic domain of MgtE is expected
to have a regulatory function.
We solved the structures of the cytosolic domain of the MgtE in the presence andabsence of Mg2+ at 2.3 Å and 3.9 Å resolutions, respectively. The cytosolic domain consistsof two subdomains. The N-terminal subdomain (N domain) forms a right-handed superhelix.
The C-terminal subdomain is composed of typical duplicated CBS domains. In the cytosolic
domain structure in the presence of Mg2+, the electron densities presumably corresponding to
Mg2+ were clearly observed between the N and CBS domains, and might be related to aregulatory function.
A structural comparison of the cytosolic domains in the presence and absence of Mg2+
revealed that the domain organization is drastically changed. Such domain reorganization
might be essential for gating of the MgtE pore.

P06-143

CRYSTAL STRUCTURE OF THE MgtE Mg2+ TRANSPORTER
Motoyuki Hattori a, Yoshiki Tanaka a, Shuya Fukai b, Ryuichiro Ishitania and Osamu NurekiaaDepartment of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo

Institute of Technology, Yokohama, Japan; bCenter for Biological Resources and Informatics, Tokyo
Institute of Technology, Yokohama, JapanThe magnesium ion, Mg2+, is one of the most abundant divalent cations in biologicalsystems and is vital for all living organisms. Mg2+ has the largest hydrated radius among all
cations, while its ionic radius is the smallest. It remains obscure how Mg2+ transporters
selectively recognize and dehydrate the large, fully-hydrated Mg2+ cation for its transport.
The MgtE family of Mg2+ transporters is ubiquitously distributed in all three kingdoms,
and human homologues were functionally characterized and suggested to be involved inmagnesium homeostasis However, the MgtE transporters have not been thoroughly
characterized, and it is even not clear whether MgtE works as a channel or an active
transporter.
We determined the crystal structure of the full-length Thermus thermophilus MgtE at
3.5 Å resolution. The transporter adopts a homodimeric architecture, consisting of the
C-terminal five transmembrane (TM) domain, and the N-terminal cytosolic domains,
composed of the superhelical N domain and the following typical duplicatedcystathionine-β-synthase domains, which reportedly plays a regulatory function in othertransporter proteins, e.g. human chloride channels and the osmoregulated ABC transporter. A
solvent-accessible pore nearly traverses the TM domains, with one potential Mg2+ bound tothe conserved Asp residues within the pore, which might be related to the ion selectivity by
MgtE. The TM5 helices from both subunits close the pore through interactions with the“connecting helices”, which connect the cytosolic and TM domains. Four putative Mg2+ ionsare bound at the interface between the connecting helix and the other domains, which may
lock the closed conformation of the pore. A structural comparison of the Mg2+-bound andMg2+-free cytosolic domains showed the Mg2+-dependent movement of the connecting helices,which might reorganize the TM helices to open the pore. These findings suggest a Mg2+
homeostasis mechanism, in which the cytosolic domains regulate the gating of the pore bysensing the intracellular Mg2+ concentration.

P06-144

STRUCTURAL BASIS OF PROSTACYCLIN BIOSYNTHESISYi-Ching Li1, Chia-Wang Chiang1, Hui-Chun Yeh2, Frank G. Whitby3, Lee-Ho Wang2, and
Nei-Li Chan1
1

Institute of Biochemistry, College of Life Sciences, National Chung Hsing University, Taichung City

402, Taiwan.
2

Division of Hematology, Department of Internal Medicine, University of Texas Health Science Centerat Houston, 6431 Fannin, Houston, TX 77030, USA.
3

Department of Biochemistry, 15 North Medical Drive East, Room 4100, University of Utah, Salt Lake

City, UT 84103, USA

Prostacyclin synthase (PGIS) converts prostaglandin H2 to prostacyclin, which is ahighly potent vasodilator and inhibits platelet aggregation. This enzyme is located to theendoplasmic reticulum membrane and was assigned to the P450 superfamily as CYP8A1
when its cDNA sequence was determined. Unlike other microsomal P450s that catalyze
mono-oxygenation or hydroxylation reaction, PGIS catalyzes an isomerizaton and does notneed molecular oxygen, reductase or any other external electron donor. Various genome
projects have identified PGIS-like sequence in the animals as low as amphibians and fish(http://drnelson.utmem.edu/CytochromeP450.html), suggesting that PGIS emerged early invertebrate evolution. Using the recombinant human PGIS obtained from a prokaryotic
expression system, we had previously determined the crystal structure of this atypical and yetphysiologically important P450 in its ligand-free state. However, critical questions regarding
the regioselectivity of PGIS-catalyzed isomerization and the catalytic roles of active residues
remain to be answered. To this end, we have now determined the crystal structures of theligand-free and substrate analog-bound zebrafish PGIS. The structural basis for theregioselectivity and how the enzyme may facilitate the isomerization reaction wererecognized. In addition, the substrate entrance and product exit channels of PGIS wereidentified. Detail structural analysis and functional significance of the ligand-bound zPGIS
will be presented and discussed.

P06-145

STRUCTURAL STUDIES OF THE HUMAN PROSTACYCLINSYNTHASE
Chia-Wang Chiang1, Hui-Chun Yeh2, Lee-Ho Wang2*, and Nei-Li Chan1*
1Institute of Biochemistry, College of Life Sciences, National Chung Hsing University, Taichung City

402, Taiwan.
2

Division of Hematology, Department of Internal Medicine, University of Texas Health Science Centerat Houston, 6431 Fannin, Houston, TX 77030, USA.

Prostacyclin synthase (PGIS) catalyzes an isomerization of prostaglandin H2 toprostacyclin, a potent mediator of vasodilation and anti-platelet aggregation. Here we report
the crystal structure of human PGIS (hPGIS) at 2.15 Å resolution, which represents the first
three-dimensional structure of a Class III cytochorme P450. While notable sequence
divergence has been recognized between PGIS and other P450s, hPGIS exhibits the typicaltriangular prism-shaped P450 fold with only moderate structural differences. The conserved
acid-alcohol pair in the I helix of P450s is replaced by residues G286 and N287 in hPGIS, but
the distinctive disruption of I helix and the presence of a nearby water channel remain
conserved. The side chain of N287 appears to be positioned to facilitate the peroxide bondcleavage, suggesting a functional conservation of this residue in activating oxygen. A
combination of bent I helix and tilted B’ helix creates a channel extending from the heme
distal pocket, which seemingly allows binding of various ligands; however, residue W282,
placed in this channel at a distance of 8.4 Å from the iron with its indole side chain lying
parallel to the porphyrin plane, may serve as a threshold to exclude most ligands from binding.
In addition, we have also determined the crystal structure of hPGIS in complex with the
known inhibitor minoxidil at 1.62 Å. A clear piece of electron density in the heme distal
pocket which corresponds to the bound minoxidil was easily recognized in the weighted
Fo-Fc map. Interestingly, in contrast to the previous thought that a primary amine nitrogenmay serve as the distal ligand, it was found that the oxygen of minoxidil is ligated to theheme-iron at a distance of 2.2 Å. The minoxidil binding prompts the formation ofwater-mediated hydrogen bonds between the heme propionates and residues from the B and C
helices, turning the termini of both helices toward the heme. The functional significance of
these findings will be presented during the meeting.

P06-146

HIGHLY AMPHIPHILIC INTERFACE IN THE COMPLEX FORMED
BETWEEN DPPIV (CD26) AND ADENOSINE DEAMINASE
Wolfram Saengera, Wilhelm A. Weihofena, Jiango Liub, Werner Reutterb, Hua FanbaInstitute for Chemistry and Biochemistry/ Crystallogra- phy, Freie Universitaet Berlin, Takustrasse 6,

D-14195 Berlin, Germany. bInstitute for Molecular Biology and Biochemistry,
Charité-Universitaetsmedizin Berlin, Arnimallee 22, D-14195 Berlin, Germany
E-mail: saenger@chemie.fu-berlin.de

Dipeptidyl-peptidase IV (DPPIV or CD26) is a homodimeric type II membrane
glycoprotein in which the two monomers are subdivided into a propeller domain and an
α/β-hydrolase domain.
As dipeptidase, DPPIV modulates the activity of various biologically important peptides
and, in addition, DPPIV acts as a receptor for adenosine deaminase (ADA), thereby mediating
co-stimulatory signals in T-lymphocytes.
The 3.0 Å resolution crystal structure of the complex formed between human DPPIV
and bovine ADA presented here shows that each β-propeller domain of the DPPIV dimerbinds one ADA [1]. At the binding interface, two hydrophobic loops protruding from theβ-propeller domain of DPPIV interact with two hydrophilic and heavily charged α-helices of
ADA, giving rise to the highest percentage of charged residues involved in a protein-protein
contact reported thus far. Additionally, four glycosides linked to Asn229 of DPPIV bind to
ADA. In the crystal structure of porcine DPPIV, the observed tetramer formation was
suggested to mediate epithelial and lymphocyte cell-cell adhesion [2]. ADA binding to DPPIV
could regulate this adhesion, as it would abolish tetramerization.
Reference:[1] Weihofen W. A., Liu J., Reutter W., Saenger W., Fan H., J. Biol. Chem. 2004, 279, 43330..
[2] Engel M., Hoffmann T., Wagner L., Wermann M., Heiser U., Kiefersauer R., Huber R.,
Bode W., Demuth H.-U., Brandstetter H., Proc Natl Acad Sci U S A 2003, 100, 5063.

P06-147

CRYSTAL STRUCTURE OF BOVINE LACTOPEROXIDASE AT 2.3 Å
RESOLUTION
Amit Kumar Singh, Nagendra Singh, Sujata Sharma, Mau Sinha, Punit Kaur, A. Srinivasan
and T. P. Singh
Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India, 110029

Lactoperoxidase (LPO, E.C. 1.11.1.7) is a redox enzyme with antibacterial properties
found in several biological fluids, like milk, tears, saliva etc. In vivo, LPO catalyzes theoxidation of thiocyanate, iodide and bromide. The crystal structure of bovine lactoperoxidase(CLPO) has been determined at 2.3 Å resolution. It crystallizes in space group P21 with unit
cell dimensions, a = 53.9 Å, b = 80.0 Å, c =75.7 Å and β = 103.2°. The structure has beenrefined to an R – factor of 23.1 % (R free = 24.7 %). The structure revealed the presence of aheme group which is covalently attached to the protein via two ester linkages between
carboxyl groups of Glu258 and Asp108 and modified methyl groups on pyrrole rings A and Cof the heme. Ser198 is phosohorylated in CLPO, which apparently facilitates the intake ofcalcium ion. The calcium ion forms distorted pentagonal bipyramidal coordination. Sixteen
anion-binding sites have been observed in the structure. The amino acid sequence of CLPO
reveals four potential N- gycosylation sites, with Asn-X-Ser/Thr sequence motifs, these are at
Asn95, Asn205, Asn205, Asn332 and structure shows that all the four sites are actuallyglycosylated. The structure shows five buried water molecules and His266 form a chain ofhydrogen bonds extending from the Nδ of the distal His109 to the surface of molecule.

P06-148

CRYSTAL STRUCTURE OF CAMEL PEPTIDOGLYCANRECOGNITION PROTEINS AT 3.0 Å RESOLUTION
Pradeep Sharma, Nagendra Singh, Sujata Sharma and T.P.Singh
Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India, 110029

Peptidoglycan recognition protein (PGRP) is a soluble, conserved pattern recognition
protein of vertebrates and invertebrates that binds to peptidoglycans (PGNs). PGNs forms agroup of conserved microbial motifs (Pathogen- associated molecular patterns- PAMPs) thatare unique products of microbial metabolism not produced by the host. PGNs are located on
the surface of virtually all bacteria and fungi as such, constitute excellent targets torecognition by PGRP. We have isolated a 20 kDa PGRP from camel mammary secretions. It
has been crystallized in the space group I 222 with cell dimensions, a =89.9Å, b = 102.5Å, c =164.2Å with 32 molecules within unit cell. The structure reveals the presence of a tertramericassociation unlike human PGRP, which is monomer. PGN binding groove is located in thedomain close to C-terminus. The molecular structure contains a central β-sheet composed offive β-strands, four parallel and one (β5) antiparallel and three α- helices. PGN binding site
resides in a long cleft whose walls are formed by helix α1 and five loops β3 – α1, α1- β4, β5 –β6, β6 – α2 and β7 – α3. The second site is located on the opposite side of the protein to the
PGN- binding site, apparently accommodates host effector or signaling molecules. It is
formed by the variable PGRP-specific segment and helix α2.

P06-149

CRYSTAL STRUCTURE OF THE COMPLEX OF SHEEP SIGNALINGGLYCOPROTEIN WITH 2-METHYL-2,4-PENTANEDIOL AT 1.65Ǻ
RESOLUTION
Mau Sinha, Pradeep Sharma, Nagendra Singh, Sujata Sharma, Punit Kaur and Tej P. Singh
Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India

The onset of the involution represents a period of large scale tissue remodeling in
mammary glands. During this process the production of a new class of signaling
glycoproteins is induced that binds to viable tissues and protect s them from programmed
apoptosis. The binding proteins are designated as SPX-40 where X represents a species with amolecular weight of 40 kDa. The present protein is isolated from sheep dry secretions which
crystallized in orthorhombic space group P212121 with cell dimensions, a=62.9Ǻ, b=66.4Ǻ,c=105.7Ǻ having four molecules in the unit cell. The structure was determined by molecularreplacement method and refined to a R factor of 16.7% (Rfree=21.7%) using data to 1.65Ǻ
resolution. A Ramachandran plot for the whole molecule shows 92.1% of residues in the mostfavoured regions and 7.9% in the additionally allowed regions. The structure reveals that theligand binds in the sugar-binding groove with protein residues Trp10, Arg14, Tyr185 andTrp331 involved in direct interactions whereas residues Thr8, Tyr120, Arg242 and Asp334
interact through solvent water molecules. Residues Trp78, Leu183, Tyr185, Asp186, Ile 272
and Thr267 form Van der Waals interactions. The overall strength of interactions is of theorder of 10-8M.

P06-150

CRYSTAL STRUCTURES OF COMPLEXES OF C-LOBE OF BOVINELACTOFERRIN WITH VARIOUS SACCHARIDES AT HIGHRESOLUTIONS REVEAL A COMMON BINDING SURFACE IN THE
C-LOBE
Rafia Mir, Mau Sinha, Nagendra Singh, Vikram Gopalakrishnapillai, Sujata Sharma, Punit
Kaur and Tej.P.Singh
Department Of Biophysics AIIMS, New Delhi India

Lactoferrin is a monomeric, iron binding 80kDa glycoprotein with antibacterial activity
against Helicobacter pylori. In order to understand the role of lactoferrin against gastricdamage caused by NSAIDS and bacterial colonization, a number of crystal structures ofcomplexes of C-lobe of bovine lactoferrin with various saccharides were determined.
Lactoferrin was proteotically cleaved into N- and C-lobes. The structure of C-lobe wasdetermined at high resolution. It revealed the presence of the shallow saccharide binding site.
C-lobe was crystallized with at least more than two dozens of different mono- anddi-saccharides. The structures of these complexes showed that all the sugars bind at the samesite but the numbers of interactions were different between the C-lobe and sugars indicatingvarying degree of affinities between them. The sugars used in the complexes were: Lactose,
maltose, galactose, glucose, xylose, mannose, sucrose, fucose, N-acetylglucoseamine,cellobiose, raffinose, sorbitol, trehalose, melibiose, rhamnose, arabinose, melezitose, fructose,
ribose, N-acetylgalactoseamine, methyalpha-D-mannopyranoside, adenosine, trisaccharide,
tetrasaccharide, pentasaccharide. The resolution of structures varied from 1.5Å to 2.8Å. The
protein residues that were involved in the interactions with ligands were Glu 659, Tyr 660,
Leu 661 and Glu 664.

P06-151

CRYSTAL STRUCTURE OF GOAT LACTOPEROXIDASE AT 2.4ǺRESOLUTION
Nagendra Singh, Amit Kumar Singh, Sujata Sharma, Asha Bhushan, Punit Kaur and Tej P.
SinghDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi-110029, India

Lactoperoxidase (LPO) is a Fe (III) – heme enzyme belonging to the mammalianperoxidase family. LPO catalyzes the oxidation of SCN- to hypothiocyanate. This enzyme wasisolated from goat secretion. It was sequenced and crystallized. The crystals diffracted to 2.4Ǻresolution and belong to monoclinic space group P21 with cell dimensions, a=54.2Ǻ, b=80.8Ǻ,
c=77.0Ǻ, β=102.9°. The first crystal structure has been determined by molecular replacement
method and refined to an R factor of 0.196 (Rfree=0.203). The structure shows that the hemegroup is covalently bonded to the protein via two ester linkages between the carbonyl groupsof Glu258 and Asp108 and modified methyl groups on pyrrole rings A and C of the heme. The
iron is positioned slightly to the proximal side. On the distal side a funnel shaped channel
filled with water molecules leads from the narrow opening to the surface of the protein. The
distal heme cavity is occupied by the side chains of Glu105, His109 and Arg255 together withfive water molecules. The structure also has a calcium binding site with typical pentagonal
bipyramidal coordination geometry.

P06-152

CRYSTAL STRUCTURE OF A COMPLEX OF PHOSPHOLIPASE A2( PLA2 ) WITH A NEW GRAMINE DERIVATIVE AT 2.2 Å
RESOLUTION
Sanjit Kumar, Nagendra Singh, Sujata Sharma, Tej.Pal.Singh
Department of Biophysics, All India Institute of Medical Sciences, New Delhi-110029, India

PhospholipaseA2 (PLA2) constitute a family of signal transduction enzymes. PLA2
catalyzes the hydrolysis of fatty acids from the sn-2 position of phospholipd in the first step of
the inflammatory pathway resulting in the production of key inflammatory lipid mediators e.g.
prostanoids, leukotrenes and platelet activating factor. Several PLA2 isoforms are consider as
potential target for this role. Therefore inhibition of PLA2 may reduce the concentration ofproinflammatory compounds. We have obtained a new gramine (DAIP) derivative that binds
to PLA2 with a very high affinity.PLA2 was complexed with DAIP and crystallized .The
crystal belong tetragonal space group P4 with cell dimensions, a = b = 53.0Å ,c = 48.5 ÅThex-ray intensity data were collected using in house facility to 2.2 Å resolution.The structure has
been refined to an R-factor of 0.182(RFree = 0.226) The structure revealed an excellent
electron density for the Ligand.The Ligand is located in the substrate binding site.The OH
group forms hydrogen bonds with a catalytically important water molecules and carboxyl
oxygen of Tyr 22.The aromatic moiety is nicely stacked with Trp31 and fills thehydrophobic channel significantly.

P06-153

CRYSTAL STRUCTURES OF THREE ACTIVE SITE MUTANTS OF
BOVINE PANCREATIC PHOSPHOLIPASE A2
Shankar Prasad Kanaujia and Kanagaraj Sekar
Bioinformatics Centre and Supercomputer Education & Research Centre, Indian Institute of Science,
Bangalore 560 012, India.

Phospholipase A2 hydrolyzes the phospholipids at the sn-2 position to form fatty acidand lysophospholipid products. The enzyme Phospholipase A2 is of high pharmaceuticalconcern since it is responsible for the release of arachidonic acid from membranes and its
subsequent conversion produces leukotrienes and prostaglandins, which are part of theinflammatory response. The catalytic diad (Asp-His) along with a nucleophilic watermolecule forms the active site of the enzyme. It has been known that the two nitrogens of His
48 play an important role in the active site. Biochemical and biophysical studies have shownthat the single mutant H48N results in unstable conformation of the enzyme with almost
negligible activity. The residue, Asp 49, in the calcium binding loop is essential forcontrolling the binding of the calcium ion and the catalytic action of phospholipase A2.
Solution studies reveal that the single mutants D49N and D49K show no binding to thecalcium ion and hence no catalytic activity. To further elucidate the structural role of His 48
and Asp 49 at the active site, the crystal structures of the active site mutants, H48N, D49N
and D49K, have been determined at high resolutions (1.9 Å). Although the catalyticallyimportant calcium ion binds to H48N, the crystal structure reveals the loss of the criticalhydrogen bonding network and provides explanation as observed in proton NMR experiments.
However, the tertiary structures of the three active site mutants are similar to that of wild type.
The details will be presented.

P06-154

CRYSTAL STRUCTURE OF BOVINE C-LOBE WITH RIBOSE AT 2.5 Å
RESOLUTION
G. Vikram, R. Mir, M. Sinha, N.Singh, S. Sharma, P. Kaur and T.P. Singh
Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India

The lactoferrin molecule consists of a single polypeptide chain with a molecular mass ofabout 80 kDa and is folded into two similarly sized homologous N- and C-lobes. Two lobes
are connected by a single bridge peptide segment. The proteolytic studies have shown that Nand C-lobes can be produced by enzymatic digestion. It has also been shown that the C-lobe
is resistant to further enzymatic digestion indicating its role as a functional protein. Studies
have also been reported showing that C-lobe provides relief in certain forms of gastropathy. In
order to understand the medicinal effects of C-lobe, we have been carrying out systemic
structural studies of the complexes of C-lobe with various carbohydrates andanti-inflammatory agents. For this purpose bovine C-lobe has been cocrystallized with ribose
sugar. The crystals belong to monoclinic space group P21 with a = 59.0 Å, b = 49.6 Å,
c = 64.7 Å and β = 105.8˚. The crystal structure has been determined at 2.5 Å resolution andrefined to an R-factor of 20.9% (Rfree=23.4%). The structure revealed two ribose binding sites,
one at Glu659 - Tyr660 and the second at the cleft involving residues Asp378 and Asp462.
Although both sites are shallow in shape but at both sites ribose molecules interact
extensively with protein residues. The interaction include atleast five hydrogen bonds at eachlocation indicating a moderate level of specificity.

