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International
Crystallography
Meetings

AsCA'03/Crystal-23
Joint conference of the
Asian Crystallographic Association and theSociety of Crystallographers in Australia and New Zealand

Biological Structure Workshop
Meeting of the IUCr Commission on
Biological Macromolecules

Sagamore XIV
Meeting of the IUCr Commission on
Charge, Spin and Momentum Densities

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Contents
Committees

5

Sponsors & Exhibitors

6

General Information

7

Program Timetable
AsCA'03/Crystal-23
MondayAugust 11
Tuesday
August12
VVednesday August13
Biological Structure Workshop
Thursday August14
FridayAugust 15
Sagamore XIV
Thursday August14
August15
FridayAugust16
Saturday
SundayAugust17
August 18
Monday

19
31
41
45
49
51
58
60
63
65

Abstracts
AsCA'03/Crystal-23

77

Biological Structure Workshop

283

Sagamore XIV

297

Ad hoc Workshop Programs

379

AUTHOR INDEX

385

3

4

Committees
Organising
Syd Hall (Chair)
Mitchell Guss
Trevor Hambley
Brian O'Connor
Brian SkeltonMark Spackman
Allan White
Matthew Wilce

AsCA/Crystal
Program

Sagamore XIV
Program

Mitchell Guss (Chair)
Jenny Martin (Co-chair BioWshop)
Mark Spackman (Chair Sagamore)
Matthew Wilce (Co-chair BioWshop)
Ted Baker
Yuji Ohashi
Allan WhiteM Vijayan
Brendan Kennedy
Yu Wanglan Williams

Mark Spackman (Chair)
Arun Bansil
Pierre Becker
Joanne Etheridge
Carlo Gatti
Heinz Graafsma
Arsen Gukasov
Bo Iversen
Dylan Jayatilaka
Wim Klooster
Claude Lecomte
Thomas Lippman
Seppo Manninen
Rob Robinson
John Spence
Francis Tasset
Erich Weigold
Jian-Min Zuo
5Sponsors & Exhibitors
International Union of Crystallography
Asian Crystallographic Association
Society of Crystallographers in Australia and New ZealandAustralian Synchrotron Projectmarresearch
Bruker Nonius
Rigaku/MSC
Oxford Cryosystems
CCP4
Fluidigm
PANalyticalJohn Morris Scientific
Moreton Bay Scientific
Meeco
Sietronics
Biolab Australia
Hampton ResearchDiscovery Partners International
deCODE genetics- BioStructures Group
Institute of Physics Publishing
Royal Society of Chemistry- CrystEngComm
Australian Synchrotron Research Program
Australian Nuclear Science & Technology Organisation
Protein Data Bank
Broome Aviation
Willie Creek Pearls
6General Information
Meeting Dates & Venue
Three international crystallography meetings will be held at theCable Beach Club resort in Broome from August 10-18 2003.
The joint conference AsCA'03/Crystal-23 of the Asian
Crystallographic Association and the Society of
Crystallographers in Australia and New Zealand will be held
as parallel sessions in the Sam Male rooms A and B at theCable Beach Club resort held from August 11-13.

0

The Biological Structure Workshop is held under the
auspices of the IUCr Commission on Biological
Macromolecules as a single session in the Sam Male room
A at the Cable Beach Club resort held from August 14-15.
The Sagamore XIV Meeting is held under the auspices of
the IUCr Commission on Charge, Spin and Momentum
Densities as a single session in the Sam Male room B at
the Cable Beach Club resort held from August 14-18.

The dates for the scientific sessions for all three meetings are
summarised below.
August 2003
10---'--------

11

12

13

14

15

16

17

18

AsCA/Crystal
Bio workshop
Sagamore XIV

Note: Detailed program timetables of the scientific sessions for each meetingare given in the respective program sections edged with these colours.

7Evening Functions
Bruker-Nonius Welcoming Reception (R)Sunday August 10th at 18:00
A social mixer will be held for AsCA'03/Crystal-23 registrants at theClub Pool. Music by the Steve Pigrim Trio.

marresearch Sunset Dinner (D)Wednesday August 13th at 18:00
The farewell dinner for AsCA'03/ Crystal-23 participants, and thewelcome to Bio Workshop and Sagamore XIV registrants, will beheld at the Cable Beach Amphitheatre. Music by Mick Manolis.