P06-155

FRAGMENT-BASED INHIBITION OF PROTEINASE K: CRYSTALSTRUCTURE OF A COMPLEX OF PROTEINASE K WITH BORONICACID AT 0.83 Å RESOLUTION
R. Jain1, N. Singh1, M. Perbandt2, C. Betzel2, S. Sharma1, P. Kaur1, A. Srinivasan1, T.P. Singh1
1-Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India
2- Department of Biochemistry and Molecular Biology, University of Hamburg, Germany

Fragment-based design of tight inhibitors offers good scope of developing new
medicines. More than one compound can be designed to occupy subsites in the ligand binding
space of the target protein. Proteinase K is a fungal protease which has been implicated as a
key enzyme in certain fungal based disorders. In order to understand the mechanism of ligand
binding with Proteinase K, the crystal structure of a complex of Proteinase K with boronic
acid has been determined at 0.83Å resolution. The complex was co- crystallized. The X-ray
intensity data were collected at 100 K using Synchrotron beamline. The unit cell dimensions
were a = b = 67.3Å, c = 106.5Å. The structure has been refined to an R-factor of 12.0% ( Rfree
13.6%). The structure contains 2118 protein atoms and two boronic acid molecules bound at
subsites S1 and S1’. Both molecules are held tightly with atleast five hydrogen bonds between
individual ligands and protein molecule. Residues His69, Gly134, Asn161, Ser221, Thr223
and Ser224 are involved extensively in the interactions with boronic acid. The building ofboronic acid also perturbs the stereochemical arrangement between His69 and Ser224.

P06-156

CRYSTAL STRUCTURE OF BUFFALO LACTOPEROXIDASE AT 2.8Å
RESOLUTION
Ishfaq Ahmed Sheikh, Nagendra Singh, Sujata Sharma, Asha bhushan and T.P. Singh
Department of Biophysics, All India Institute of Medical Sciences, New Delhi-110029, India

Mammalian peroxidases include lactoperoxidases (LPO), myeloperoxidase (MPO),
eosinophil peroxidase (EPO), and thyroid peroxidase (TPO) utilize H2O2 to catalyze a diverse
set of reactions. LPO is found in milk and other biological fluids like tears, saliva etc. and is acomponent of an antimicrobial defense system that catalyzes the bielectronic oxidation of
thiocynate to hypothiocynate. It is a glycoprotein characterized by a single polypeptide chainof 78KDa whose carbohydrate content is of the order of 10%. LPO has been isolated frombuffalo milk (BLPO) and crystallized using PEG 3350.The crystals belong to monoclinic
space group P2, with cell dimensions, a =54.5Å, b =80.8Å, c =77.6Å, ß = 102.9º. The
structure has been determined by molecular replacement method and refined to an R value of0.186 (R free =0.217). The structure reveals that heme is covalently attached to the protein via
two ester linkages between the carboxyl groups of Glu 258 and Asp109 and modified methylgroups on pyrrol rings A and C of the heme. The structure has a calcium binding site with atypical pentagonal bipyramidal coordination geometry. The linkages to proximal and distal
sites reveal several novel features.

P06-157

CRYSTAL STRUCTURE OF MAMMARY SECRETORY
GLYCOPROTEIN FROM BUFFALO AND ITS COMPLEXES WITH
OLIGO-SACCHARIDES
Punit Kaur, A.K. Singh, Rishi Jain, N. Singh, S. Sharma and T.P. Singh
Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India

Mammary involution in buffalo is characterized by a rapid loss of tissue function anddegeneration of the alveolar structure and massive loss of epithelial cells. This cell loss is due
to programmed cell death or apoptosis. During this period of large scale tissue destruction, a
40 kDa glycoprotein is secreted in significantly high concentrations which is implicated to bebinding to viable cells and protects them from the process of programmed cell death. The
protein has been isolated from buffalo dry secretions and crystallized. It has also beencocrystallized with tetrasaccharide. The crystals belong to orthorhombic space group P212121
with cell dimensions a = 62.8 Å, b = 66.5 Å, c = 107.1 Å. The structure determination reveals
that the tetrasaccharide residues occupy subsites S2 - S5. The conformation of Trp 78 isunperturbed because S1 subsite is not occupied. The shape of sugar-binding groove isconsiderably distorted particularly beyond S2 subsite. The flexible domain which is assumed
to be involved in the intermolecular recognition through protein-protein interactions isunaffected by carbohydrate binding. Protein has an N-linked glycan chain which is integrated
well with protein structure near the covalent linkage but extends into space indicating its
participation as a glycan chain - protein interactions. All the binding components are
independently involved in the recognition making this protein as a binding protein with highaffinity.

P06-158

X-RAY CRYSTAL STRUCTURE ANALYSIS OF
ERK1/IODOTUBERCIDIN COMPLEX
Ikuyo Yoshida,a Takayoshi Kinoshita,a Masaki Gouda,b Mamoru Matsubara,b Hiroshi
Ishiguro,b Toshiji TadaaaDepartment of Biological Science, Graduate School of Science, Osaka Prefecture University, Osaka,

Japan; bCARNA BIOSCIENCES, INC., Hyogo, JapanERK is a member of MAP kinase family that contributes to the coordination andregulation of cell growth and differentiation in response to extracellular stimulation. ERK
consists of two isoforms, ERK1 and ERK2, which have a high degree of amino acid sequencehomology. ERK1 and ERK2 are different from each other in the intravital behavior. Micelacking ERK1 are viable and fertile, but have a deficient thymocyte maturation, while micelacking ERK2 die during embryogenesis due to a defect in trophoblast development.
In order to clarify the difference in the in vivo function between ERK1 and ERK2, wedetermined the crystal structure of human ERK1/Iodotubercidin complex. Crystals of thecomplex were obtained at 277 K using a reservoir solution of 1.6 M - 1.8 M ammonium
sulfate, 100 mM MES buffer, pH 6.5, and 3% - 5% PEG 400. Diffraction data were collected
to 3.2 Å resolution at beamline BL6A, Photon Factory, Tsukuba. The crystal belongs to thespace group P21, with unit-cell parameters, a = 62.11 Å, b = 90.91 Å, c = 63.41 Å, β = 91.58°
and Z = 4. ERK1 structure was solved by molecular replacement method. The structuralrefinement and model modification are currently in progress. A detailed comparison of thestructure of ERK1 with that of ERK2 will be reported.

P06-159

CRYSTAL STRUCTURE OF HUMAN LYN KINASE DOMAIN
Nao Miyano,a Takayoshi Kinoshita,a Koichi Yokota,b Hiroshi Ishigurob and Toshiji TadaaaDepartment of Biological Science, Graduate School of Science, Osaka Prefecture University, Osaka,

Japan; bCarna Biosciences, Hyogo, Japan

Lyn tyrosine kinase is a member of Src family kinases and plays a critical role in thesignal transduction of immune system. Its excess activity is involved in cancer andinflammatory diseases. The crystal structure of Lyn kinase domain would help to design novel
inhibitors of Lyn.
Human Lyn kinase domain (233 - 513) fused to His-tag at C-terminal was expressed in
Sf9 insect cells and purified using a Ni-column, His trap HP, and an anion exchange column,
MonoQ (GE Healthcare). A crystal of Lyn was obtained with the sitting drop vapor diffusion
technique at 4ºC with a reservoir buffer containing 0.2 M proline, 10% (w/v) PEG 3350 and
0.1 M HEPES (pH 7.5). Diffraction data were collected at 3.2 Å resolution using synchrotron
radiation at Photon Factory beamline BL-17A. The data were processed and scaled using the
program HKL2000. The crystal belongs to rhombohedral space group R3, with unit-cellparameters a = b = 129.6 Å, c = 58.6 Å, α = β = 90°, γ = 120°. The crystal structure wassolved by the molecular replacement method using a Lyn homology model derived fromhuman Fyn kinase domain. Further, structural refinement and model modification are
currently in progress.

P06-160

PROTEOMIC ANALYSIS OF MANGANESE REGULATION OFNEISSERIA GONORRHOEAE
Hsing-Ju Wu1, Kuan-Tin Pan1, He-Hsuan Hsiao1, Chen-Wen Yao3, Alastair G. McEwan2,
Michael P. Jennings2 and Andrew H-J. Wang1
1

Core Facilities for Proteomics Research, Institute of Biological Chemistry, Academia Sinica, Taipei,

Taiwan; 2 School of Molecular and Microbial Sciences & Centre for Metals in Biology, The University of
Queensland, Brisbane, Australia; 3 Chinese Herbal Medicine Research Center, Tri-Service General
Hospital, Taipei, Taiwan

Neisseria gonorrhoeae is an important human pathogen which causes gonorrhoea andpelvic inflammatory disease. It is a facultative aerobe with a high iron requirement and ahighly active aerobic respiratory chain. These factors would suggest that this bacterium would
require defense systems to respond to toxic oxygen species. In the previous studies, we haveshown that the accumulation of manganese (Mn) and Mn(II) uptake system, MntABC, in N.
gonorrhoeae protected against killing by superoxide anion, and was independent ofsuperoxide dismutase activity. Also, investigation of a regulatory role for Mn(II) in
N. gonorrhoeae has revealed that a key virulence factor, pili, is repressed by Mn via a
PerR-independent post-transcriptional mechanism. To provide a more comprehensive view of
the regulatory network and its molecular mechanism, the shotgun proteomic approach, i.e.
one dimensional (1D) sodium dodecyl sulfate-polyacrylamide gel electrophoresis(1D-SDS-PAGE) coupled with 1D liquid chromatography (LC) - tandem mass spectrometry(MS/MS) and the quantitative method, i.e., isotope coded affinity tag (ICAT) were performed.
N. gonorrhoeae cells were grown in the presence and absence of Mn and cell lysates
were fractionated into cytoplasmic, inner membrane and outer membrane components. These
results revealed that 98 proteins were differentially regulated at the post transcriptional level
under conditions of increased or decreased Mn. The Mn-regulated proteins have a broad rangeof functions including oxidative stress defence (i.e. superoxide dismutase (SodB), azurin,
bacterioferritin), cellular metabolism, protein synthesis, RNA processing, cell division, pilin
and the proteins involved in the pilus assembly, such as PilC1 and PilQ. This confirms ourprevious study and may explain how the expression of pili was downregulated when cells
were grown in the Mn supplement. Taken together, these data give us a proteomic view of Mn
regulation and provided us with leads to correlate protection against oxidative stress withpilus formation and surface protein expression.

P06-161

MOLECULAR BASIS FOR RECOGNITION OF A SELECTIVE
NUCLEOSIDE INHIBITOR BY PLASMODIUM FALCIPARUM
S-ADENOSYL-L-HOMOCYSTEINE HYDROLASE
Yoshio Kusakabe,a Nobutada Tanaka,a Ken-ichi Aoki,a Masayuki Nakanishi,b,e Yukio
Kitade,b,c,d and Kazuo T. NakamuraaaSchool of Pharmaceutical Sciences, Showa University, Tokyo 142-8555, Japan; bDepartment of

Biomolecular Science, Faculty of Engineering, Gifu University, Gifu 501-1193, Japan; Centers forc

Infectious Diseases and dAdvanced Drug Research, Gifu University, Gifu 501-1193, Japan; Collegeof Pharmaceutical Sciences, Matsuyama University, Ehime 790-8578, JapanThe human malaria parasite Plasmodium falciparum is responsible for the death of
more than a million people each year. The emergence of strains of malarial parasite resistant
to conventional drug therapy has stimulated searches for antimalarials with novel modes ofaction.
S-Adenosyl-L-homocysteine hydrolase (SAHH) is a regulator of biological methylations.
In 2004, we reported the crystal structure of Plasmodium falciparum SAHH (PfSAHH)
complexed with a reaction product adenosine [Tanaka et al., J. Mol. Biol., 2004]. A structuralcomparison of PfSAHH with human SAHH (HsSAHH) revealed that a single substitution
between the PfSAHH (Cys59) and HsSAHH (Thr60) accounts for the differential interactions
with nucleoside inhibitors. Chemical studies suggested that introduction of a fluorine atom atthe 2-position of an adenine nucleoside derivative improve the selectivity index between
HsSAHH and PfSAHH inhibition. To obtain an insight into molecular basis for selective
inhibition of SAHHs by the inhibitors, structural analyses of PfSAHH complexed with theselective inhibitors are essential.
Here we report the crystal structure of PfSAHH complexed with a selective inhibitor,
2-fluoronoraristeromycin (2-F-NAM).

P06-162

CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSISS-ADENOSYL-L-HOMOCYSTEINE HYDROLASE
Nobutada Tanaka,a Yoshio Kusakabe,a Masayuki Nakanishi,b,f Koichi Maruyama,b Takayuki
Ezaki,e Yukio Kitade,b,c,d and Kazuo T. NakamuraaaSchool of Pharmaceutical Sciences, Showa University, Tokyo 142-8555, Japan; bDepartment of

Biomolecular Science, Faculty of Engineering, Gifu University, Gifu 501-1193, Japan; Centers forc

Infectious Diseases and dAdvanced Drug Research, Gifu University, Gifu 501-1193, Japan;eDepartment of Microbiology, Gifu University School of Medicine, Gifu-501-1193, Japan; fCollege of

Pharmaceutical Sciences, Matsuyama University, Ehime 790-8578, Japan

Mycobacterium tuberculosis is a main pathogen causing tuberculosis (TB). It currently
infects one-third of the world's population, resulting in 2 million deaths annually. The
increased prevalence of drug-resistant and multi-drug-resistant strains, together with the lethal
combination that tuberculosis and AIDS represents, makes the need for new and better drugs
urgent. Given the multiple problems in fighting TB, effective control of the disease requires
the identification of new drug targets and discovery of novel drugs.
S-Adenosyl-L-methionine (SAM) is the most widely used methyl donor. Numerous
methyl transferases transfer the methyl group from SAM to their respective biologic acceptors,
forming
S-adenosyl-L-homocysteine(SAH).
SAH
ishydrolysedbyS-adenosyl-L-homocysteine hydrolase (SAHH, EC 3.3.1.1) to adenosine (Ado) andL-homocysteine (Hcy). Inhibition of SAHH results in a cellular accumulation of SAH, which
is a potent feedback inhibitor of SAM-dependent biological methylation. Thus, SAHH
inhibitors can be potent inhibitors against various pathogenic organisms.
To design selective inhibitors for Mycobacterium tuberculosis SAHH (MtSAHH), we
initiated structural analysis of recombinant MtSAHH. Medium-resolution crystal structure
analyses of human, rat, and Plasmodium falciparum SAHHs have been reported, however,high-resolution crystal structure analysis of SAHH has not been reported yet. Here we report
the crystal structure of MtSAHH complexed with the reaction product Ado at 1.75 Å
resolution. This is the first high-resolution crystal structure analysis of SAHH.

P06-163

ELUCIDATION OF A CATALYTIC-CRITICAL HYDROGEN BOND
NETWORK IN THE ACTIVE SITE OF ANIMAL GLUTAMINYLCYCLASES SUGGESTS AN ESSENTIAL PROTON TRANSFER
PROCESS DURING CATALYSIS
Kai-Fa Huang‡§, Yu-Ruei Wang¶, En-Cheng Chang‡, Tsung-Lin Chou†, and Andrew H.-J.
Wang‡§†‡

Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan§

National Core Facility of High-Throughput Protein Crystallography, Academia Sinica, Taipei 115,

Taiwan¶Department of Biochemical Science and Technology, College of Life Science, National Taiwan

University, Taipei 106, Taiwan†

Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan

Glutaminyl cyclases (QCs) catalyze the N-terminal pyroglutamate (pGlu) formation ofnumerous bioactive peptides. The enzymes were reported to relate to several pathologicalprocesses, such as amyloidotic diseases, osteoporosis, rheumatoid arthritis, and melanoma.
The crystal structure of human QC revealed an unusual hydrogen bond network in the active
site, formed by several highly conserved residues (Ser160, Glu201, Asp248, Asp305, and His319),
within which Glu201 and Asp248 were found to bind to substrate. In this study, we combine
steady-state enzyme kinetic and X-ray structural analyses of eleven single-mutation human
QCs to investigate the roles of the hydrogen bond network on catalysis. Our results
demonstrated that disrupting one or both of the central hydrogen bonds, i.e., Glu201•••Asp305
and Asp248•••Asp305, reduced the steady-state catalysis dramatically. The roles of these two
COOH•••COOH bonds on catalysis could not be replaced by COOH•••CONH2 bonds, but
could be slightly replaced by COOH•••HOH bonds. Mutations on Asp305, a residue locating at
center of the hydrogen bond network, raised the Km value of the enzyme 3.6-17.5-fold and,surprisingly, decreased the kcat value 89-3267-fold, indicating that Asp305 primarily plays acatalytic role. In addition, results from mutational studies on Ser160 and His319 suggest thatthey might help to stabilize the conformations of Asp248 and Asp305, respectively. These data
allow us to propose an essential proton transfer process during catalysis of animal QCs.

P06-164

STRUCTURAL COMPARISON STUDIES FOR 2H
PHOSPHOESTERASE SUPERFAMILY PROTEINS
Yasumitsu Sakamoto,a,b Nobutada Tanaka,a Tomomi Ichimiya,c Tadashi Kurihara,c andKazuo T. NakamuraaaSchool of Pharmaceutical Sciences, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo

142-8555, Japan,bSchool of Nursing and Rehabilitation Sciences, Showa University, 1865

Tokaichiba-cho, Midori-ku, Yokohama, 226-8555 Japan, cDepartment of Bioinformatics, Faculty ofEngineering, Soka University, 1-236 Tangi-cho, Hachioji-shi, Tokyo 192-8577, Japan

Recently, the structures of several 2H phosphodiesterase super family proteins havebeen determined by X-ray crystallography and NMR spectroscopy. Here we report thestructure-function relationship studies of two hydrophobic residues in cyclic-nucleotide
phosphodiesterase (CNP) family proteins.
The structures of CNP family proteins are highly similar to each other in the active site
region. Our previous crystallographic study of human CNP (hCNP-CF) implies that Phe236
and Val322 are involved in non base-specific substrate recognition. Among the sevenvertebrate CNPs, Val322 is completely conserved in seven cases (human, bovine, rat, mouse,chicken, frog, and goldfish). Structural superpositions using recently published NMR
structures (rat CNP-CF (rCNP-CF): PDB code 1ILX; goldfish RICH protein (gRICH): PDB
code 2I3E) and the crystal structure of hCNP-CF (PDB code 1WOJ) indicate that Phe236 andVal322 in hCNP-CF are structurally equivalent to Phe235 and Val321, and Phe239 andVal332, respectively, in rCNP-CF and in gRICH. These results support our previous study
and imply functional significance of these residues.

P06-165

CRYSTAL STRUCTURE OF PARASPORIN-2, AN ANTI-TUMORTOXIN FROM BACILLUS THURINGIENSIS
Toshihiko Akiba,a Yuichi Abe,b Sakae Kitada,b Yoshitomo Kusaka,b Akio Ito,b Tokio
Ichimatsu,c Hideki Katayama,c Tetsuyuki Akao,c Kazuhiko Higuchi,c Eiichi Mizuki,c Michio
Ohba,d Ryuta Kanai a and Kazuaki Harata aaBiol. Info. Res. Center, AIST, Tsukuba; bDept. Chem., Kyushu Univ., Fukuoka; cBiotech. Food Res.

Inst., Fukuoka Ind. Tech. Center, ; dDept. Appl. Gen. Pest Manage., Kyushu Univ., Fukuoka, Japan

Parasporin-2 is a protein toxin isolated from parasporal inclusions of a Gram-positivebacterium, Bacillus thuringiensis, strain A1547. While the bacterium is generally known as
a valuable source of protein toxins that are harmless to mammals but specifically effective
against insect pests, parasporin-2 does not have insecticidal activity but has a strong cytocidal
activity against various human cells with markedly divergent target specificity, preferentiallyeffective to liver and colon cancer cells. The 37-kDa inactive nascent protein is proteolyticallyconverted to the 30-kDa active form, which causes susceptible cells rapid ballooning andsubsequent burst to death. To elucidate the basis for toxicity and specificity, the crystal
structure of the recombinant active-form has been determined at 2.65 Å by the MAD method.
The protein has an unusually elongated structure dominated by b-strands, many ofwhich are remarkably long, running all or two-thirds of the longer axis of the molecule. The
molecule can be divided to three domains: the N-terminal domain 1 is composed of a small
four-stranded b-sheet surrounded by three short a-helices; domains 2 and 3 are bothb-sandwiches. The overall structure of the protein resembles those of epsilon-toxin from
Clostridium perfringens and domains 2-4 of aerolysin from Aeromonas hydrophila. Since
these toxins belong to the b-pore-forming toxin, parasporin-2 would also develop toxicity by
perforation of target cell membrane through formation of a large multimeric b-sheet-walled
channel. This assumption agrees with reported changes in susceptible cells treated with theprotein. Comparison of each domain with counterparts of those structural homologues
highlights remarkable structural conservation in domains 2 and 3, suggesting they may be
responsible for pore formation. Particularly interesting is an elongated patch of hydroxylatedamino acid residues on the surface of these domains; a non-toxic structural homologue, the
26-kDa crystal protein from B. thuringiensis, strain A1470, lacks this feature. On the other
hand, there is noticeable structural divergence between the domain 1 parts of the homologues,
suggesting its involvement in target specificity. There is an extensive cluster of aromatic
residues in domain 1 of parasporin-2, which could be suitable for binding to sugar moieties ofglycoproteins or glycolipids on the cell surface.

P06-166

CRYSTAL STRUCTURE OF THE HRDC DOMAIN OF HUMANWERNER SYNDROME PROTEIN, WRN.
Ken Kitano, Nozomi Yoshihara and Toshio Hakoshima
Structural Biology Laboratory, Nara Institute of Science and Technology (NAIST), Ikoma, Japan.

Werner syndrome is a human premature aging disorder characterized by chromosomal
instability. The disease is caused by the functional loss of WRN, a member of the
RecQ-helicase family that plays an important role in DNA metabolic pathways. WRN
contains four structurally folded domains comprising an exonuclease, a helicase, awinged-helix, and a helicase-and-ribonuclease D/C-terminal (HRDC) domain. In contrast to
the accumulated knowledge pertaining to the biochemical functions of the three N-terminal
domains, the function of C-terminal HRDC remains unknown.
Recently we determined the crystal structure of the human WRN HRDC domain(Kitano et al., 2007, J. Biol. Chem.). The domain forms a bundle of α-helices similar to thoseof Saccharomyces cerevisiae Sgs1 and Escherichia coli RecQ. Surprisingly, the extra ten
residues at each of the N and C termini of the domain were found to participate in the domainarchitecture by forming an extended portion of the first helix α1, and a novel looping motifthat traverses straight along the domain surface, respectively. The motifs combine to increase
the domain surface of WRN HRDC, which is larger than that of Sgs1 and E. coli. In WRN
HRDC, neither of the proposed DNA-binding surfaces in Sgs1 or E. coli is conserved, and thedomain was shown to lack DNA-binding ability in vitro. Moreover, the domain was shown tobe thermostable and resistant to protease digestion, implying independent domain evolution in
WRN. Coupled with the unique long linker region in WRN, the WRN HRDC may be adapted
to play a distinct function in WRN that involves protein-protein interactions.

P06-167

CRYSTAL STRUCTURE OF FUSOBACTERIUM ADHESIN A (FADA):IMPLICATIONS FOR ORAL DISEASES AND PRETERM BIRTH
Stanley Nithianantham,a Minghua Xu,b Mitsunori Yamada,b Hongqi Liu,b Jonathan Ross,bMark Durham,b Hameem Kawsar,b Menachem Shohama* and Yiping W. Hanb,caDepartments of Biochemistry, bPeriodontics and cPathology, Case Western Reserve University,

Cleveland, Ohio 44106, U.S.A.

Epidemiological and microbiological-immunological studies have lent credence to theconcept that periodontal disease is a risk factor for cardiovascular, cerebrovascular andrespiratory diseases in addition to preterm delivery of low-birth-weight infants.
Fusobacterium nucleatum is one of the predominant anaerobes associated with periodontal
disease and preterm birth. It originates in the oral cavity and it is transmitted to the uterus via
the blood stream. A 13.7 kDa FadA (Fusobacterium adhesin A) protein is required for thebacterium to attach to host mammalian cells. FadA has been expressed in Escherichia coli,
purified and crystallized. The crystals belong to the hexagonal space group P61, with
unit-cell parameters a = b = 59.3, c = 125.7 Å. Synchrotron X-ray data have been collected
to 1.9 Å. We have solved the structure by MAD (Multiple Anomalous Dispersion) method.
The analysis of FadA reveals two antiparallel coiled coil α-helices connected by aneight-residue hairpin loop. The two helices interact with each other via leucine residues.
The N-terminal helix has four additional exposed leucines that interact with leucines of aneighboring molecule. This novel oligomerization motif is the leucine chain. The structureand function of FadA will be discussed in detail.
References:[1]Nithianantham, S., Xu, M., Wu, N., Han, Y. W., and Shoham, M. (2006). Crystallization and preliminary
X-ray data of the FadA adhesion from Fusobacterium nucleatum. Acta Crystallograph Sec F 62, 1215-1217.
[2]Xu, M., Yamada, M., Li, M., Liu, H., Chen, S. G., and Han, Y. W. (2007). FadA from Fusobacterium
nucleatum utilizes both secreted and non-secreted forms for functional oligomerization for attachment andinvasion of host cells. J Biol Chem (in press).

P06-168

STRUCTURE-BASED DESIGN OF INHIBITORS OF HUMAN MTH1
PROTEIN I
Teruya Nakamura,a Miyuki Inazato,a Sinji Ikemizu,a Yusaku Nakabeppu,b and Yuriko
YamagataaaGraduate School of Pharmaceuical Sciences, Kumamoto University, Kumamoto 862-0973, Japan;bMedical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.

Human MutT homolog-1 (hMTH1) hydrolyzes a variety of oxidized purine nucleoside
triphosphates including 8-oxo-dGTP, 2-oxo-dATP, 2-oxo-ATP, and 8-oxo-dATP to theircorresponding nucleoside monophosphates, while E. coli MutT possesses prominent substratespecificity for 8-oxoguanine nucleotides. Up to date, we have determined the crystal
structures of hMTH1 complexed with three oxidized nucleotides, 8-oxo-dGMP, 8-oxo-dGTP,
and 2-oxo-dATP. Their structures indicate that hMTH1 exhibits the broad substrate specificity
for oxidized purine nucleoside triphosphates with a very novel manner.
hMTH1 suppresses the cell death occurred by oxidative stress. The expression of thehMTH1 protein increases in human cancerous tissues including brain tumors, kidney and lungcancers with an increased accumulation of 8-oxoguanine. This indicates that compounds
which suppress the hMTH1 function or expression must be new candidates for chemotherapyof cancer to sensitize cancer cells against certain type of anticancer drugs. Thus we are trying
to seek inhibitors of hMTH1 based on the characteristic active site structure of hMTH1. In
this presentation, we will discuss the examination using the program MOE.

P06-192

CRYSTAL STRUCTURES OF D-AMINO ACID AMIDASE FROMOCHROBACTRUM ANTHROPI SV3 AND α-AMINO-ε-CAPROLACTAMRACEMASE FROM ACHROMOBACTER OBAE
Seiji Okazakia, Atsuo Suzukia, Tsunehiro Mizushimaa, Hidenobu Komedab, Yasuhisa Asanob,
Takashi YamaneaaDepartment of Biotechnology, School of Engineering, Nagoya University, Chikusa, Nagoya,464-8603, Japan, bBiotechnology Research Center, Toyama Prefectural University, Imizu, Toyama,939-0398, Japan.

D-amino acid amidase (DAA) from Ochrobactrum anthropi SV3 catalyzes thestereospecific hydrolysis of D-amino acid amides to yield the D-amino acid and ammonia.
And, α-amino-ε-caprolactam racemase (ACL racemase) from Achromobacter obae catalyzes
racemization of D,L-ACL. Recently, racemase activity on amino acid amide was discoveredin ACL racemase. By combinating of ACL racemase and D-stereospecific hydrolase like
DAA, the production of D-amino acid in 100% theoretical yield can be possible. In ordered toclarify the structute-function relationships of DAA, the crystal structures of native DAA,
D-phenylalanine complex, L-phenylalanine complex and L-phenylalanine amide complex
were determined at 2.1, 2.4, 2.3 and 2.2 Å, respectively. Also to clarify the structute-function
relationships of ACL racemase, the crystal structure of native ACL racemase was determinedat 2.5 Å resolution. The structure of ACL racemase is composed of three segment; (1) an
N-terminal segment (residues 1 to 43); (2) a large, pyridoxal phosphate (PLP) binding domain(residues 44 to 319); and (3) a C-terminal domain (residues 320 to 436). The overall structureof ACL racemase is similar to those of the other aminotransferase subgroup Ⅱenzymes,
especially γ-aminobutyrate aminotransferase (GABA-AT) from E. coli, and dialkylglycine
decarboxylase (DGD) from Pseudomonas cepacia. Like GABA-AT and DGD, two monomers
of ACL racemase make extensive contacts to form a dimer. Interestingly, differed from
GABA-AT and DGD, ACL racemase having unique elongated C-terminus polypeptide chain(Ser423 - Trp436), and the C-terminus residue Trp436 elongated to active site. The C4' in PLP
covalently bonded to the ε-amino group of Lys267 forming the internal aldimine.

P06-193

XC5848, AN ORFan PROTEIN FROM XANTHOMONAS CAMPESTRIS,ADOPTS A NOVEL VARIANT OF Sm-LIKE MOTIF
Ko-Hsin China, Andrew H.-J. Wangb, & Shan-Ho Choua,c,*aNational Chung Hsing University Biotechnology Center, National Chung-Hsing University, Taichung,40227, Taiwan, bInstitute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan, ROC,c

Institute of Biochemistry, National Chung-Hsing University, Taichung, 40227, Taiwan, ROC

The XC5848 gene from a plant pathogen Xanthomonas campestris pv. campestris str.
17 (Xcc) encodes a hypothetical protein comprising 102 amino acid residues, with amolecular weight of 11945 Da. A BLAST search using XC5848 sequence against the
UniProtKB/TrEMBL database (http://us.expasy.org/sprot/) finds orthologs only in the
Xanthomonas genus. No close sequence homologue could be detected for other organisms.
We have determined the XC5858 crystal structure to 1.68 Å resolution, and found that
XC5848 adopts a well-conserved Sm or Lsm (Sm-like) fold widely found in eukarya, arachea,
and bacteria, despite the very low sequence identities. However, considerable differences with
the Sm-like motif were observed at the N-terminal and internal regions. Since critical residues
responsible for RNA recognition and oligomer formation of Sm-like proteins are generally
absent, XC5848 could play biological roles other than RNA metabolism. To the best of ourknowledge, this is the first structural report of the novel variant of the highly conserved
Sm-like motif.

P06-194

THE CRYSTAL STRUCTURE OF XC1258 FROM XANTHOMONAS
CAMPESTRIS: A PUTATIVE PROCARYOTIC NIT PROTEIN WITH
AN ARSENIC ADDUCT IN THE ACTIVE SITE
Ko-Hsin China, Andrew H.-J. Wangb, & Shan-Ho Choua,,b*aNational Chung Hsing University Biotechnology Center, National Chung-Hsing University, Taichung,40227, Taiwan, bInstitute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan, ROC,c

Institute of Biochemistry, National Chung-Hsing University, Taichung, 40227, Taiwan, ROC

The nitrilase superfamily proteins are involved in a wide variety of non-peptide
carbon-nitrogen hydrolysis reactions, characterized by a thiol acylenzyme intermediate
formed through the attack of a cyano or carbonyl carbon by a novel conserved catalytic triadof Glu-Lys-Cys, to produce important natural products such as auxin, biotin, precursors ofantibiotics etc. Based on extensive sequence analysis, members of the nitrilase superfamily
were classified into 6 or 13 functionally district groups. However, although sequence
searching can identify polypeptides as members of the nitrilase superfamily, their annotations
have been perplexing. It is necessary to re-classify these protein members preferably by
structure-based methods. Currently only a few protein structures are available in thissuperfamily, including a NitFhit protein from Caenorhabditis elegans, two
N-carbamyl-D-amino acid amidohydrolases (DCases) from Agrobacterium sp. Strain
KNK712 and Agrobacterium radiobacter, and a putative CN hydrolase from Sacchromyces
cerevisiae strain S288C. They are either dimeric or tetrameric α−β−β−α sandwich proteins.
We now report the crystal structure of XC1258, a putative nitrilase superfamily proteinfrom the plant pathogen Xanthomonas campestris pv. campestris str. 17 (Xcc). Based on amultiple sequence alignment, XC1258 was found to exhibit only low sequence identities withother nitrilase superfamily proteins for which the tertiary structures have been determined. We
have determined the crystal structure of XC1258 to a resolution of 1.73 Å using thetwo-wavelength MAD approach. Interestingly, a cacodylate or dimethylarsinic acidcompound was found to situate perfectly in the active region, forming a strong arsenic adductwith the active cysteine residue. This observation allows us to propose a reaction mechanism
for the nitrilase superfamily proteins and suggests that their activity could be inhibited by thedimethylarsinic compound through a sulfur-arsinic covalent bond.

P06-195

KINETIC AND STRUCTURAL PROPERTIES OF TRIOSEPHOSPHATEISOMERASE FROM HELICOBACTER PYLORIChen-Hsi Chu, Yi-Ju Lai, and Yuh-Ju Sun*
Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 30013,
Taiwan, ROC

Triosephosphate isomerase (TIM) catalyzes the interconversion between
dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (GAP) in theglycolysis-gluconeogenesis metabolism pathway. The Helicobacter pylori TIM gene
(HpTIM) was cloned, and HpTIM was expressed and purified. The enzymatic activity of
HpTIM for the substrate GAP was determined (Km = 3.46 ± 0.23 mM and kcat = 8.8 × 104
min-1). The crystal structure of HpTIM was determined by molecular replacement at 2.3 Å
resolution. The overall structure of HpTIM was (β/α)β(β/α)6, which resembles the common
TIM barrel fold, (β/α)8; however, a helix is missing after the second β-strand. The
conformation of loop 6 and binding of phosphate ion suggest that the determined structure of
HpTIM was in the “closed” state. A highly conserved Arg-Asp salt bridge in the“DX(D/N)G” motif of most TIMs is absent in HpTIM because the sequence of this motif is“211SVDG214”. To determine the significance of this salt bridge to HpTIM, four mutants,
including K183S, K183A, D213Q, and D213A, were constructed and characterized. The
results suggest that this conserved salt bridge is not essential for the enzymatic activity of
HpTIM; however it might contribute to the conformational stability of HpTIM.

P06-196

CARBOHYDRATE-BINDING OF THE STARCH BINDING DOMAIN
OF RHIZOPUS ORYZAE GLUCOAMYLASE IN COMPLEX WITH
β-CYCLODEXTRIN AND MALTOHEPTAOSE
Jung-Yu Tung , Yen-Yi Liu, Wei-I Chou, Fang-Yu Chang, Dah-Tsyr Chang and Yuh-Ju Sun
Department of Life Science, National Tsing Hua University, Hsinchu

Glucoamylase hydrolyses starch and polysaccharides to β-D-glucose. Rhizopus oryzae
glucoamylase (RoGA) consists of two functional domains, an N-terminal starch binding
domain (SBD) and a C-terminal catalytic domain. The two domains are connected by an
O-glycosylated linker. The crystal structures of the SBD in complex with a cycliccarbohydrate, β-cyclodextrin (β-CD), and a linear carbohydrate, maltoheptaose (G7), were
determined. The overall structures of the SBD complexes belong to a β-sandwich fold with
an immunoglobulin-like structure and two carbohydrate-binding sites were observed. Site I
is created by several conserved aromatic residues, Trp47, Tyr83, and Tyr94, to form a broad,flat, and firm hydrophobic surface. In addition to the hydrophobic interaction, numerous
asparagine residues are involved in the hydrophilic interactions to carbohydrate. Site II isbuilt up by Tyr32 and Phe58 to produce a protruded and narrow binding environment. Site I
undergoes a bigger conformational change than site II upon the carbohydrate binding.

P06-197

ATP-DRIVEN MOTIONS OF 70-KDA HEAT SHOCK PROTEINS(HSP70S): INSIGHTS INTO STRUCTURAL DYNAMICS OF THE
HSP70 POWER STROKE
Yi-Wei Chang,a,b Chung Wang,a and Chwan-Deng HsiaoaaInstitute of Molecular Biology, Academia Sinica, Taipei, 11529, Taiwan; bInstitute of Bioinformatics

and Structural Biology, National Tsing Hua University, Hsinchu, 300, Taiwan

The 70-kDa heat shock proteins (Hsp70s) are interspecific highly conserved molecularchaperones which participate in many crucial cellular functions, such as promoting the correct
folding of nascent or stress-denatured polypeptides, assisting the protein translocation acrossmembranes, and helping the assembly/disassembly of protein complexes.. Under particular
control by the J-domain ATPase activating proteins and nucleotide exchange factors (NEFs),
Hsp70s process their substrates in ATP-driven cycles. Previous studies clearly defined thatHsp70 protein can be distributed into two major functional domains, the NH2-terminal
nucleotide-binding domain (NBD) and the COOH-terminal substrate-binding domain (SBD).
To date, the ATP dependent allosterically regulating mechanism between these two domains
has been long explored. However, precise structural understanding of the interdomain
communication during ATPase cycle is still limited. In this report, we have determined the
X-ray structures of ATP form intact Hsp70 chaperone proteins in various species, including
the DnaK in eubacterium Geobacillus kaustophilus HTA426 and the 70-kDa heat shock
cognate protein (Hsc70) in mammalian Rattus norvegicus. Together with the result ofdetecting the solvent accessibility of a Trp reporter on the domain-domain interface, thestructures reveal typical domain releasing behaviors of Hsp70s upon ATP binding andhydrolysis. This is in good agreement with previous studies that the hydrolysis of ATP may
drives large domain movement of SBD related to NBD and provides power to allow Hsp70s
serving as motors in processes such as protein translocation trough transport channels.
Furthermore, the insertion of the hydrophobic linker region of gkDnaK into anothercrystallographic symmetry molecule’s substrate binding pocket suggests a characteristic
cooperative mechanism of Hsp70s. These important findings demonstrate exciting insights
into structural dynamics of Hsp70 family proteins during chaperone cycles.

P06-198

CRYSTAL STRUCTURE OF PHOSPHORIBOSYLPYROPHOSPHATE
BOUND NICOTINATE PHOSPHORIBOSYLTRANSFERASE FROMPYROCOCCUS FURIOSUS
KyuBeen Sohn1, Yilan Fang1, Andrea Schulte2, Christiane Dahl2, Sung-Hou Kim3 and Dong
Hae Shin1*
1College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea, 2Institut für Mikrobiologie &Biotechnologie, Universität Bonn, Meckenheimer Allee 168, D-53115 Bonn, Germany, 3Department ofChemistry, University of California, Berkeley, California 94720-5230, USA,*

Corresponding author

The dsrEFH genes are part of the dsr (dissimilatory sulfite reductase) operon of the
anoxygenic phototrophic sulfur bacterium Allochromatium vinosum. The dsr gene products
are essential for the oxidation of sulfur stored in intracellular sulfur globules in this organism.
The polypeptides DsrE, DsrF and DsrH are homologous to each other. From A. vinosum they
are isolated as a soluble a2b2g2-structured holoprotein with an apparent molecular mass of 75
kDa [1]. DsrE and DsrF are the prototypes of a family of conserved proteins domains (COG
1553, 2044, 2923). DsrH is the prototype of yet another family of conserved proteins found inbacteria and archaea (COG 2168) but also fits into the DsrE/F family. In our effort to dissect
functions of the proteins encoded at the A. vinosum dsr locus we have determined the three
dimensional structure of DsrEFH by X-ray crystallography at 2.5 Å resolution to a
crystallographic R-factor of 20.5 % and free R-factor of 26.2%.

P06-199

STABILIZATION OF COLLAGEN TRIPLE-HELIX BY ARG IN THE Y
POSITION
Tatsuya Morimoto,a Mitsuru Haga,b Chizuru Hongo,a Keiichi Noguchi,c Kenji Okuyamaa andToshiki TanakadaDepartment of Macromolecular Science, Graduate School of Science, Osaka University,

Toyonaka,Osaka, Japan; bDepartment of Biotechnology and Life Science, Tokyo University ofAgriculture andTechnology; cInstrumentation Analysis Center, Tokyo University of Agriculture andTechnology; dDepartment of Materials Science and Engineering, Nagoya Institute of Technology

Because of the small number of diffraction spots, structural information available from
X-ray fiber diffraction data of native collagen is very limited, which resulted in the twoplausible molecular models for collagen, the Rich and Crick (10/3-helix) and Okuyama model(7/2-helix) (Okuyama, et al., Biopolymers, 84, 181-191, 2006). The amino acid sequence ofcollagen has very characteristic features with Gly in every third poison and high contents ofimino acid. Collagen-model peptides with these sequence characteristics have provided
valuable physicochemical information from 1960’s. Especially, single crystal structures ofthese peptides at high resolution have provided very important structural information during
the last decade. One of them is the predominant supports for the Okuyama model instead of
the Rich and Crick model (Okuyama, et al., Biopolymers, 84, 421-432, 2006) which isbelieved to be correct since 1955. High resolution structures of model peptides also provide
structural bases for understanding of stabilization of triple-helix by some amino acid residues.
It is well known that Hyp in the Y position stabilizes the collagen triple-helix. This is veryclear by comparing the helix-coil transition temperatures (Tm) of (Pro-Pro-Gly)10 (Tm = 30 ºC)
and (Pro-Hyp-Gly)10 (Tm = 60 ºC). It was reported that the Gly-Pro-Arg sequence in thehost-guest peptide showed a similar Tm compared with that of the Gly-Pro-Hyp sequence(Persikov, et al., Biochemistry, 39, 14960-14967, 2000) . In this study, we report the side
chain conformation of Arg in the collagen triple-helix based on the single crystal structure of
the host-guest peptide, (Pro-Hyp-Gly)3-Pro-Arg-Gly-(Pro-Hyp-Gly)4 (hereafter, PRG).
Single crystal structure of PRG-peptide (a= 23.28, b= 19.57, c= 49.02 Å, b= 94.51º, P21,
Rwork= 0.13, Rfree= 0.198) was analyzed at 1.45 Å resolution by using 6808 reflections with
|Fo|>2σ|Fo| collected in the BL40B2 of SPring-8. No substantial difference of the triple-helix
was observed in the peptide backbone conformation between the PRG-peptide and thehomopeptide with Pro-Hyp-Gly sequence. In the structures of T3-785 (Kramer, et al., Nature

Structural Biology, 6, 454 – 457, 1999) and GFOGER (Emsley, et al., Cell, 101, 47-56, 2000)
peptides, direct hydrogen bonds were reported between Arg side chain and oxygen atom in theadjacent chain. However, no such direct hydrogen bond was observed in the present case.
Instead, the side chains of Arg residues seem to stabilize its triple-helix in two ways. One isvan der Waals interactions between the long side chain of Arg and several parts of theadjacent chain. The other is water-mediated hydrogen bonds between one of three nitrogenatoms in the Arg side chain and one of oxygen atoms in the same molecule.

P06-200

THE STRUCTURAL ANALYSIS OF THE COLLAGEN-MODELPEPTIDE, (Pro-Pro-Gly)4-Hyp-Asp-Gly-(Pro-Pro-Gly)4 CRYSTAL
Tatsuya Kawaguchi1, Masaki Shimura2, Chizuru Hongo1, Keiichi Noguchi2, Kenji Okuyama1,
Kazunori Mizuno3 and Hans Peter Bachinger3
1Department of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka,
Osaka 560-0043, Japan; 2Department of Biotechnology and Life Science, Graduate School ofEngineering, Tokyo University of Agriculture and Technology; 3Department of Biochemistry andMolecular Biology, Oregon Health & Science University

Collagen is the most abundant protein in vertebrate. The triple-helix formation is one of
the characteristics of collagen, with which collagen accomplish its functions in organism. The
triple-helix formation of collagen and its stabilization mechanism had been much interesting
themes. Recently, the Hyp-Y-Gly with high content of Thr in Y position was found in the
Riftia pachyptila cuticle collagen. To investigate the stabilization mechanism of Hyp-Thr-Gly
sequence in collagen, we are analyzing a series of host-guest peptides in which the guest
Hyp-Y-Gly triplet is sandwiched by host Pro-Pro-Gly triplets. In this study, we determined themolecular and crystal structures of (Pro-Pro-Gly)4-Hyp-Asp-Gly-(Pro-Pro-Gly)4 (hereafter,ODG peptide).
The ODG peptide was crystallized by hanging-drop vapor-diffusion method. X-ray
diffraction experiments were performed using the synchrotron radiation source at the BL6A
beam line of PF in KEK, Ibaragi, Japan. The crystal belongs to P21 space group with cellparameters of a = 31.59, b = 21.71, c = 39.15 A, and β = 100.17°. A total of 25,367 uniquereflections with [Fo > σ(Fo)] in the resolution range of 10 to 1.02 A were used for structurerefinement (Rwork = 0.128, Rfree = 0.159).
The helical twist of each triplet had the average values of 49.0° for the host and 52.6°
for the guest regions, which agreed very well with that for the ideal 7/2-helical model (51.4°;
Okuyama model), and not with the 10/3-helical model (36°; Rich and Crick).
The typical interchain hydrogen-bond of (Gly)NH···O=C(X) was observed in the ODG
peptide. Similar to the other Hyp-Y-G peptide, water mediated inter- and/or intra-chainhydrogen-bonds concerning Oδ of Hyp residue were observed. Water mediated inter- and/or
intra-chain hydrogen-bonds concerning Asp carboxyl group were also observed. These
hydrogen-bonds were thought to enhance the stability of the triple helix.
The lateral packing structure of this peptide showed the quasi-hexagonal packing, whichwas usually observed for the peptides with the Pro-Hyp-Gly rich sequence. Two Asp residues
in a triple helix were found to form hydrogen-bonds with Asp residues in the adjacentmolecules and the third Asp was found to interact electrostatically with N-terminal of theadjacent staggered molecule. The poler side chain groups in ODG peptides enhance not only
the intramolecular interaction, but also the intermolecular interaction, which stabilizes
packing structure of this peptide.

P06-201

CRYSTAL STRUCTURE OF 3D8 scFv ANTI-DNA ANTIBODY, ITS
SINGLE DOMAINS, AND THE COMPLEX WITH A SMALL
MOLECULE
Suk-Yeol Park1, Young-Rim Kim2, Yong-Sung Kim3, Myung-Hee Kwon2, Jeong-Sun Kim1,*
1

Dept. of Chemistry, College of Natural Science, Chonnam National University, 300, Yongbong-dong,

Buk-gu, Gwangju, 500-757, Korea.
2

Dept. of Microbiology, Ajou Medical School, San 5, Woncheon-dong, Yeongtong-gu, Suwon 443-749,

Korea.
3

Dept. of Molecular Science and Technology, Ajou University, San 5, Woncheon-dong, Yeongtong-gu,

Suwon 443-749, Korea.

*Corresponding author: jsunkim@chonnam.ac.kr

Anti-DNA antibodies (Abs) are of biomedical interests due to their association with
autoimmune diseases in human and mice. The characterized anti-DNA monoclonal Ab 3D8
scFv from an autoimmune-prone MRL-pr/lpr mouse has shown the binding and hydrolyzing
activities against single stranded (ss-) and double stranded (ds-) DNAs. The lack of theconserved amino acid residues of 3D8 scFv, VH, and VL for DNA-hydrolyzing activities
upon comparison with other nucleases suggests that 3D8 belongs to another family of DNAhydrolyzing enzymes. To understand the molecular mechanism of nucleotide recognition andhydrolysis, we elucidated crystal structure. The detailed structural features will be discussed.
(This work was supported by grant No. R01-2006-000-10743-0 from the Basic
Research Program of the Korea Science & Engineering Foundation.)P06-202

CRYSTAL STRUCTURE OF ydjA FROM ESCHERICHIA COLI
Ji-Woo Choi, Ji-Eun Lee, Che-Hun Jung, and Jeong-Sun Kim
Department of Chemistry, Chonnam National University, Gwangju, 500-757, Korea*Corresponding author: jsunkim@chonnam.ac.kr

Nitrogenreductases mediate the reduction of nitrogen-containing compounds. Often
they require FMN as a cofactor. We elucidated the crystal structure of the putative
nitrogenreductase from E.coli, ydjaA of 193 amino acids, without and with a FMN cofactor.
The structure is composed of a beta-sheet of 5 beta-strands that are sandwiched by threealpha-helices. The detailed structural features will be discussed.

P06-203

CRYSTAL STRUCTURE OF ybfF FROM ESCHERICHIA COLI
Nishi Kosuke, Suk-Youl Park, Sang-Hak Lee, Ji-Woo Choi, Nguyen To Uyen, Ji-Eun Lee,
Che-Hun Jung, and Jeong-Sun Kim
Department of Chemistry, Chonnam National University, Gwangju, 500-757, Korea*Corresponding author: jsunkim@chonnam.ac.kr

The ybfF gene from E.coli belongs to the putative hydrolase family upon the amino acidsequence analysis. To get the clue on the molecular function, we elucidated the crystal
structure of ybfF at 1.1 Å resolution using SAD experiment. The ybfF protein is composed of
two globular domains and the active site is constructed on the domain interface. The detailed
structural features will be discussed.

P06-204

STRUCTURE AND FUNCTIONAL STUDY OF RICE BIFUCTIONAL
ALPHA-AMYLASE/SUBTILISIN INHIBITOR FROM Oryza sativa

Wen-Yan Penga,c, Yi-Hung Lina, Yen-Chieh Huanga, Hong-Hsiang Guana,c, Ying-Cheng
Hsieha,c, Ming-Yih Liua,Tschining Changd, and Chun-Jung Chena,b*aLife Science Group, Research Division, National Synchrotron Radiation ResearchCenter, Hsinchu 30076, Taiwan; bDepartment of Physics, cInstitute of Bioinformatics and Structural
Biology, National Tsing-Hua University, Hsinchu 30013, Taiwan; dDepartment of Hospitality
Management, Nan Jeon Institute of Technology, Yen-Shui, Tainan 73746, Taiwan

Rice seeds are rich sources of different proteinaceous inhibitors with characteristic
bifunctional enzyme-inhibiting activities such as α–amylase/subtilisin and trypsin/chymotrypsin inhibitors. These inhibitors were generally expressed in developing seeds andother organs, and were thought to play an important role in plant’s defense system. It was
generally believed that these inhibitors not only playing a role in plant development but also
conferring a broad spectrum of resistance against pests and pathogens. Nevertheless,high-resolution structures of these inhibitors and in complex with target enzymes are available
in other species but not in rice. Therefore, in this study, we purified RASI (ricealpha-amylase/subtilisin inhibitor, 18.9 kDa) from rice bran into homogenous and crystallizedusing the handing drop vapor diffusion method. According to X-ray diffraction of RASI
crystals at resolution 1.80 Å, the unit cell belongs to space group P21212 with parameters
a=79.99 Å, b=62.95 Å and c=66.70 Å. Preliminary analysis of the protein indicate that there
are two RASI molecules in an asymmetric unit with a solvent content of 44.05 %.Detail of thefunction of RASI in plant seeds seems to remain unclear. Because of its inhibition to
Subtilisin and alpha-amylase of certain bacteria, RASI was considered playing a defense role.
Despite it close structural relationship to other cereals showed distinct differences insequences, in enzymatic and physico-chemical properties as well as the physiologicalexpression to other species. Here we describe the successful purification and crystallographic
characterization of RASI, and the goal of this project is to provide an alternative structuralbases and ultimately functional illustration of enzyme-inhibitor interactions in rice plant
which is one of the three most valuable cereal crops grown worldwide. In comparing between
RASI and the homologous proteins, we can get more information about the protein functions.

P06-205

X-RAY 3D STRUCTURE AND FUNCTION STUDY OF RICELECTIN-LIKE COMPLEX
Chin-Wen Wu,aYen-Chieh Huangb, Hong-Hsiang Guana, Yin-Cheng Hsieha, Chia-Hao Shina,
Tschining Changc, Yi-Hung Linb and Chun-Jung ChenbaInstitute of Bioinformatics and Structural Biology, National TsingHua University, Hsinchu, TaiwanbSynchrotron Radiation Research Center, Hsinchu, TaiwancDepartment of Hospitality Management, Nan-Jeon Institute of Technology, Tainan, Taiwan

Lectins with sugar-binding specificity are widely distributed in higher plants andvarious other species. The expression of rice lectin from Oryza sativa is up-regulated in thegrowing coleoptile when anaerobic stress persists. A rice lectin of molecular weight 15.2 kDa
has been crystallized using the hanging-drop vapour-diffusion method. Except the native
lectin crystal, the complex of lectin and mannose has also been crystallized. In this study,
three crystals (native lectin and two lectin-2αmannobiose crystal with different crystallization
condition) are used to get X-ray diffraction pattern. From the diffraction of the native lectin
crystals at 1.8 Å resolution, the unit cell belongs to space group P3 (1). Preliminary analysis
indicates that there are two lectin molecules in an asymmetric unit. The unit cell of thelectin-2αmannobiose crystals at 1.8 Å resolution belongs to space group C222 (1).
Preliminary analysis indicates that there is one lectin molecule and one 2αmannobiose in an
asymmetric unit. The unit cell of the second lectin-trehalose crystals at 1.78 Å resolution
belongs to space group P2 (1) 2 (1) 2 (1). Preliminary analysis indicates that there are two
lectin molecules and one trehalose in an asymmetric unit.The result of study shows the ricelectin composed of 12 β sheets is a prism structure. The packing forms of the crystal under thedifferent crystallization condition are monomer, dimmer and tetramer. Analyzing the exteriorcharge, there is an anion pocket at the active site composed of six amino acids: Gly14, Leu88,
Gly133, Thr134, Leu135 and Asp137. In the three-dimensional structure, the interaction areaof rice and mannose is in this anion pocket. Gly14, Gly133, Thr134, Leu135 and Asp137 will
form the hydrogen network with O3, O4, O5 and O6 of mannose, and these hydrogen bonds
can stabilize the structure of complex.

P06-206COMPLEX STRUCTURE OF XYLANASE WITH
XYLO-OLIGOSACCHARIDES FROM TRICHODERMAHARZIANUM ETS323 : STRUCTURAL EVIDENCE FOR GLYCOSYL
TRANSFERASE REACTION
En-Hung Liue, Kun-Che Changc, Yuan-Lung Chiange, Ying-Cheng Hsieha,e, Chaur-Tsuen Lob,
a

a

a,e

c

Yi-Hung Lin ,Yen-Chieh Huang , Hong-Hsiang Guan , Kuo-Cheng Peng , Chun-Jung
a,d
Chen
a

Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu

30076, Taiwan;bDepartment of Biotechnology, National Formosa University of Science andTechnology, Yunlin 63208, Taiwan;c Institute of Biotechnology, National Dong-Hwa University,
Hualien, 97401, Taiwan;d Department of Physics, National Tsing-Hua University, Hsinchu 30013,
Taiwan;e Institute of Bioinformatics and Structural Biology, National Tsing-Hua University, Hsinchu
30013, Taiwan

Xylanases catalyze the random hydrolysis of xylan, the most abundant hemicellulose inhigher plants, to xylooligosaccharides and xylose. Trichoderma harzianum have diverse
beneficial effects on plants as biocontrol agents against many soil-borne plant pathogens.
Xylanase from Trichoderma harzianum ETS323, having a molecular weight of 20.5 kDa, hasbeen crystallized using the hanging-drop vapor-diffusion method. According to X-ray
diffraction data of native xylanase crystals at a resolution 1.00 Å, the unit cell belongs tospace group P212121 and has parameters a = 43.21 Å, b = 51.35 Å and c = 95.07 Å. The
crystals of xylanase and xylotriose complex have also been obtained by the soaking methodand diffracted to 1.31 Å.
Complete model building, refinement and analysis of the structure to 1.0 Å-resolution
for native xylanase; structural details of other complex, such as xylobiose, xylotriose,
exlotetraose, xylopentaose and xylohexaose, will also be discussed.

P06-207

CRYSTAL STRUCTURE AND FUNCTIONAL STUDY OF THE
BOWMAN-BIRK INHIBITOR FROM RICE BRAN IN TERNARYCOMPLEX WITH BOVINE TRYPSIN
Hsin-Tai Lia, Yi-Hung Linb, Yen-Chieh Huangb, Ying-Cheng Hsieha,b, Hong-Hsiang Guana,b,Tschining Changc, Andrew H.-J. Wangd and Chun-Jung ChenbaInstitute of Bioinformatics and Structural Biology, National TsingHua University, Hsinchu, TaiwanbSynchrotron Radiation Research Center, Hsinchu, TaiwancDepartment of Hospitality Management, Nan-Jeon Institute of Technology, Tainan, TaiwandInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan

The 15-kDa trypsin inhibitors from rice bran (RBTI) are members of the Bowman-Birk
protease inhibitor (BBI) family. The crystal structure of a 1:1 complex between RBTI andbovine pancreatic trypsin (BPT) was determined by combination of molecular replacement
and electron density modification methods. This complex model has been refined to a
crystallographic R-factor of 26.2% and free R-factor of 31.6% at 3.0 Å resolution. The
RBTI structure consists of seven β-strands and loops without α-helices structure and folds
into two compact domains (N- and C-domain) which are similar to each domain from barley
BBI. However, orientation between two domains is quite different to barley BBI, this makes
the distance between two P1 residues (17Lys and 83Lys) in RBTI is only 23 Å apart rather
than distance of 40 Å in barley BBI. The closer distance provides evidence to support result
from activity assay that two domains show different abilities to inhibit trypsin. RBTI
C-domain with protruding 84Met at P1’ position, moreover, mainly leads into breakdown of
the classically canonical conformation of reactive site loop. Major interaction with BPT isachieved by RBTI N-domain but C-domain plays an auxiliary role to block trypsin molecule.

P06-208

CRYSTAL STRUCTURE STUDY OF WILD TYPE AND MUTATEDBACILLUS CEREUS NCTU2 CHITINASE
Yin-Cheng Hsieh1,2, Chueh-Yuan Kuo1,2 , Huei-Ju Tasi3 , Yi-Hsin Pan3 , Yaw-Kuen Li3 , andChun-Jung Chen1,2
1Life science Group, National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan

2

Department of Bioinformatics and Structure Biology, National Tsing-Hua University, Hsinchu 30076,

Taiwan 3Department of Applied Chemistry , National Chiao-Tung University , Taiwan

Chitin, a β-(1,4)-linked polymer of N-acetyl D-glucosamine (GlcNAc), is widelydistributed in nature, particularly as a structural polysaccharide in fungal cell walls in theexoskeleton of arthropods, the outer shell of crustaceans, nematodes, etc. Chitinases whichhydrolyze chitin as carbon and nitrogen nutrient, occur in a wide range of organisms include
in viruses, bacteria, fungi, insects, higher plants, and animals. A gene of family 18 chitinasefrom Bacillus cereus NCTU2 encodes a signal peptide (27 amino acids) and a mature protein(333 amino acids), The gene of family 18 chitinase from Bacillus cereus NCTU2 wasconstructed in pET-22b(+) and over-expressed by E. coli BL21 (DE3) strain. Amino acidmulti-alignment reveals that E145 and Y227 are the potential residues mediating the catalytic
function of ChiNCTU2. ChiNCTU2 and mutant E145Q of MW 36 kDa have been crystallizedusing the hanging-drop vapor diffusion method with solution consisted of polyethene glycerol
8000、sodium cacodylate and zinc acetate dihydrate. According to diffraction of ChiNCTU2
crystals at resolution 1.20 Å, the unit cell belongs to space group P21 and has parameters a =50.789 Å, b = 48.788 Å and c = 66.867 Å. And E145Q crystal at resolution 1.49, the unit cellbelongs to space group P1 and has parameters a = 61.306 50.820 Å, b =72.888 Å and c =76.343 Å. The protein structure of ChiNCTU2 is monomer by using multiwavelength
anomalous dispersion method and the crystal packing of E145Q is tetramer by using
molecular replacement method. The structure of ChiNCTU2 comprises 12 α-helices and 10
β-sheets. Five residues Asp143、Glu145、Glu190、Gln225 and Tyr227 bind with zinc atoms
in the catalytic domain of ChiNCTU2 protein structure. We proved that zinc atoms will cause
declined activity of ChiNCTU2 by detecting the amount of chitobioside using DNS(3,5-Dinitrosalicylic acid) .We find an angular difference between residue E145 and Q145
when doing superimposition with dimer form ChiNCTU2 and E145Q protein structures
reveals the declined activity of mutant E145Q. We also find that S.marcescens ChiA has
greater catalytic velocity than Bacillus cereus chitinase when interact with colloidal chitin
after doing DNS (3,5-Dinitrosalicylic acid) experiment .After comparing sequences andstructures with other 18 family chitinase, we discover that ChiNCTU2 is the smallest protein
among microbe chitinases.

P06-209

CRYSTALLOGRAPHIC STUDIES OF THE C-TERMINAL DOMAIN OF
DNA GYRASE.
Tung-Ju Hsieha, Hsun-Tang Changa, Te-Sheng Lina, Shu-Yun Haunga, Lynn Farhb, and Nei-Li
Chana.
aInstitute of Biochemistry, National Chung Hsing University, Taichung City 402, Taiwan, andb

Department of Applied Chemistry and Life Science, National Ping Tung University of Education,

Ping Tung 900, Taiwan.

Most bacteria harbor two essential Type IIA DNA topoisomerases, DNA gyrase andtopoisomerase IV (TopoIV). While these two enzymes are homologous, they exhibit distinct
activities. DNA gyrase supports transcription and replication with its unique capability of
introducing (－) supercoils, whereas Topo IV preferentially relaxes (+) supercoils and serves
as the main decatenating enzyme during chromosome segregation. Based on crystal structuresof the C-terminal domains (CTDs) from Borrelia burgdorferi gyrase (BbGyrA-CTD) andBacillus stearothermophilus TopoIV (BsTopoIV-CTD), it was proposed previously that thedivergence of enzyme function can be attributed to differences in the overall shaping of thesetwo domains. However, recently determined CTD of Escherichia coli gyrase (EcGyrA-CTD)
closely resembles BsTopoIV-CTD, rather than its functionally equivalent partner
BbGyrA-CTD.
To understand the molecular basis of this functional divergence in greater detail, we
have now determined the crystal structure of Xanthomonas campestris gyrase CTD(XcGyrA-CTD), and the structure of EcGyrA-CTD was re-determined in a new crystal form.
These two new structures provide strong support for the idea that GyrA-CTD with canonical
GyrA-box sequence most likely folds into a spiral β-pinwheel. A piece of electron density
corresponds to the highly-conserved GyrA-box sequence was identified in one of the
XcGyrA-CTD molecules in the asymmetric unit, representing the first structural information
for this critical functional motif. In contrast to the molecular “Velcro” role of GyrA-box seenin BbGyrA-CTD, we noticed that a region downstream of GyrA-box was found to participate
in the ring-closure in XcGyrA-CTD. Interestingly, the overall spiral-shape of GyrA-CTD
ισ περσιστεντ ρεγαρδλεσσ ωηετηερ τηε β-pinwheel ring is closed or not. Detailed
structural analysis and functional implication of our findings will be presented during themeeting.

P06-210

STRUCTURAL AND FUNCTIONAL STUDIES OF THE
6-PHOSPHOGLUCONATE DEHYDROGENASE ASSOCIATED WITH
PATHOGENESIS OF KLEBSIELLA PNEUMONIAE
Ying-Yin Chen (陳盈頴)1,2, Tzu-Ping Ko (柯子平)2, Li-ping Lo(羅麗萍)2, Chun-Hung Lin(林俊宏)2,3, Andrew H-J Wang (王惠鈞)2,3
1. Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan
2. Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan
3. Genomics Research Center, Academia Sinica, Taipei, Taiwan

The Gram-negative bacterium, Klebsiella pneumoniae, is an opportunistic pathogen thatis commonly isolated from urinary tract infections, nasocomial pneumonia, surgical wounds
and blood stream infections. The enzymes directly related to its virulence are validated as
novel targets for the understanding of the pathogenicity of K. pneumoniae, development of
new antibiotics, as well as decoding of the structure and functional relationship of innate
immunity. The 6-phosphogluconate dehydrogenase (6PGDH) has been determined andannotated as a metabolic enzyme of the pentose phosphate (PPP) pathway. Recent finding
demonstrates that 6PGDH is one of cell wall lectin proteins and elicits a protective immune
response in mice. Our study identifies the structures of 6PGDH from E. coli and K.
pneumoniae and predicts the carbohydrates binding region for its adhesion function. The
resulting high resolution three-dimensional structures will provide valuable information to
design potent enzyme inhibitors as potential new drug candidates.

P06-211

CRYSTALLIZATION AND STRUCTURAL ELUCIDATION OF
PLASMODIUM VIVAX DIHYDROFOLATE
REDUCTASE-THYMIDYLATE SYNTHASE
Puttapol Khongsuk,a Ubolsree Leartsakulpanich,b Yongyuth Yuthavongb and Palangpon
KongsaereeaaDepartment of Chemistry and Center for Protein Structure and Function, Faculty of Science, Mahidol

University, Rama VI Road, Bangkok 10400; bBIOTEC, National Science and Technology Development
Agency, Paholyothin Road, Klong 1, Klong Luang, Pathumthani 12120, Thailand.

The bifunctional enzyme Plasmodium vivax dihydrofolate reductase-thymidylate
synthase (PvDHFR-TS) were purified using a single-step affinity chromatography on
methotrexate-sepharose column. The PvDHFR-TS protein solution was complexed with
NADPH, dUMP and pyrimethamine (Pyr) as an inhibitor. Crystallization was performed by
the microbatch method and DHFR-TS crystal was collected data by using the synchrotron
source equipped with a CCD detector by using beamline 13B1, NSRRC, Taiwan.
The rod-shaped crystal of PvDHFR-TS from mother liquor containing PEG, buffer andsalt grew slowly within 3 weeks. The first crystal belonged to the orthorhombic space group
P212121 with unit-cell parameters of a = 62.36, b = 114.81, c = 198.90 Å. The calculated
Metthews coefficient suggests the presence of two molecules in the asymmetric unit, with asolvent content of 50.6% and the crystal packing revealed a different dimerization mode fromother bifunctional DHFR-TS. The details about the crystallization and the structural
elucidation will be presented and discussed.

P06-212

THE CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF PLANTS
NADPH OXIDASE
Takashi Oda,a Kokoro Hayashi,b Chojiro Kojima,b Hiroshi Hashimoto,a Tsutomu Kawasaki,b
Ko Shimamotob, Mamoru Satoa, and Toshiyuki ShimizuaaInternational Graduate School of Arts and Sciences, Yokohama City University, Japan; b Graduate

School of Biological Sciences, Nara Institute of Science and Technology, Japan

Reactive Oxygen species (ROS) produced by NADPH oxidase play critical roles invarious cellular activities including defense against pathogens by plant. To generate ROS in
defense response against pathogen, plant cells need oxygen in large amounts called
respiratory burst. Plant NADPH oxidase named Rboh (respiratory burst oxidase homolog), isa homolog of mammalian phagocyte NADPH oxidase catalytic subunit gp91phox. The
phagocyte NADPH oxidase forms multi-protein complex containing several membrane andcytosolic regulatory factors and small GTPase Rac. However, in plants, no homologs of theseregulatory factors expect Rac have been found. Rboh possesses an extended N-terminal
domain including two EF-hand motif (EF1 and EF2) which does not exist in gp91phox,suggesting that Ca2+ ions are also involved in the regulation. The regulation mechanism of
NADPH oxidase is different between plants and mammals. It is suggested that Rac functions
as a positive regulator of Rboh. Moreover, plant Rac directly interacts with the N-terminal
domain of Rboh.
To elucidate the regulation and recognition mechanism of Rhoh by Rac and Ca2+ ions,
we determined the crystal structure of N-terminal domain of Oryza sativa RbohB(OsrbohB(138-313)). OsrbohB(138-313) formed homo dimer by two EF-hand motif andcoiled-coil structure. Electron density of Ca2+ ion in EF1 was clearly detected but not in EF2.
The CD spectrum of OsrbohB(138-313) is different between a Ca2+ loaded and free form.
This result suggests that Rboh changes its conformation in a Ca2+-dependent manner. While,
the result of GST pull down assay suggests that Rboh interact with Rac in a Ca2+-independent
manner.

P06-213

HIGHER SIGNAL, LOWER NOISE: HOW TO GET THE BEST DATAFROM YOUR CRYSTALSMartin Adam1, Anita Coetzee1, Bram Schierbeek1, Cary Bauer2 and Rob Hooft2
1

Bruker AXS B.V., Delft, The Netherlands, 2 Bruker AXS Inc., Madison, WI, USA

In a macromolecular crystallography, where crystals are small and often weakly
diffracting, it is imperative to obtain data with as high a signal-to-noise ratio as possible.
Improving the signal usually involves using a more powerful source, since obtaining samples
with larger diffraction volume is often not possible.
The contribution of the noise should not be underestimated. Especially when looking
at weak reflections or small differences in anomalous signal (e.g. doing S SAD phasing on
native proteins) one has to take great care to minimize the experimental noise as much as
possible. This can be done by careful sample handling, minimizing the effect of backgroundscatter from the cryo protectant and loop as well as in setting up the data collection
experiment. Examples of more efficient data collection methods will be presented which canlead to a dramatic increase in signal to noise ratio, with the same amount of X-ray photons
falling on the crystal. If all precautions have been taken to lower the noise of the experiment,
then there is only one way to get a higher a signal-to-noise ratio: increasing the amount of
X-rays on your sample. The MICROSTAR ULTRA, the next generation of the MICROSTAR
series of generators, is substantially brighter than any other X-ray home source available
today. With its revolutionary HyperCoolTM anode cooling technology the MICROSTARULTRA is more intense and yet easier to maintain than other rotating anode generators.

Measurements show that this source compares with many second generation beam lines. Results ofcrystal data will be presented.

P06-214

CRYSTALLOGRAPHIC CHARACTERIZATION OF THE RADIXINFERM DOMAIN BOUND TO CYTOPLASMIC TAIL OF ADHESION
MOLECULE CD44
Tomoyuki Mori, Ken Kitano, Shin-ichi Terawaki, Ryoko Maesaki and Toshio Hakoshima
Structural Biology Laboratory, Nara Institute of Science and Technology (NAIST), Ikoma, Japan.

CD44 is an important adhesion molecule that specifically binds hyaluronic acid, a
typical major component of the extracellular matrix, and regulates cell-cell and cell-matrix
interactions. Increasing evidence has indicated that CD44 is assembled in a regulated manner
into protein complexes at the membrane-cytoskeletal junction, a process mediated by ERM(Ezrin/Radixin/Moesin) proteins. Formation of this protein complex, involving both direct
and indirect interactions, serves to focus downstream signal transduction events that regulate
cell growth and development.
Ezrin, radixin and moesin form the ERM family of proteins, which link membraneproteins to the cytoskeleton and perform structural and regulatory roles at the polarized cellcortex. ERM proteins consist of three functional domains; an N-terminal FERM (Four point
one, Ezrin, Radixin, Moesin) domain, an extended coiled-coil region and a short C-terminal
domain that binds F-actin. The FERM domain associated with the plasmamembrane directly
binds the juxtamembrane region of the cytoplasmic tails of the various transmembraneproteins such as intercellular adhesion molecules ICAM-1, 2, 3 of the immunoglobulin
superfamily, cell-surface glycoprotein CD43, cell-surface hyaluronate receptor CD44. Thus,
notwithstanding the critical role played by these protein-protein interactions from a biologicaland medical perspective, precise details concerning the interaction between the FERM
domain and CD44 remain unknown. Crystallographic studies of the protein complex were
therefore performed in an effort to delineate the interactions between ERM proteins andCD44.
Recently, we obtained the crystal of complex between the radixin FERM domain and
the C-terminal cytoplasmic region of CD44. The crystal of the radixin FERM domain boundto the CD44 cytoplasmic tail peptide belong to space group P212121 with unit-cell parameters
a = 62.70, b = 66.18 and c = 86.22 Å, containing one complex in the crystallographic
asymmetric unit. Intensity data set was collected to a resolution of 2.1 Å.

P06-215

CRYSTALLOGRAPHIC STUDIES OF A LECTIN FROM THE
OCTOCORAL
Akiko Kita,a Mitsuru Jimbo,b Yukio Morimoto,a Ryuichi Sakai,b Hisao Kamiya,b and Kunio
Mikica

Research Reactor Institute, Kyoto University, Kumatori-cho, Sennan-gun, Osaka 590-0494, Japan;b

Department of Marine Biosciences, School of Fisheries Sciences, Kitasato University, Ofunato, Iwate

022-0101, Japan;c

Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto

606-8502, Japan.

A number of lectins, sugar-binding proteins, are known to be present in a variety ofanimals or plants. In marine animals, lectins are believed to contribute as non-selfrecognition factors to the defence mechanism. Interestingly, it has been theorized that somelectins from marine animals mediate the interaction between symbiont and host.
SLL-2 is a D-galactose binding lectin isolated from the octocoral Sinularia lochmodes.
SLL-2 is composed of 94 amino acid residues and contain one glycosylation site. It was
found that SLL-2 was distributed densely on the surface of symbiotic dinoflagellate
Symbiodinium sp. cells. Recently, SLL-2 was confirmed to transform free-swimming stage
Symbiodinium cells into non-motile stage Symbiodinium cells and keep them in their
non-motile stage (K. Koike, et al., Biol. Bull. 207, 80 (2004)). These results indicate that
SLL-2 is a chemical cue in the symbiosis between dinoflagellates and coral. The
three-dimensional structure of SLL-2 may provide information about the symbiosis
mechanism. We started crystallographic works of SLL-2 to elucidate its structure.
SLL-2 was extracted and purified as previously reported (M. Jimbo et al., Biochem.
Biophys. Res. Commun. 330, 157 (2005)). The protein solutions were prepared in Bis-Tris
buffer at pH 6.5. The best crystals of SLL-2 were obtained from the solutions containing
2-methyl-2,4-pentanediol as a precipitant and calcium formate as an additive reagent by thesitting-drop vapour diffusion method at 20˚C. The parallelogram thin crystals were grown
up to the maximum dimension of 0.5mm on one side. The crystals belonged to space group
P21 with cell dimensions of a=52.7 Å, b=189.2 Å, c=57.2 Å, and β=110.8°. The crystal
structure analysis is in progress.

P06-216

CRYSTALLIZATION AND STRUCTURAL ELUCIDATION OF
PLASMODIUM VIVAX DIHYDROFOLATE
REDUCTASE-THYMIDYLATE SYNTHASE
Puttapol Khongsuk,a Ubolsree Leartsakulpanich,b Yongyuth Yuthavongb and Palangpon
KongsaereeaaDepartment of Chemistry and Center for Protein Structure and Function, Faculty of Science, Mahidol

University, Rama VI Road, Bangkok 10400; bBIOTEC, National Science and Technology Development
Agency, Paholyothin Road, Klong 1, Klong Luang, Pathumthani 12120, Thailand.

Antifolate drugs, such as pyrimethamine and trimethoprim, are used to treat malaria.
The target enzyme of these drugs is dihydrofolate reductase (DHFR) that involves in the DNA
synthesis of the malaria parasite.
In nature, Plasmodium vivax dihydrofolate
reductase-thymidylate synthase (PvDHFR-TS) is found to be the bifunctional enzyme.
Drugs resistance to PvDHFR has found in many parts of the world. In order to understandthe drug-resistance mechanism of the enzymes, x-ray crystallography technique has been used
to determine their three dimensional structure.
Recently, PvDHFR structure has been solved by our research group and published.
We found that the inhibition constant (Ki) of the double point mutation (S58R+S117N) shown300-fold and 14-fold (data unpublished) higher resistant to pyrimethamine in PvDHFR andPvDHFR-TS, respectively. In this study, the first structure of PvDHFR-TS has found that its
crystal packing has a different homology dimerization structure from other bifunctional
DHFR-TS structures such as, Plasmodium falciparum and Cryptosporidium hominis. It
speculates that its different structure might come from the interaction of protein surface in themolecule of the enzyme. This x-ray diffraction data were collected by using the synchrotron
source equipped with a CCD detector by using beamline 13B1, NSRRC, Taiwan. The
details of the crystallization and the structure elucidation of the enzyme will be presented anddiscussed.

P06-217

NOVEL DNA-BINDING FOLD AND DNA-RECOGNITION MODEDISCOVERED IN PABI FAMILY OF RESTRICTION ENZYMES
Ken-ichi Miyazono1,7, Miki Watanabe2,7, Jan Kosinski3, Ken Ishikawa2,5, Masayuki Kamo1,
Tatsuya Sawasaki4, Koji Nagata1, Janusz M. Bujnicki3, Yaeta Endo4, Ichizo Kobayashi2,5,6, &Masaru Tanokura1
1 Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences,
University of Tokyo, Tokyo, 113-8657, Japan, 2 Department of Medical Genome Sciences, Graduate
School of Frontier Science, University of Tokyo, Tokyo 108-8639, Japan., 3Laboratory of
Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology,
Trojdena 4, 02-109 Warsaw, Poland, 4 Department of Applied Chemistry, Faculty of Engineering,
Ehime University, Matsuyama 790-8577, Japan, 5 Graduate Program in Biophysics and Biochemistry,
Graduate School of Science, University of Tokyo, Tokyo 108-8639, Japan, 6 Institute of Medical
Science, University of Tokyo, Tokyo 108-8639, Japan, 7 These authors contributed equally to thiswork

PabI is a Type II restriction endonuclease that recognizes 5’GTAC sequence and leave a3’TA overhang (5’GTA/C). PabI and its cognate modification enzyme were identified in
Pyrococcus abyssi through comparison of closely related genomes based on the behavior ofType II restriction-modification gene complexes as mobile elements. While the modification
methyltransferase was easily recognized, PabI was predicted to have a novel
three-dimensional structure by the analysis of amino acid sequence. Additionally, unlike mostrestriction enzymes analyzed, PabI is able to cleave a target DNA in the absence of added
Mg2+. It is very important to analyze PabI structure to understand its overall structure andenzymatic function. To reveal structural basis of PabI, we determined its three-dimensional
structure by X-ray crystallography.
We expressed PabI in a wheat-germ cell-free translation system because protein
expression systems using eukaryotic or prokaryotic cells are not suitable for the expression ofcytotoxic protein. The structure of PabI was determined by the single-wavelength anomalous
dispersion (SAD) method using selenomethionine derivative at 3.0 Å resolution. Structural
analysis of PabI showed that this enzyme adopt a novel protein fold as predicted.
PabI form homodimer by a formation of extended anti-parallel β-sheet that is curved toform an extended groove, which is the unique architecture of PabI. We named this uniquesubstructure “half pipe”. Mutational and in silico DNA binding analyses have assigned thegroove as the double-strand DNA binding site.
Mutational analysis has revealed that there are three residues, Arg32, Glu63, andTyr134, which are indispensable for the catalytic activity of PabI. All of three residues arelocated in the “half pipe” structure of PabI dimer. These residues would act as catalytic or
DNA binding residues.
Miyazono, Watanabe et al. Nucleic Acids Research 2007 35(6):1908-18.

P06-218

SINGLE MUTATIONS LEAD TO SIGNIFICANT INCREASE IN
SUBSTRATE SPECIFICITY AND ACTIVITY: STRUCTURAL, ENZYMEKINETICS AND MOLECULAR MODELING STUDIES FOR CYSTEINEPROTEASE FROM A TROPICAL PLANT
Raka Ghosh, Chandana Chakrabarti, Sampa Biswas and J.K. Dattagupta
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF
Bidhannagar, Kolkata-700064, India.

Latex of a tropical flowering plant, Ervatamia coronaria, contains three papain-like
cysteine proteases - Ervatamin-A, -B and -C. These proteases have been isolated, purified andcharacterized. Among these three proteases, Ervatamin-A and Ervatamin-C, have highhomology in their primary and tertiary structures and they also bear 90 % sequence identity.
In spite of having high similarities, these two proteases show deviations in stability, activity
and specificity. S2 subsite is the major specificity determinant for papain family cysteine
proteases. Enzyme kinetics studies using chromogenic peptides revealed that both theervatamins show preference for branched hydrophobic residues at P2 position of the peptide
substrates but with different degree of efficiency. Biochemical studies show high activity ofErvatamin-A amongst ervatamins towards synthetic peptides and protein substrates.
Compared to Ervatamin-A, there is only one substitution at the S2 pocket of Ervatamin-C(Tyr67 → Ala67) within 10Å sphere around catalytic cysteine. From structural point of view,
this single replacement made the S2 cavity of Ervatamin-C wider preventing proper
environment to bind and fix P2 residue of the above substrates. This is reflected in the higher
KM value of Ervatamin-C compared to Ervatamin-A, i.e., Ervatamin-C exhibits lower
substrate affinity due to this change. There is another single substitution in the helix
containing catalytic cysteine residue which have reducing effect on the catalysis rate (kcat) ofErvatamin-C by reducing polarizibility of the specified helix and inter-domain plasticity.
These two single substitutions reduced specificity constant (kcat/ KM) of Ervatamin-C
significantly (57-times lower). This can be used as a template for SDM studies toappropriately design enzymes. Some results will be discussed.

P06-219

SYNTHESIS AND CHARACTERIZATION OF CuMPt6 (M= 3D
ELEMENTS) TERNARY ALLOYS
Ejaz Ahmed a,b, Miwako Takahashi a, Hiroshi Iwasaki a and Ken-ichi Ohshima aaInstitute of Materials Science, University of Tsukuba, Tsukuba, 305-8573, Japan;bPhysics Division,

Pakistan Institute of Nuclear Science and Technology (PINSTECH), Nilore, Islamabad,Pakistan

We have already identified the crystal structure of newly designed CuMPt6 (M=3delements) alloys by X-ray, electron and neutron diffraction methods [1, 2]. In the analysis, adouble step ordering without any change of cubic symmetry was discovered for CuMnPt6
alloy for the first time. In order to obtain more quantitative information on structure, transition
temperature, electrical behavior and magnetism of this alloy group, we have performed X-ray
diffraction (room temperature and in-situ), electrical resistivity and magnetic susceptibility
measurements. The transition temperatures from disordered to Cu3Au type ordered phases
were determined in a temperature range from 880 oC for M=Co to 1320 oC for M=Ti [3]. The
values of the resistivity were determined as (5~7)x10-3 Ωm. A general trend in magnetic
properties is as follows: paramagnetic – spin-glass like – ferromagnetic – paramagnetic withincreasing atomic number. The variation of the structural ordering in this alloy group is foundto be more systematic with increasing atomic number as compared to magnetic ordering. The
nature of the magnetism is not much affected by the structural phase changes in the present
alloys, though a little change is observed in Tc or Tg. The original nature of the magnetism in
the ternary CuMPt6 alloys remains the same as in the binary MPt3 one. We believe that theunpaired electrons in 3d-elements are responsible for the magnetic properties of CuMPt6
alloys.

P06-220

X-RAY STRUCTURE OF THE SKP1-FBS1 GLYCOPROTEINCOMPLEX
Tsunehiro Mizushima,a Yukiko Yoshida, b Taichi Kumanomidou, a Yuko Hasegawa,a Atsuo
Suzuki,a Takashi Yamanea and Keiji TanakabaDepartment of Biotechnology, Graduate School of Engineering, Nagoya University; Nagoya, Japanb

Department of Molecular Oncology, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan

Ubiquitin-mediated proteolysis plays a regulatory role in a number of diverse cellular
processes and involves the selective destruction of short-lived functional proteins. The
ubiquitin–proteasome system also is responsible for the disposal of misfolded and unfolded
cellular proteins, the aberrant accumulation of which usually causes cell death, which can leadto neurodegenerative diseases. Protein ubiquitination is catalyzed by a sophisticated cascadesystem consisting of the ubiquitin-activating (E1), ubiquitin-conjugating (E2), andubiquitinligating (E3) enzymes. Among these enzymes, the E3 enzymes are responsible forthe selection of target proteins. The ubiquitin ligase complex SCFFbs1, which contributes to theubiquitination of glycoproteins, is involved in the endoplasmic reticulum-associateddegradation (ERAD) pathway. Misfolded proteins and unassembled protein complexes thatfail to assume their functional states in the endoplasmic reticulum are subjected to ERAD,
which involves retrotranslocation into the cytosol and degradation by theubiquitin–proteasome system. In SCF ubiquitin ligases, a diverse array of F-box proteinsconfers substrate specificity. Fbs1/Fbx2, a member of the F-box protein family, recognizes
high-mannose oligosaccharides. To elucidate the structural basis of SCFFbs1 function, we
determined the crystal structures of the Skp1–Fbs1 complex and the sugar binding domain(SBD) of the Fbs1–RNaseB complex at 2.4 and 2.7 Å resolutions, respectively. The structureof the Skp1–Fbs1 complex illustrates a different class of F-box proteins within the SCF
ubiquitin ligase model. The mechanistic model indicated by the structures appears to be wellconserved among the SCF ubiquitin ligases. The structure of the SBD–glycoprotein complex
indicates that the SBD primarily recognizes Man3GlcNAc2. In addition, there are limited
contacts between the SBD and RNaseB; the interface involves only 514 Å2 ofsurface-accessible area. The surface areas occupied by Man3GlcNAc2 and the protein portionof the substrate are 349 and 165 Å2, respectively, suggesting that Man3GlcNAc2, but not theprotein in RNaseB, defines the interaction with Fbs1. SCFFbs1 is a functionally uniquemolecule that recognizes the innermost Man3GlcNAc2 in N-glycans as a marker of denatured
proteins. Our results provide a mechanistic basis for the recognition and ubiquitination ofvarious glycoproteins by SCFFbs1.

P06-221

X-RAY MULTIPLE-WAVE DIFFRACTION ANOMALOUS FINESTRUCTURE
S.-C. Wenga, Y.-R. Leea, Yu. P. Stetskob, W.-H. Suna, Y.-L. Sooa and S.-L. ChangaaDepartment of Physics, National Tsing Hua University, bNational Synchrotron Radiation ResearchCenter, Hsinchu 300, Taiwan, R.O.C.

The combination of x-ray multiple-wave diffraction with diffraction anomalous finestructure (DAFS) technique, Multiple-wave Diffraction Anomalous Fine Structure (MDAFS),
provides long-range order structure information by measuring the multiple-wave diffraction
profiles in the vicinity of an absorption edge of the constituent atom of the sample crystal. The
real part of dispersion correction and fine structure function can be obtained directly bymultiple diffraction analysis without using Kramers-Krong relations (KKR) and kinematicalfitting of diffracted intensity. The useful x-ray phase information of the structure-factor
multiplets, linking the imaginary part with the real part of the structure factor, can easily
replace the Kramers-Kronig relations. Moreover, the constraint imposed by the additionalreflection on the diffraction geometry makes the MDAFS a much more wavevector andsite-sensitive technique than the two-wave DAFS for the measurements. The three-wave
diffraction measurement of GaAs single crystal near the Ga K-edge will be demonstrated as
an example.

P06-222

DYNAMICAL CALCULATION FOR TWENTY-FOUR BEAM X-RAY
DIFFRACTION IN A TWO-PLATE CRYSTAL CAVITY OF SILICON
M.-S. Chiu1), Yu. P. Stetsko2), and S.-L. Chang1)
1)

Department of Physics, National Tsing Hua University; 2)National Synchrotron Radiation ResearchCenter, Hsinchu 300, Taiwan, R.O.C.

The X-ray back diffraction of (12 4 0) in a two-plate silicon resonator takes place at
14.4388 keV, at which simultaneous twenty-four beam diffraction consisting of nine coplanarreflections occurs. Based on the dynamical theory of X-ray diffraction, the numericalcalculation method using a Cartesian coordinate system is employed to deal with the backdiffraction, the interference due to Fabry-Perot type resonance that produces intensity
undulation in both transmitted and back-reflected beams. The coordinates of tie points of thedispersion surface, linear absorption coefficients, wavefield intensities, and excitations ofmode are calculated. The disentangling of 96 dispersion sheets and related linear absorption
coefficients will be discussed. The involved phases in this 24-beam diffraction with X-ray
cavity resonance will be discussed.

P06-223

STRUCTURAL FEATURES OF PSYCHROPHILIC MALATEDEHYDROGENASE ADAPTING TO THE EXTREME ENVIRONMENT
Yasuo Hata,a Tomomi Fujii, a Tadao Oikawab and Kenji Soda a,baInstitute for Chemical Research, Kyoto University, Uji, Japan; bGraduate School of Engineering,Kansai University, Suita, Japan

The psychrophilic and thermolabile malate dehydrogenase from Flavobacterium
frigidimaris KUC-1(FfMDH) was isolated from Antarctic seawater. The enzyme is a
homotetramer with a molecular weight of 123kDa and the number of amino acid residues is
311 for the subunit. To understand structural features of psychrophilic enzymes adapting toetreme environments, the structure of holo-FfMDH has been solved by X-ray crystallography
and compared to those of mesophilic and thermophilic enzymes.
Holo-FfMDH was crystallized by a hanging-drop vapor diffusion method at 288 K. The
crystal grew up to 1.00 x 0.15 x 0.05 mm in a few days. It has space group P3221 with unit
cell dimensions of a=b=147.8 Å and c=165.1 Å, and contains four subunits in the asymmetricunit. Diffraction data were collected at 100 K to 1.8 Å resolution at BL-5A, PF, Tsukuba,
Japan. The crystal structure was solved by molecular replacement using the program
MOLREP and search-model coordinates of a hybrid MDH (PDB code 1GUZ), and refined for
1.8 Å diffraction data to Rwork=0.146 and Rfree=0.164 with the programs CNS and
Refmac5.
The tetrameric structure of FfMDH is a dimer of dimmers and similar to those of MDHs
from other bacteria. A structural comparison of four MDHs from the present psychrophilic,
mesophilic, moderate thermophilic and thermophilic bacteria, however, reveals several
differences in molecular architecture, especially intersubunit interaction. The number of ion
pairs in the FfMDH tetramer is smallest among the MDH molecules compared. Although nofeatures are found in the number of intrasubunit ion-pairs, a remarkable difference lies in thatof intersubunit ion-pairs. The present FfMDH has no intersubunit ion-pairs, although threeother MDHs have two to six ion-pairs between every two subunits in each molecule. Thisdifference becomes marked in two close dimers formed in the tetramer. The lack ofintersubunit ion-pair in the oligomeric molecule results in the loose contact among thesubunits in the molecule. This possibly contributes to the activity expression of the present
psychrophilic enzyme at low temperatures, which may be common to other psychrophilic
enzymes. Further investigations are needed to elucidate the structure-activity relationship ofproteins in such extreme environments.

P06-224

GROWTH RING OF TEETH- A MICRO X-RAY DIFFRACTION STUDYHejing Wanga, Jian Zhoub, Nan Zhenga and Tingjing Xuaa

X-ray Laboratory, School of Earth and Space Sciences, Peking University, Beijing 100871, P. R.
b

CHINA; Chinese Academy of Geosciences, 26 Baiwanzhuang Road, Beijing 100037, P. R. CHINA

Crystallinity of hydroxylapatite in human teeth was investigated using a micro X-ray
diffractometer with a beam spot of 200μm in diameter. A 10-point section crossing
10-year-old deciduous teeth was hopefully selected to clarify the growth ring in teeth. It isrevealed from this 10-point section analysis that most reflections of hydroxylapatite are
getting more and more outstanding and isolating from the most inner parts to the most outerparts in teeth while some reflections of hydroxylapatite are becoming weaker and weaker.
This phenomenon is induced by age of teeth or crystallinity of hydroxylapatite in the sense of
crystallography.
This change of hydroxylapatite in teeth is quantitatively described by the intensity ratioof reflections 112 to 211 that is decreasing from 0.84 in the most inner parts to 0.29 in themost outer parts of teeth and by the intensity ratio of reflections 300 to 211 that is generally
increasing from 0.82 via 0.76 to 2.33 respectively. Meanwhile these three reflections 211, 112
and 300 gradually merge from "two rabbit-ear peaks" into "one peak" with a shoulder.
Accompanying with this cluster change in hydroxylapatite the relative intensity of reflections
130 and 210 decrease from the outer parts to the inner parts and those reflections in the rangeof 45-54º2θ,CuKα merge into three peaks with a bump. The three peaks are reflections 222,
213 and 004 and the bump is consisting of very broad and heavily overlapped reflections 132,
230, 321, 410, 402 and 303. Therefore the intensity ratios of reflections 112 to 211 and 300 to
211 are proposed as the diagnostic indices of crystallinity of hydroxylapatite in teeth.
The TREOR method was used to refine the cell parameters of hydroxylapatite in teeth
and it results a 9.456 angstroms of a and 6.889 angstroms of c lattice parameters with a 7.3
Snyder's Figure of Merit for the most outer parts hydroxylapatite in teeth. For the middle partsof hydroxylapatite, it derives the same cell parameter a as the most outer parts ofhydroxylapatite and a 6.895 angstroms c which is a little bit larger than that of the outer partsof hydroxylapatite in teeth. It is failed to refine the cell parameters of hydroxylapatite in the
inner parts of teeth since heavier overlapping in peak or poor crystallinity.

P06-225

STRUCTURES OF SOME CRYSTAL SOLVATES OF
N-(3-ETHYLTHIO-1,2,4-THIADIAZOL-5-YL-AMINOCARBONYLMETHYL) CYTIZINE
U.S. Mahmudov, T.F. Ibragimov, K.K. Turgunov, B. Tashkhodjaev.
S.Yunusov Institute of Chemistry of Plant Substances, Kh.Abdullaev Str. 77, Tashkent 700170,
Uzbekistan

Investigating structure of N-(3-ethylthio-1,2,4-thiadiazol-5-yl-aminocarbonylmethyl)
cytizine have found inclusion in its crystal a solvent molecules. The crystals obtained by us
for X-Ray analyses from different solvents: aqueous methanol (1) and a absolute acetone (2)had different unit cells and a space groups. Such phenomena aviable at solvatomorphism(inclusion in a crystal of different molecules of the solvent) of crystals. So
N-(3-ethylthio-1,2,4-thiadiazol-5-yl-aminocarbonylmethyl) cytizine behaves as a hostmolecule in relation to solvent molecules and probably is potential clathratogen. For explain
the causes of these phenomena are carried out a X-Ray structural analysis of crystals of titledcompound , grown in above-stated solvents. Results of X-Ray analyses have shown, thatcrystals (1) and (2) contain molecules of water and acetone, accordingly, i.e. takes place aphenomena of inclusion. If, in a crystal (1) solvate (guest) and “host” molecules are in theratio 1:1 whereas in (2) ratio of host and solvent molecules are as 1:2 (in the asymmetric unit
there are two molecules of N-(3-ethylthio-1,2,4-thiadiazol-5-yl-aminocarbonylmethyl)
cytizine and one molecule of acetone).
(1)
• H2O
• 0,5 (СН3) 2СO (2)
14
13
4

5
6

3
2

O

N1

7
8

11
9

10

N12

15

H
N2

N
S N

O

S

C2H5

P06-226

STRUCTURAL EVIDENCE THAT AN α-PROTEOBACTERIA IS THE
OLDEST SURVIVING SPECIESWilliam L. Duax, Robert Huether, Qilong Mao, Vladimir Pletnev, Timothy Umland andCharles M. Weeks
Structural Biology, Hauptman-Woodward Medical Research Institute, Buffalo, NY 14203, USA

The Rossmann fold is one of the most ancient and commonly encountered protein folds.
From 5 to 50 members of the short-chain oxidoreductase (SCOR) enzyme family, whichcontains a Rossmann fold, are present in the genomes of all species sequenced to date. The
SCOR family is part of a much larger superfamily of Rossmann folds that use NAD(H) or
NADP(H) as cofactors. Crystallographic and biochemical studies have revealed that, in thevast majority of Rossmann folds, NAD or NADP cofactor preference is controlled by thepresence of an Asp residue in a specific sequence position in the β2α3 turn or an Arg in theadjacent sequence position, respectively.
The β-ketoacyl [acyl carrier protein] reductase (β-k-ACPR) enzymes, a 912-member
subset of the SCOR family, are essential to fatty acid synthesis in bacteria and plants. By
focusing analysis on the sequence and structure of the 912 β-k-ACPRs in the gene bank, wehave discovered that (1) the most primitive member of the family was an NADP reductase, (2)that NADP binding was originally contingent upon a Ser or Thr residue in the β2α3 turn (notan Arg), (3) that a specific dimer assembly is stabilized by the stacking of aromatic groups at
specific sites on the α5 and α6 helices and (4) that a previously undetected GGMxM sequenceat the C-terminus, conserved in all species of proteobacteria, stabilizes the functionallyrequired tetramer by multiple hydrogen bonding and aromatic ring stacking crosslinking thefour monomers together. We previously discovered that 20% of all the genes in thegenebank have multiple open reading frames (MORFs) and a severe bias in codon use suchthat 85% of the coding in these genes is from the GC-rich half of the genetic code. We havebeen able to identify this pattern in the most ancient members of families of essential proteinthat are present in all species. We have found that 33% of the β-k-ACPR enzymes inα-proteobacteria have multiple open reading frames and a codon bias. Our analysis
indicates that the primordial members of the β-k-ACPR family probably arose in GC-rich
α-proteobacteria and that they are distinguished by the presence of multiple open reading
frames (MORFs), an extreme codon bias in their DNA and an amino acid bias in their protein
composition. In a separate study of the evolution of the (α/β)8 barrel via gene duplication
we have traced the earliest members of that family to α-proteobacteria having high MORF
content, and a codon bias restricted to codon ending in G or C. This research was supported
by NIH grant No. DK26546.

P06-227

STRUCTURAL STUDY FOR THE ENZYME MECHANISM OF
EUKARYOTIC GLUTAMINE SYNTHETASE FROM ZEA MAYS
Takeshi Ozakia, Hideaki Unnob, Toshiharu Hasea, Masami KusunokiaaInstitute for Protein Research, Osaka University,3-2 Yamada-oka Suita, Osaka 565-0871Japan;b

Factulty of Engineering, Nagasaki University, Japan

Plants provide nourishment for animals and other heterotrophs as the sole primary
producer in the food chain. Glutamine synthetase (GS), one of the essential enzymes for plant
autotrophy catalyzes the incorporation of ammonia into glutamate to produce glutamine withconcomitant hydrolysis of ATP, and plays a crucial role in the assimilation and re-assimilationof ammonia derived from a wide variety of metabolic processes during plant growth anddevelopment. The detailed reaction mechanism of higher plant GS is important to obtaininsight into plant productivity and agronomical utility. Recently we determined the crystal
structures of maize glutamine synthetase in complexes with three kinds of substrate analogues.
From these structures we found a unique decameric structure of the enzyme which issignificantly different from the bacterial glutamine synthetase and proposed a phosphatetransfer reaction mechanism of ATP.
In this study, we aims at gaining insights how the enzyme recognize the substrateglutamic acid by the methods of mutagenesis and X-ray crystal structure analysis and we
prepared several mutant enzymes where residues interacting substrate glutamic acid are
mutated. So far we assayed the enzyme activities of the mutant enzymes and have crystallized
some of them. We obtained diffraction data of one mutant. We report here the experimental
procedures and results so far obtained.

P06-228

CRYSTAL SOLVATES OF N-(3-METHYLTHIO-1,2,4-THIADIAZOL-5YL-AMINOCARBONYLMETHYL)CYTISINE
Kambarali Turgunov, Utkur Makhmudov, Temur Ibragimov, Bakhodir Tashkodjaev
S.Yunusov Institute of Chemistry of Plant Substances, Academy of Sciences of Republic of Uzbekistan,77, Kh.Abdullaev str., Tashknent, 100170, Uzbekistan

Cytisine alkaloid (I) and its derivatives attract considerable attention of researchers due
to a broad spectrum of physiological activities [1]. In an effort to get a new physiologic active
substances by institute researchers have been synthesized a series of cytisine derivatives [2].
H

NH
N
O

N

N
N

O

N
S

S

CH3

N

O

I

II

By crystallization of the titled cytisine derivative with structural formulas of II havebeen obtained host-guest complexes containing as guests water, methanol, chloroform, benzol
and pyridine molecules. X-ray structural investigations of obtained crystals shows thatmolecule of II have taken different conformations due to its intramolecular rotate-ability. This
conformation changeability allows to the molecule to forming isostructural host-guest
complexes with functional and geometrical close solvent molecules (Fig.1).

Figure 1. Water and methanol included crystal structures. (H atoms have been omitted)
Reference:1.

Boido CC, Tasso B, Boido V, Sparatore F. Farmaco, 2003, 58(3), p.265. ;2.

V.A.Saprykina, V.I.Vinogradova, R.F.Ambartsumova, T.F.Ibragimov, A.Sultankulov andKh.M.Shakhidoyatov, Chemistry of Natural Compounds, 2004, 40, p.582.

P06-229

SYNTHESIS OF NANOCRYSTALLINE (Co,Ni)Al2O4 SPINEL POWDERBY QUASICRYSTALLINE PRECURSOR
T.P. Yadav1, N.K. Mukhopadhyay2, R.S. Tiwari 1 and O.N. Srivastava1
1

Department of Physics, Banaras Hindu University, Varanasi-221 005 (INDIA)

2

Department of Metallurgical Engineering, Institute of Technology,

Banaras Hindu University,

Varanasi-221 005, (INDIA)

In the present study, attempts have been made to synthesize the nano-crystalline(Co,Ni)Al2O4 spinel
powders by ball milling and subsequent annealing. An alloy of
Al70Co15Ni15, exhibiting the formation of a complex intermetallic compound known as
decagonal quasicrystal is selected as the starting material for mechanical milling. The milling
was carried out in an attritor mill at 400 rpm for
40 hours
with ball to powder ratio of
20:1 in hexane medium. Subsequent to this annealing was performed in an air ambience for10, 20 and 40 h at 600 °C in side the furnace in order to oxidize the decagonal phase andfinally to form the spinel structure Significant enhancement in the magnetic properties has
been found in nano-spinels compared to that of nano-decagonal phase, which can be
attributed to the spinel structures. The weak ferromagnetic close to superparamagnetic
behaviour is established for the first time in the nano-quasicrystalline phase. In case ofnanospinels, the ferromagnetic properties are distinct although it is lower than the ferrite
spinels.

P06-230

PROBING LOCAL STRUCTURES AROUND CO IN
FERROMAGNETIC HfO2:CO THIN FILMS USING EXAFS
Y. L. Soo,a S. C. Weng,a W. H. Sun,a S. L. Chang,a W. C. Lee,a Y. S. Chang,a J. Kwo,a M.
Hong b J. M. Ablett,d C-. C. Kao,d D.G. Liu,c and J. F. Lee ca

Department of Physics;bDepartment of Materials Science and Engineering, National Tsing Hua

University; cNational Synchrotron Radiation Research Center, Hsinchu, Taiwa; dNational
Synchrotron Light Source, Upton, New York, U.S.A.

Local structure surrounding Co in MBE-grown HfO2:Co thin films has been
investigated using the extended x-ray absorption fine structure (EXAFS) technique. Thesefilms are ferromagnetic with Curie temperatures above room temperature. Our EXAFS
results indicate progressive formation of Co clusters accompanied by interstitial doping of Co
in samples grown at a substrate temperature of ~700ºC. On the other hand, films grown at alower substrate temperature ~100ºC were found to be nearly Co-cluster-free. The
low-temperature-grown films are also thermally stable up to an annealing temperature of~700ºC.
Our EXAFS results therefore verify the feasibility for preparing
room-temperature-ferromagnetic HfO2:Co diluted magnetic oxide without formation ofmagnetic Co clusters. These materials have great potential for applications in spintronic
devices.

P06-231

CRYO-CRYSTALLIZATION OF DIETHYL OXALATE AND STUDIESON INTERMOLECULAR INTERACTION
T. Vijay, S. J. Prathap and T. N. Guru Row
Solid State and Structural Chemistry Unit, Indian Institute of Science, Bangalore-12 India

In situ crystallization of a liquid, the subsequent determination of the molecular andcrystal structure and consequently the study of intermolecular interactions is an area ofcontemporary interest. Recently, in situ cryo-crystallization has been used to crystallize
liquids. In this novel methodology in our laboratory, liquid samples are solidified by
selectively cooling them near crystallization temperatures with suitable ramp rates. The
appearance of single crystal is followed by recording rotation photographs on the CCD
detector of the Bruker Apex AXS diffractometer. The cryo-cooling is achieved using either the
N2 stream or the He stream to reach temperatures of crystallization depending on the melting
point of the compound. Diethyl oxalate, a liquid at room temperature, solidifies at about 150
K, has been crystallized in a capillary of diameter 0.3 mm under the nitrogen cold stream
generated by Oxford Cryostream system. The crystal belongs to a monoclinic system, spacegroup P21/c, with Z =4.

The structure is refined to a final R value of 0.08 for 1286 observed reflections. The
molecules are held together via C-H…O interactions generating a sheet like structure whenviewed down the b-axis.

P06-232

CRYO-CRYSTALLIZATION OF DIETHYL OXALATE AND STUDIESON INTERMOLECULAR INTERACTION
T. Vijay, S. J. Prathap and T. N. Guru Row
Solid State and Structural Chemistry Unit, Indian Institute of Science, Bangalore-12 India

In situ crystallization of a liquid, the subsequent determination of the molecular andcrystal structure and consequently the study of intermolecular interactions is an area ofcontemporary interest. Recently, in situ cryo-crystallization has been used to crystallize
liquids. In this novel methodology in our laboratory, liquid samples are solidified by
selectively cooling them near crystallization temperatures with suitable ramp rates. The
appearance of single crystal is followed by recording rotation photographs on the CCD
detector of the Bruker Apex AXS diffractometer. The cryo-cooling is achieved using either the
N2 stream or the He stream to reach temperatures of crystallization depending on the melting
point of the compound. Diethyl oxalate, a liquid at room temperature, solidifies at about 150
K, has been crystallized in a capillary of diameter 0.3 mm under the nitrogen cold stream
generated by Oxford Cryostream system. The crystal belongs to a monoclinic system, spacegroup P21/c, with Z =4.

The structure is refined to a final R value of 0.08 for 1286 observed reflections. The
molecules are held together via C-H…O interactions generating a sheet like structure whenviewed down the b-axis.

P06-233

CRYSALISPro’S ADVANCED STRATEGY MODULE FOR CHARGEDENSITY EXPERIMENTS
Dr. Jiwen Cai
Oxford Diffraction, 68 Milton Park, Abingdon, OX14 4RX, UK

Oxford Diffraction manufactures and supplies single crystal X-ray diffraction
equipment, including a range of kappa-goniometer based Xcalibur and dual wavelength
Gemini diffractometers, as well as the sub 15K base-temperature Helijet open flow helium
cooler.
Our award winning hardware and CrysAlisPro software are being used in over 150
laboratories world-wide to carry out a broad range of crystallographic research, including theareas of modulated / incommensurate, quasi-crystalline materials as well as high pressure,
diffuse scatter and highly demanding charge density studies.
The strategy module in CrysAlisPro takes full advantage of the agility of the four circle
kappa platform and allows an unprecedented ease of use for creating data collection strategies
for everyday use and for advanced charge density studies. Calculation of the most optimal,
multiply-redundant, high resolution strategies are created at a click of a button, whilst
maximising coverage and fully utilising the particular crystal symmetry and orientation.

P06-234

NON-CONVENTIONAL SCATTERING STUDIES OF MATERIALSUSING A LABORATORY IMAGE PLATE DIFFRACTOMETER
Lynne H. Thomas1, Sylvia E. McLain2, Andrew Parkin1, and Chick C. Wilson1
1. Department of Chemistry and WestCHEM Research School, University of Glasgow, Glasgow, G12
8QQ, U.K.

2. 2Oak Ridge National Laboratory, PO Box 2008 MS6475, Oak Ridge TN 37831-6475,

U.S.A.

Recent trends in the development of X-ray diffractometers have been towards fast
readout detectors such as CCDs. Image plate detectors, however, have the advantage thatlong exposure times are possible due to their high dynamic range, allowing weaker scattering
to be observed without suffering from detector overloads or from dark current accumulation.
Experiments involving measurements such as liquid scattering and diffuse scattering whichhave previously required the use of high flux synchrotron radiation have been demonstrated to
be possible on a laboratory diffractometer using a curved image plate detector. Diffuse
scattering has been observed to arise from a wide range of different materials and its presence
is often unexpected. The mechanism behind such scattering is often complex, however
insights can be gained from consideration of the average structure of the material and thecomparison to similar features in systems where the disorder has been characterised using
modeling techniques such as Monte Carlo and Reverse Monte Carlo. The feasibility ofcollecting liquid diffraction patterns with the aim of studying the early stages of moleculararrangement within solution prior to crystallisation has also been investigated and preliminary
results arising from this will be presented.

P06-235

CLASSIFYING MOLECULAR GEOMETRIES: APPLICATION OF
FACTOR ANALYSIS TO CLUSTER FORMATION IN dSNAP.
Duncan Sneddon, Christopher J. Gilmore, Gordon Barr, Wei Dong, Andrew Parkin, andChick C. Wilson,
WestChem. Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, Scotland.

Cluster analysis is a well-established tool in statistics, but one that is used surprisingly
little in crystallography. We have established its use in analysing the results of databasesearches using the Cambridge Structural Database (CSD).
CSD searches can produce thousands of 'hits' especially if a simple fragment is used as
the search fragment. As a result processing and interpreting the results can be a laborious
task and one where mistakes are easy to make. Cluster analysis, involving dendrograms,
metric multidimensional scaling and other visualisation tools, can reduce the workload to afew hours in the hand of an experienced user. dSNAP is a cluster analysis program thatprovides these tools.
Factor analysis and other statistical methods are being used, in combination withvisualisation techniques, including biplots, to uncover the latent underlying structuralproperties of the molecular fragments under investigation. This process is being undertaken inconcert with investigations into many of the possible descriptions of the geometries of thefragments under study.
Details of this two-pronged approach will be presented, along with its utility as amethod to uncover the underlying reason behind the formations of clusters in dSNAP. The
development of this additional feature within our suite of automated methods for interpreting
CSD data should substantially ease the interpretation of the results of cluster analysis.
The application of the biplots being developed will be discussed, and illustrated with asimple example to illuminate the properties of biplots and what makes them such a useful tool
to a user of dSNAP.
The dSNAP software is available free of charge to all interested researchers, distributed
through Glasgow University and Bruker-AXS (http://www.chem.gla.ac.uk/snap/).

P05-014

Araki, Hiromi

O2C05-A1

Abe, Nobuyuki

O2B05-A5

Arima, Hiroshi

P05-089

Abe, Yuichi

P06-165

Arima, Taka-hisa

O2B05-A5

Ablett, J. M.

P06-230

Arimoto, Masanori

P05-184

Acharya, B.S.

P06-079

Aruga, Kumiko

O6B07-A4

Adachi, Shin-ichi

O3C06-M3

Asai, Kazuhiro

P05-087

Adam, Martin

O2C05-A5

Asano, H.

Abdel-Baset, A.M.

O5C07-M4

P05-108

Asano, Yasuhisa

P06-192

P06-213Ashida, Hiroki

P05-177
P05-178

Adams, Chris

O4B06-A6

Adams, Julian

O3C06-M1

Ago, Hideo

P05-184

Ahmed, Ejaz

P06-219

Ashmore, Jason

O4B06-A1

Ahmed, Gulzar

P05-034

Athimoolam, S.

P05-115

Ahuja, B. L.

P05-034

Aizawa, K.

O5C07-M4

Aizawa, Kazuya

P05-001

Ashida, Yasunari

O6B07-A3
P05-127

P05-116
Au-Yeung, Alex S-F.
Avdeev, M.

P06-063
O5C07-M1

P05-002

P05-093

Akao, Tetsuyuki

P06-165

P05-102

Akiba, ToshihikoP06-165

Akita, Fusamichi

O2A05-A6

Baba, Seiki

P06-008
P06-010

Akita, Koichi

P05-001

Babu, K.H.Venkatesh

O1A05-M5

Alemi, A A

O4C06-A6

Bachinger, Hans Peter

P06-200

Alshahateet, Solhe F.

O4B06-A1

Balaji, A.K.

P05-121

Amanokura, Natsuki

P05-127

Balamurugan, B.

P06-054

Barr, Gordon

O1A05-M5
P06-067
P06-235

P06-055
Anders, Robin

O2A05-A4

Anilkumar, G. N.

P05-137

Bauer, Cary

P06-213

P05-138

Beckers, D.

O1B05-M5

Aoki, Ken-ichi

P06-161

Aoki, Ryoma

P05-122

Aoyagi, Shinobu

O6C07-A1

Batchelor, Adrian

O2A05-A4

P05-141
Benedik, Mike

O4A06-A1

Betzel, C.

P06-155

P05-030

Bhagavannarayana, G.

P05-117

P05-184

Bhakuni, V.

O5A07-M2

Aoyama, H.

O3A06-M3

Bhattacharjee, Shuvrajyoti

P05-017

Appelqvist, I.A.M.

O5B07-M1

Bhushan, Asha

P06-151

Arai, Masatoshi

O5C07-M4

P06-156

P05-001

Bird, A.R.

O5B07-M1

P05-002

Bishop, Roger

O4B06-A1

Biswas, Sampa

P06-218

Chang, Yi-Wei
Chantrapromma, Suchada

P06-197
O1B05-M4

Bong, Young-Jong

O4A06-A5

Boonnak, Nawong

O1B05-M4

Bora, Sanchay J.

P06-064

Briggs, James

O4A06-A1

Chao, Chun-Hsiung

P06-004Brindha, T.

O1A05-M5

Charles, P.

P05-171

O2B05-A4
Chanvrier, H.

O5B07-M1

Broennimann, ChristianP06-007

Chatkon, Aungkana

P06-059

Bujnicki, Janusz M.

P06-217Chatterji, Dipankar

O2A05-A1

Butun, Vural

O1C05-M6

Chen, Andy P.

O3A06-M5

Cai, Jiwen

O4A06-A2

Chen, Cheng-Chi

P06-013

P06-233

Chen, Cheng-Yu

P06-051

O3B06-M4

Chen, Chien-Te

P06-004

O6B07-A1

Chen, Chun- Jung

P06-074

P06-013

Chen, Chun-Hsien

P06-082

Caira, Mino R

P05-139

Chen, Chun-Jung

P06-004

Chak, Kin-Fu

P05-169

P06-204

Chakrabarti, Chandana

P06-218

P06-205

Chan, Nei-Li

P06-144

P06-206

P06-145

P06-207

P06-209

P06-208

Cai, Y. Q.

Chandramani, R.

O6B07-A2

Chen, Jinli

P06-052

Chang, Chi-Fon

P05-027

Chen, Lirong

O1A05-M4

Chang, Dah-Tsyr

P06-196Chen, S. M.

P05-105

Chang, En-Cheng

P06-163

Chang, Fang-Yu

P06-196

Chang, Geoffrey

P05-113
Chen, S.-Y.

P06-069

O3A06-M5

Chen, Szu-Miao

P05-040

Chang, Hsun-Tang

P06-209

Chen, Wei-Ti

P05-175

Chang, Kun-Che

P06-206

Chen, Wen -Liang

P06-074

Chang, P.

P06-045

Chen, Yen-Fu

P05-132

Chang, S. L.

P06-230

Chen, Yen-Ju

O3A06-M5

Chen, Yi

O4A06-A2

O4C06-A4

Chang, Tschining

P06-069

Chen, Ying-Yin

P06-210P06-221Cheng, Li-Chi

O6C07-A5

P06-222Cheng, Wen-Chi

P05-132

P06-070

Cheng, Zhongyun

O1A05-M2

P06-204

Chernega, Alexander N.

P06-049

P06-205

Chiang, Cheng-Hung

P06-004

P06-207

Chiang, Chia-Wang

P06-144

Chang, Y. S.

P06-230

Chang, Y.-Y.

P06-069

P06-145
Chiang, Fu-Kuo

P05-100

Chiang, T.-C.

O4C06-A4

Czabotar, Peter E.

O4A06-A6

Chiang, Yuan-Lung

P06-206

Czoschke, P.

O4C06-A4

Chin, Ko-Hsin

P06-193

Dahl, Christiane

P06-198

P06-194

Dai, Shuen-Jie

P06-056

Chinte, U.

O3A06-M2

Daimon, Masahiro

O3C06-M3

Chirifu, Mami

O6A07-A5

Das, Birinchi K.

P06-064

Chiu, M.-S.

P06-222

Dasgupta, Prabal

P06-046

Cho, B. K.

O2B05-A3

Dattagupta, J.K.

P06-218

Choi, Hyungkyu

O1C05-M4

Davis, Simon J.

O6A07-A5

Choi, Ji-Woo

P06-202

Davlieva, Milya

O4A06-A1

P06-203

Degen, T.

O1B05-M5
P05-141Choi, Sung-Min

O5C07-M2

Chollet, Matthieu

O3C06-M3

Deniz, Hakan

O4C06-A2

Chong, Khoon Tee

O2A05-A6

Deshayes, Kurt

O4A06-A6

Chopra, Deepak

P05-128

Dharmaprakash, S. M.

P05-117

Chou, Shan-Ho

P06-193

Dillard, Bret

P05-191

P06-194

Doe, Changwoo

Chou, Tsung-Lin

P06-163

Dong, Wei

Chou, Wei-I

P06-196

O5C07-M2
P06-067
P06-235

Christensen, Mogens

O2B05-A2

Dönni, A.

P05-090

Chrzas, John

O1A05-M4

Dorset, Douglas

P05-022

O3C06-M2

Du, Chao-hung

O3B06-M6

Chu, Chen-Hsi

P06-195

Du, S.

O3A06-M2

Chu, Chia-Hung

P06-070

Duangthongyou, Tanwawan

O4B06-A6

Chu, Ming-Wen

P05-100

Duax, William L.

P06-226

Chuang, Wei-Tsung

P05-025

Dungkaew, Winya

P06-076
P06-077

P05-026
Chuang, Yu-Chun

P05-123

Durham, Mark

P06-167

P05-036

Ebara, Kazuhiro

O5C07-M4

P05-040
Chung, Shih-Chun

P05-002

P06-004

Ebiszaki, Toshikazu

P05-184

P06-013Ehrenberg, H.

P06-047

Clements, Richard

P05-106

Eikenberry, Eric F.

P06-007

Coetzee, Anita

P05-108

Elcombe, M.M.

O5C07-M1

P06-213Endo, Yaeta

P06-217

Coley, Andrew

O2A05-A4

Ethayathulla, A. S.

O5A07-M2

Colman, Peter M.

O4A06-A6

Ezaki, Takayuki

P06-162

Craig, Donald C.

O4B06-A1

Fairlie, W. Douglas

O4A06-A6

Cramer, William A.

O3A06-M4

Fait, James

O3C06-M2

Cuong, Tran-Kim

P06-075

Fait, Jim

O1A05-M4

Fan, Hua

P06-146

Ghosh, Raka

P06-218

Fang, Yilan

P06-198

Gidley, M. J.

O5B07-M1

Farh, Lynn

P06-209

Gilbert, E.P.

O5B07-M1

Feng, Donglai

O6B07-A1

Feng, Zhe Chuan

O6C07-A5

P06-067

P06-052

P06-235

Ferrara, Joseph D.

O1A05-M3
P06-006

Gilmore, Christopher J.

P05-022

Gonczy, John

O3C06-M2

Gopalakrishnan, K.

O1A05-M5

Gopalakrishnapillai, Vikram

P06-150

Goto, T.

P05-090

Flanagan, B.M.

O5B07-M1

Florence, Quentin

P05-191

Foley, Michael

O2A05-A4

Gouaux, Eric

O3A06-M1

Forwood, Jade K.

O4A06-A3

Gouda, Masaki

P06-158

Fu, Zeng-Qing Albert

O1A05-M4

Gray, A.

O3C06-M2

Guan, Hong-Hsiang

O4C06-A4
P06-074

Fuess, H.

P06-047

P06-204

Fujii, Hiroki

P05-101

P06-205

Fujii, Isao

P05-122

P06-206

P05-135

P06-207

O6B07-A3

Guegan, R.

O4C06-A1

P05-126

Guendouz, M.

O4C06-A1

P05-133

Guérin, Laurent

O3C06-M3

Fujii, Tomomi

P06-223

Guncar, Gregor

O4A06-A3

Fujimoto, DaisukeP05-131

Guo, Rey-Ting

P05-179

Fujinami, Shuhei

P05-109

Guo, Yu-Ruei

P06-056

Fujiwara, KeikoP05-096

Gupta, Surbhi

O2A05-A1

Fukai, Shuya

P06-142

Gutov, Olexii V.

P06-049

P06-143

Haga, Mitsuru

P06-199

PL07-004

Hagiya, KenjiP05-110

O5A07-M4

Hakoshima, Toshio

P06-166

Fujii, Kotaro

Fukami, Takaaki A.
Fukui, Hiroshi

P05-089

P06-214

Fukumori, Yoshihiro

O2A05-A7

Hall, Syd

P05-190

Fukuyama, Yoshimitsu

O3C06-M4

Haller, Kenneth J.

P05-136

Fun, Hoong-Kun

O1B05-M4

P06-058

O2B05-A4

P06-059

P05-117

P06-060

Funahashi, Shiro

O2C05-A3

P06-061

Gaponov, Yurii

P06-011

P06-076

Gee, Christine L.

O6A07-A1

P06-077

Geng, Jie

O4A06-A2

Ghosh, Baidyanath

P05-021

Hameed, B.ShaahulHan, Yiping W.

O1A05-M5
P06-167

Han, Young-Soo

O5C07-M2

Hibino, H.

P05-087

Hanashima, Takayasu

P06-043

P05-098

HANESAKA, Makoto

O1C05-M3

P06-009

Hanke, G. T.

P05-180

Hietschold, Michael

P06-072

Hanrahan, Jane

P05-028

Higuchi, KazuhikoP06-165

Harada, Jimpei

P05-019

Hikima, Takaaki

P06-008

Harada, Jun

O6B07-A5

Hiraki, MasahikoP06-011

Harakawa, Mayuko

O6B07-A5

Harata, Kazuaki

P06-165

Hirano, Yu

O6A07-A4

Harjo, Stefanus

P05-001

Hiraoka, N.

O3B06-M4

Hase, T.

P05-180

Hase, Toshiharu

P06-227

Hirata, Kazuto

P05-101

Hasegawa, Kazuya

P06-005

Hirata, Kunio

P06-005

P06-012

O6B07-A1

P06-008

P06-008
P06-010

Hiro, Kazuya

P05-118

Hasegawa, Yuko

P06-220

Hirota, Kazuma

O2B05-A5

Hashimoto, Hiroshi

P06-212

Homrichhausen, Tanja

O3A06-M1

Hashimoto, Shouichi

O6B07-A6

Hashimoto, Takafumi

P05-086

Hong, H.

O4C06-A4

P05-094

Hong, M.

P06-045

Honda, Nobuo

P06-011

P06-230

Hashizume, Daisuke

P05-032

Hata, Yasuo

P06-223

Hong, Po-Da

P05-025

Hattori, Motoyuki

PL07-004

Hongo, Chizuru

P06-199
P06-200

P06-142
P06-143

Hooft, Rob

P05-108P06-213

Haung, Shu-Yun

P06-209

Hayashi, Chiharu

O6A07-A5

Horiguchi, Masahiro

P05-131

Hayashi, Kokoro

P06-212Horward, Andrew

O1A05-M4

O5C07-M4

Hoshida, Kazunori

P05-124

Hayashi, M.

P05-002

Hoshikawa, A.

O5C07-M4

Hayashi, Yoshihito

O6B07-A6

P05-101

Hayashi, Yusuke

P06-081P05-186

Haynes, Richard K.

O1B05-M2

Hoshino, Manabu

O2C05-A2

Hefni, M. A.

P05-014

Hosoya, Takaaki

P05-002

Heinemann, Udo

P05-171

Hossain, Md. Motarab

O6A07-A4

Henderson, Kylie

O2A05-A4

Houslay, Miles

O4A06-A2

Heo, Kyuyoung

O1C05-M1

Howard, Andrew

O3C06-M2

Hester, J.R.

O5C07-M1

Hsiao, Chwan-Deng

P05-130

Hibbs, David

P05-028

P05-173

P05-029

P05-175

Hsiao, Chwan-Deng

P06-197

Hume, David A.

O4A06-A3

Hsiao, He-Hsuan

P06-160

Hung, Chiu-Lien

P06-051

Hsiao, Yu-Yuan

O2A05-A2

Hung, Luu Tien

P06-072

Hsieh, Tung-Ju

P06-209

Hung, Mien-Chie

P05-173

Hsieh, Yin-Cheng

P06-205

Hussain, A.

P05-085

P06-208

Hwang, Ching-Shiang

P06-004

P06-204

Hwang, Kuo Chu

P05-114

P06-206

Hwang, Kwang Yeon

O4A06-A5

P06-207

Iversen, Bo B.

O2B05-A2

P05-026

Ibragimov, T.F.

P06-225

Hsu, C.-H.

P06-228

P06-045
P05-035

Ichikawa, Hirohiko

O3C06-M3

P05-039

Ichimaida, Fumiko

O5A07-M3

P05-113

Ichimatsu, Tokio

P06-165

P06-082

Ichimiya, Tomomi

P06-164

Htoon, A.

O5B07-M1

Ichiyanagi, Kouhei

O3C06-M3

Hu, Shu-Hong

O6A07-A1

Ida, AkihiroP05-109

Hua, Yu-Wen

P06-051

Ida, Takashi

P05-087

Huang, Cheng-Yang

P05-173

Hsu, I. J.

Hsu, Liang-Yan

P05-175
Huang, Ching-Mao

O1C05-M5

P06-009
Ide, Semra
Igarashi, Noriyuki

O1C05-M6
P06-011
P06-012Huang, Chi-Yi

P06-013Huang, Chu-Wan

O6C07-A5

Ihara, Hideshi

P05-185

Huang, Di-Jing

O3B06-M2

Ikeda, Naoshi

P05-020

Huang, Fei-Ting

P05-100

Ikemizu, Shinji

O6A07-A5

Huang, Kai-Fa

P06-163

Huang, M. L.

P06-045

Ikoma, Kyoko

P05-185

Huang, Tzu-Wen

P05-024

Inagaki, Y.

O2B05-A6

Huang, Wei-Ting

P06-056

Inaka, Koji

P05-181

Huang, Yen-Chieh

P06-204

Inazato, Miyuki

P06-168

P06-205

In-noi, Orrasa

P06-060

P06-206

INOUE, Katsuaki

O1C05-M2

P06-207

Inoue, Tsuyoshi

P05-177

Huang, Yu-Shan

P06-168

P05-023

P05-178

P05-026

P05-181P05-027

P05-182

P05-040

Ip, Nancy Y.

P06-004

Iriyama, MichikoP06-054

Iseki, Aika

P05-124

Ishida, Hiroyuki

P05-178

Huber, Thomas

O4A06-A3

Huether, RobertP06-226

O1B05-M3

Ishigaki, T.

O5C07-M4
P05-003

Jean, Yuch-Chen
Jeng, U-Ser

P06-004
O1C05-M5

P05-186

O1C05-M6

P06-158

P05-023

P06-159

P05-025

Ishii, H.

O3B06-M4

P05-026

Ishii, Kenji

O3B06-M1

P05-027

Ishii, Satoshi

P05-111Jeng, Wen-Yih

P05-179

Ishikawa, Ken

P06-217Jennings, Michael P.

P06-160

Ishitani, Ryuichiro

P06-142

Jeon, Hye-Jin

O1C05-M4

P06-143

Jeyaprakash, A.A.

O6A07-A3

PL07-004

Ji, S.

O2B05-A3

O2B05-A6

Jiang, Long

O4B06-A3

P05-098

Jimbo, Mitsuru

P06-215

P05-099

Jin, Bih-Yaw

P06-082

Isobe, Kiyoshi

O6B07-A6

Jin, Kyeong Sik

O1C05-M1

Isobe, MasahikoP05-107

Jin, Sangwoo

O1C05-M1

Ito, Akio

P06-165

Jin, Zhongmin

O1A05-M4

Ito, Eiji

P05-094

Ito, Ken-ichi

P05-038

Ito, Koreaki

PL07-004

Ito, L.

O1A05-M1

Kabuto, Chizuko

P06-053

P05-188

Kabuto, Kuninobu

P06-053

Ito, Makoto

P05-182

Kadowaki, Kazuo

P05-101

Ito, Takayoshi

P05-020

Kagomiya, I.

O2B05-A6

Itoga, ChihiroP05-133

Kai, Hirofumi

O6A07-A5

Itoh, Shinji

P05-101

Kai, Yasushi

O2C05-A4

Iversen, Bo Brummerstedt

P05-030

P05-177

Iwasaki, Hiroshi

P06-219

P05-178

Iwata, Makoto

P05-018

P05-181

Ishiguro, Hiroshi

Ishizawa, N.

Iwata, So

O3A06-M2

Izumi, F.

P05-090

Jaikumar, M.

O3C06-M2
Jung, Che-Hun

P06-202
P06-203

Kaizu, Youkoh

O2C05-A2
P05-111

O1A05-M5

Kakeya, Itsuhiro

P05-101

Jain, R.

P06-155

Kakimoto, K.

O2B05-A6

Jain, Rishi

P06-157

Kakinuma, Yoshimi

O3A06-M2
O3B06-M3

James, David E.

O6A07-A1

Kakiuchi, Toru

Jarrige, I.

O3B06-M4

Kakuta, Yoshimitsu

P05-182

Jarry, AngéliqueP05-093

Jasti, Jaysankar

O3A06-M1

Kambayashi, Koji

P05-182

Jayatilaka, Dylan

P05-187

Kamiya, Hisao

P06-215

Kalaivani, M.

O1A05-M5

Kawata, Hiroshi

O3C06-M3

P05-003

Kawate, Toshimitsu

O3A06-M1

P05-186

Kawsar, Hameem

P06-167

Kamo, Masayuki

P06-217

Ke, Hengming

O4A06-A2

Kanai, Ryuta

P06-165

Kamiyama, T.
Kamiyama, Takashi

Kanamono, Hiroshi
Kanaujia, Shankar Prasad

O5C07-M4

O5A07-M5

O6B07-A6

Ke, Mei-Ju

P06-056

P06-153

Kellie, Stuart

O4A06-A3

Kennedy, Brendan J

O6C07-A3

Kanehisa, Nobuko

O2C05-A4

Kaneko, Koji

O2B05-A1

P05-015

Kaneko, M.

P05-090P05-084

P05-127

P05-106

P06-054

Kesavulu, Muppuru M.

P05-130

P06-055

Khongsuk, Puttapol

P06-211
P06-216

Kang, Min Kwan

O1C05-M4

Kanoda, Kazushi

O3B06-M3

Khosavithitkul, Nongnaphat

P05-136

Kao, C-. C.

P06-230

Kiatpichitpong, Angkana

P06-078

Karakane, Yuji

P05-095

Kihara, Kuniaki

P05-109

O5C07-M4

Kikuma, Genki

P06-080

Kasao, T.
Katayama, Hideki

P06-165

Kim, Eunice EunKyeong

O4A06-A5

Katayama, Yoshinori

P05-089

Kim, J. Y.

O2B05-A3

O3C06-M4

Kim, Jehan

O1C05-M1

Kato, Kenichi
Katsuragawa, Hiroyuki

P06-041

Kim, Jeong-Sun

P06-201

P06-042

P06-202

P06-043

P06-203

Katsuya, Yoshio

P05-016

Kim, Jungeun

O3C06-M4

Kaung, Pho

P05-121

Kim, Kook-Han

O4A06-A5

O5A07-M2

Kim, Kwang-Woo

O1C05-M1

P06-154

Kim, Sung-Hou

P06-198

P06-155

Kim, Tae-Hwan

O5C07-M2

O4A06-A4

Kim, Yong-Sung

P06-201

P06-147

Kim, Young-Rim

P06-201

P06-149

Kimani, Serah

P05-183

P06-150

Kimino, TairaP05-135

P06-151

Kimura, Hiroyuki

O2B05-A1

P06-157

Kimura, Shigeru

O3C06-M4

P05-170

Kinoshita, Takayoshi

Kaur, P.

Kaur, Punit

Kawaguchi, Tatsuya

P05-185

P06-200

P06-158

Kawamoto, Atshushi

O3B06-M5

P06-159

Kawamoto, Masahide

P06-008

Kishimoto, N.

P05-090

Kawasaki, Tsutomu

P06-212

Kita, Akiko

O2A05-A7

O5A07-M4

Kosinski, Jan

P06-217

P06-215

Kosuke, Nishi

P06-203

Kitada, Sakae

P06-165

Krachodnok, Samroeng

P06-060

Kitade, Yukio

P06-161

P06-061

P06-162

P06-078

Kita, Akiko

Kitano, Ken

P06-166

Krause, Kurt

O4A06-A1

P06-214

Krishna, J.Radha

O5B07-M2

O2C05-A1

P05-120

Kitazawa, H.

P05-090P05-121Kline, Steven R

O5C07-M2

Krishna, P.S.R.

O6C07-A4

Ko, Tzu-Ping

P05-179

Krishnaiah, M.

O5B07-M2

Kitayama, Nobuyuki

P06-210P05-120

Kobayashi, H.

P05-090P05-121

Kobayashi, Ichizo

P06-217

Kobayashi, T.
Kobayashi, Yasuo

Kudoh, Yasuhiro

P06-041

O1A05-M1

Kumanomidou, Taichi

P06-220

P05-188

Kumar, K. Chandra

P05-140

P05-003

Kumar, R. Prem

O4A06-A4
O5A07-M2

Kobe, Bostjan

O4A06-A3

Kohgi, Masafumi

O2B05-A1

Kumar, R.Senthil

O1A05-M5

Kohn, Harold

O4A06-A1

Kumar, Sanjit

O4A06-A4
P06-152

Koishi, Shigenori

P05-107

Kojima, A.

P05-088

Kojima, Chojiro

P06-212

P06-008

Kokila, M. K.

P05-137

P06-010

Kumasaka, Takashi

P06-005

P05-138

Kuo, Chueh-Yuan

P06-208

P05-140

Kuribayashi, Takahiro

P06-041

Komatsuzaki, K.

O5C07-M4

Kurihara, Kazuo

P05-002

Komeda, Hidenobu

P06-192

Kurihara, Tadashi

P06-164

Komiyama, Satoshi

O3B06-M5

Kurisu, G.

P05-180

Komori, Takashi

O2C05-A3

Kuroiwa, Yoshihiro

Komura, Yasuhiro

P05-178

Kondo, S.

P05-098

Kusaka, Katsuhiro

P05-002

P05-099

Kusaka, Yoshitomo

P06-165

Kondo, T.

P05-088

Kusakabe, Yoshio

P06-161

Kongsaeree, Palangpon

P06-211
P06-216

Konno, MichikoP05-176

Konozy, Emadeldin H. E.

P05-130

Koo, J.

O2B05-A3

Koshihara, Shin-ya

O3C06-M3

O3C06-M4
P05-018

P06-162
Kusunoki, Masami

O5A07-M3
P06-227

Kwag, Gwanghoon
Kwo, J.

O1C05-M4
P06-045
P06-230

Lee, Yu-Hsuan

P06-057

Kwon, Myung-Hee

P06-201

Lai, Ying-Huang

O1C05-M5

Lefort, R.

O1C05-M6

Li, Chia-Lung

P05-174

P05-023

Li, Hsin-Tai

P06-207

P05-026

Li, Hsou-min

P05-130

Lai,, Yi-Ju

P06-195

Li, Yaw-Kuen

P06-208

Lal, Krishan

PL06-003

Li, Yi-Ching

P06-144

Latham, Catherine F.

O6A07-A1

Liang, Keng S.

O1C05-M6

Lawrence, Michael C.

P05-172

P05-021

Leartsakulpanich, Ubolsree

P06-211

P05-026

O4C06-A1

P06-216

Liao, Yen-Fa

P05-024

Lecomte, C.

P05-113

Liaw, Ben-Jie

P05-036

Lee, Beck-Sim

O2B05-A4

Lieu, Samantha

O3A06-M5

Lee, Chih-Hao

P05-024

Lii, Kwang-Hwa

PL07-005

Lee, Chi-Rung

P05-039

Lin, Chia-Her

P06-065

Lee, Chi-Shen

P05-103

Lin, Chih-Ming

P05-129

P05-104

Lin, Chun-Hung

P06-210

O4A06-A6

Lin, Hsiu-Mei

P05-039

P05-035

Lin, Jhih-Min

P05-026

P05-036

Lin, Te-Sheng

P06-209

P05-040

Lin, Tsang-Lang

P05-026

P06-056

Lin, Wei-Zeng

P06-056

P06-057

Lin, Y. C.

P05-113

P05-113

Lin, Yi-Hung

P06-204

Lee, Erinna F.
Lee, Gene-Hsiang

O2A05-A5

P06-205

Lee, J. F.

P06-230

P06-206

Lee, Jey Jau

P05-021

P06-207

Lee, Ji-Eun

P06-202

Lin, Yi-Tzu

P06-057

P06-203

Ling, Chris D.

P05-083

Lee, Hyung Ho

Lee, Ki Bong

O2B05-A3

Lee, Ming-Tao

P05-023

Liu, Chen-Wei

P05-036

P05-026

Liu, Chia-I

P05-179

Liu, Chien-Liang

P05-179

P05-106

Lee, Peter L.

O6C07-A2

Lee, Sang-Hak

P06-203

Liu, D.G.

P06-230

Lee, W. C.

P06-045

Liu, En-Hung

P06-206

P06-230

Liu, Hongqi

P06-167

Lee, Y. J.

P06-045

Liu, Jiango

P06-146

Lee, Y.-R.

O4C06-A4

Liu, Ming -Yih

P06-074

P06-069
P06-221

P06-204
Liu, Y. H.

P05-113

Liu, Y.-J.

P06-069

Matsugaki, Naohiro

P06-012

Liu, Yen-Ting

P05-129

Matsumura, Hiroyoshi

P05-177

Liu, Yen-Yi

P06-196

P05-178

Liu, Zhi-Jie

O1A05-M2

P05-181

Lo, Chaur-Tsuen

P06-206

Matsunaga, Atsushi

Lo, Li-ping

P06-210

Matsushita, Y.

P05-090

Lo, Y. Y.

O3B06-M6

Matsuura, Masato

O2B05-A5

Longtin, Joe

O4A06-A1

Matsuura, Toru

P05-020

López-Rubio, A.

O5B07-M1

McEwan, Alastair G.

P06-160

Lu, Tian-Huey

P05-114

McKinnon, Joshua J.

P05-187

Lu, Toh-Ming

O4C06-A3

McLain, Sylvia E.

P06-234

Lu, Tong-Bu

O4B06-A3

McNaughton, Don

P06-058

M.J., Swamy

O6A07-A3

Metoki, Naoto

O2B05-A1

Ma, CheO3A06-M5

Michael, Daliah

O1A05-M5

Macquart, Rene

P05-083

Mikhailova, D.

P06-047

Mae, TadahikoP05-178

Miki, Kunio

O2A05-A3

Maesaki, Ryoko

P06-214

O2A05-A7

Mahmudov, U.S.

P06-225

O5A07-M4

Makha, Mohamed

O4B06-A4

O6A07-A4

Makhmudov, Utkur

P06-228

P06-215Makino, Amane

P05-178

Mikouchi, Takashi

P05-110Makita, Ryoko

O2C05-A3

Milligan, Daniel

O4A06-A1

Mao, Qilong

P06-226

Mio, Toshiyuki

O5A07-M4

Mao, Simon JT

P06-074

Mir, Rafia

O4A06-A4

Marfori, Mary

O4A06-A3

O5A07-M1

Martin, Jennifer L

O6A07-A1

P06-150

O4A06-A3

P06-154

Martirosyan, Aida

P06-048

Maruyama, Daisuke

O5A07-M4

Maruyama, Koichi

P06-162

Masakiyo, KoichiP05-170

Mashima, Kazushi

P05-124

O3B06-M5

Mishra, P.

O5A07-M2

Mishra, Sanjay Kumar

O6C07-A4

Mitsumi, Minoru

O2C05-A1
O6B07-A6

Miyano, Masashi

P05-184

O1C05-M2

Miyano, Nao

P06-159

O1C05-M3

Miyano, Yousuke

O6B07-A6

Matin, Azadeh

P05-028

Miyazaki, Naoyuki

O2A05-A6

Matsubara, Mamoru

P06-158

Miyazono, Ken-ichi

P06-217

Matsuda, Seiichi

P05-087

Mizohata, Eiichi

P05-178

Matsuda, Tatsuma D.

O2B05-A1

Mizota, TadatoP05-096

Matsugaki, Naohiro

P05-125

Mizuki, Eiichi

P06-165

P06-011

Mizuno, Kazunori

P06-200

MASUNAGA, Hiroyasu

Mizushima, TsunehiroP06-192

Nakagawa, Taro

O2A05-A7

Mizushima, Tsunehiro

P06-220

Nakaguchi, Tomoko

Mochiku, Takashi

P05-101

Nakai, Hidetaka

O6B07-A6

Mohan, S.

P05-128

Nakaishi, Yuichiro

O2A05-A6

P05-137

Nakamura, Akira

O2A05-A3

P05-138

Nakamura, Kazuo T.

P05-111

P06-161

P05-140

P06-162

Moharram, A.H.

P05-014

P06-164

Monjusyo, Hatsumi

P05-182

Nakamura, Naotake

P05-118

Moreac, A.

O4C06-A1

Nakamura, Takahiro

P05-184

Morell, M.K.

O5B07-M1

Nakamura, Teruya

O6A07-A5

Mori, Hiroyuki

PL07-004

Mori, Kazuhiro

P05-003Mori, Takeharu

P05-092

Mori, Tomoyuki

P06-214Moriai, Atsushi

P05-001

P06-042Morii, Yukio

P05-001

P06-043

P06-168
Nakanishi, Masayuki

P06-161
P06-162

Nakanishi, Taiki

P06-041

P05-002

Nakaniwa, Tetsuko

P05-185

Morimoto, Tatsuya

P06-199

Nakao, Akiko

P06-041

Morimoto, Yukio

P06-215

P06-042
Nakatsuka, AkihikoP05-086

Morineau, D.

O4C06-A1

Morishima, T.

O5C07-M4

P05-094

P05-186

P05-096

Moritomo, Yutaka

O3C06-M4

P05-097

Moriyoshi, Chikako

P05-018

Mouradov, Dmitri

O4A06-A3

Mukhopadhyay, N.K.

P06-229

Nakayama, Toru

O5A07-M3

Mukoyama, Shota

P06-071

Namba, Kazunori

O2A05-A6

Müller, Jürgen J.

P05-171

Narukawa, T.

O1A05-M1

Murakami, Hironori

P06-010

Muraki, N.

P05-180

Murata, Takeshi

Nakayama, Noriaki

P05-096
P05-097

P05-188
Natarajan, S.

O3A06-M2

P05-115
P05-116

Murugan, Periyasamy

P05-114

Nayak, B.B.

Nagai, Minoru

P05-003

Nayak, Susanta K.

O4B06-A2

Nagata, Hiromitsu

P05-124

Neelagandan, K.

P05-171

Nagata, Koji

P06-217

Nemoto, Y.

P05-090

P06-079

Nahari, E Karimpour

O4C06-A6

Ngan, Pham-Hoang

P06-075

Nakabeppu, Yusaku

P06-168

Nguyen, Thanh Ha

P05-028

Nakagawa, Atsushi

O2A05-A6

Nakagawa, S. T.

P05-189

P05-029
Nho, Pham-Van

P06-075

Niimura, Nobuo

P05-002

Ohsumi, Kazumasa

P05-110Nimthong, Ruthairat

P05-037

Ohtaka, Osamu

P05-089

Nirmala, K.A.

P05-128

Ohtsu, Daisuke

P06-041

P05-134

P06-042

Nisawa, Atsushi

P06-008

P06-043

Nishibori, Eiji

O6C07-A1

Oikawa, Kenichi

P05-003

P05-030

Oikawa, Tadao

P06-223

P05-184

Oishi, Ryoko

P05-186

P05-186

Okada, Hironao

P05-096

Nishimaki, Yuichiro
Nishino, Tokuzo

O5A07-M3

Okada, K.

P05-099

Nishitani, Yuichi

O5A07-M4

Okamoto, Naoki

P05-181

Nithianantham, StanleyP06-167

Okano, Hiroyuki

P05-182

Noda, Isao

P06-071

Okano, Yousuke

P05-181

Noda, Takehiro

P06-068

Okazaki, Nobuo

P06-005

Noda, Yukio

O2B05-A1

P06-008

O3B06-M5

P06-010

Nogami, Yoshio

P05-020

Okazaki, Seiji

P06-192

Noguchi, Keiichi

P06-199

Okino, Nozomu

P05-182

P06-200

Okube, Maki

P05-086

Nonaka, Tsuyoshi

O5A07-M4

P05-089

Nozawa, Shunsuke

O3C06-M3

P05-092

Numoto, Nobutaka

O2A05-A7

P05-094

P06-142

P06-041

P06-143

P06-042

PL07-004

P06-043

Nuttall, Stewart

O2A05-A4

P06-044

Nyam-Ochir, L.

P06-047

OKUDA, Hiroshi

O1C05-M2

Oda, Takashi

P06-212

Okudera, Hiroki

P05-038

O6B07-A5

Okuhara, Shinichiro

P05-131

Ohba, Michio

P06-165

Okuyama, Daisuke

O2B05-A5

Ohba, Takuya

P06-080

Okuyama, KenjiP05-170

Ohhara, Takashi

P05-002

P06-199

Ohkawa, Makio

P05-097

P06-200

Ohkubo, Koichi

P05-033

Omata, Kenji

P06-053

Ohno, Atsuko

P05-030

Oo, Than Zaw

P05-121

P06-044

Oosuka, A.

O1A05-M1

Nureki, Osamu

Ogawa, Keiichiro

Ohsato, H.

O2B05-A6

Ohsawa, Seiji

P05-092

Ohshima, Ken-ichi

P06-219

Ohsumi, Hiroyuki

O2B05-A5

P05-188
Otsuka, Takuhiro

O2C05-A2
P05-111

Oya, Akihisa

P06-009

Puttaraja

P05-138

Ozaki, Takeshi

P06-227

Ozaki, Yukihiro

P06-071

Ozawa, Yoshiki

O2C05-A1

Qin, Lu-Chang

O4C06-A2

O2C05-A2

Rahman, M. S.

P05-085

O6B07-A6

Ramu, L.

O6B07-A2

Ozcan, Yusuf

O1C05-M6

Ramu, R.Chandramani

O4C06-A5

Ozeki, Tomoji

P05-002

Ranjan, Rajeev

O6C07-A4

Pakawatchai, Chaveng

P05-037

Ranjani, C.Vasuki

O1A05-M5

Pan, Kuan-Tin

P06-160

Rao, Zihe

O1A05-M2

Pan, Yi-Hsin

P06-208

Raston, Colin

O4B06-A4

Pandey, Dhananjai

O6C07-A4

P05-140

Ravikumar, Krishnan

P05-119

P05-017Ree, Moonhor

O1C05-M1

Pang, Pokka K-C.

P06-062

Reutter, WernerP06-146

Park, Joon Kyu

O4A06-A5

Robinson, Howard

O4A06-A2

Park, Suk-Yeol

P06-201

Robinson, R. A.

O5C07-M3

P06-203

Rosconi, Michael

O3A06-M1

Rose, John

O1A05-M4

Park, Y. J.
Parkin, Andrew

O2B05-A3
P06-067

O3C06-M2

P06-234

P05-191

P06-235

Roshan, M.N.A.Md.

O1A05-M5

Patil, P. S.

P05-117

Ross, Jonathan

P06-167

Peng, Kuo-Cheng

P06-206

Row, T. N. Guru

O4B06-A2

Peng, Ming-Sheng

O4A06-A2

P06-231

Peng, Shie-Ming

P06-082

P06-232

Peng, Wen-Yan

P06-204

Roy, Parag Sinchan

Perbandt, M.

P06-155

Roy, Siddhartha

O2A05-A1

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Saravanan, S.

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Shr, Hui-Lin

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Smith, Brian J.

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Taguchi, Takeyoshi

Studer, A.J.

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TAJIRI, Hiroo

P06-007
O1C05-M2

O1C05-M2

Tanaka, Yoshiki

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Tang, M.-T.

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