Rigaku/MSC Aussie Barbecue (B)Friday August 15th at 18:00
A barbecue will be held at the Kimberley BBQ at the Club Pool for
all Biological Workshop and Sagamore XIV registrants . Music by
Alana Pigrim and Calib.

Asian Buffet (A)Sunday August 17th at 18:00
A farewell Asian buffet dinner will be held at the Club Pool for all
registrants of the Sagamore XIV meeting .

The registrant entitlements for the evening social functions are
summarised below. Name badges will be required for entry into
each of these functions .
August 2003
AsCA/Crystal

10
R

11

12

13

14

15

16

17

D

Bio workshop

D

Sagamore XIV

D

8

B
B

A

18

Conference Office
The Conference Office for all three meetings is located at the CBC
room close to the Sam Male lecture rooms . It will be open in themornings from 9:00-12:00, August 11-15. For phone contact call9192 0400 (international 61 8 9192 0400) and the call will bedirected to the conference office .
Faxes should be sent to (61) 8 9192 3417.
For other enquiries contact a member of the organising committee(they have a red dot on their name tags).

Name Badges
Name badges are required for entry into all scientific sessions,lunches and evening functions .

Meals
Evening functions, lunches and mid-morning and poster
refreshments are part of the registration package for full, student
and accompanying members. Lunches are on the Sam Maleveranda from 13:00-13:45 from August 11-18. For other meals
see the information about places to eat at Cable Beach and in
Broome on page 10.

Medical and Emergency Contacts
The phone number for an urgent emergency in Australia is 000.
This will connect you immediately to POLICE , FIRE and MEDICAL
services. State the problem and your location clearly, andassistance will be sent immediately. This number should be used
ONLY for emergency help.
For the Broome Hospital call 9192 2222.
For non-emergency medical assistance contact:
Dakas Street Medical Centre and Pharmacy
Phone 9192 6311

9

Broome Medical Centre
Phone 9192 2022
AMCAL Pharmacy
Broome Boulevard Shopping Centre
Phone 9192 1866

Phone, Fax and Post
All communications for you sent to the conference hotel will be
posted on a Communications poster board at the entrance of the
Sam Male lecture halls. When you are phoning overseas numbers
from Australia remember to precede the country code with 0011 .
Broome's time zone is +8:00GMT. Here are the relative timedifferences for some cities when making phone calls .
Oh
London-7hSingaporeTokyo+1h
NewYork-12h
Sydney+2h
Chicago-13h-15hFrankfurt-6h
Los Angeles

Email and Internet
Email and Internet services are not available as part of theconference facilities. The phone jack in your hotel may be suitable
for a personal computer connection . Check if your hotel has abusiness centre for your use.

Banking and Currency Exchange
The Cable Beach Club resort reservation desk will exchange
currency and travellers cheques, and an ATM (automatic teller
machine) that accepts most credit cards is available in the gift
shop. Exchange facilities are available at banks in Broome.
Banking hours are usually between 10:00 and 16:00 Monday to
Friday only.
Most shops and restaurants in Broome will accept international
credit cards for payment.

10Restaurants
Beer & Satay Hut
Palms Resort, Walcott Street
Burgers , seafood , pizza and more, in outdoor garden setting. A fun place toeat, drink, and meet with friends. Tel: 9192 1898
Cafe Carlotta
Wood-fired pizzas and pasta (hosts: Charlotte and Mick)
Tel : 9192 7606
Charters Restaurant
Mangrove Hotel, Carnarvon Street
Full range menu in comfortable air conditioned setting with magnificent viewof Roebuck Bay.
Tel : 9192 1303
Club Restaurant
Cable Beach Club Resort
Award winning dining in elegant ambience , indoors or outdoors al fresco on
the boardwalk . Reservations essential. Tel : 9192 0411
Conti Bar & Bistro
Mercure Inn Continental Hotel, Weld Street
Breakfast lunch and dinner 7 days a week. Great value family dining . Tel :9192 1002
Kimberley BBQ
Cable Beach Club Resort
An Australian outdoors a Ia carte restaurant serving the best in local bushspecialties, including Kimberley beef, emu , crocodile and barramundi . Liveentertainment every evening . Call for reservations. Tel : 9192 0413
Lord Mac's
Cable Beach Club Resort
Breakfast, a Ia carte lunch and theme smorgasbord dinner 7 days a week.
The Saturday night seafood buffet is a local favourite.
Tel : 9192 0470
Matso's Cafe & Brewery
Hamersley Street
Open 7 days breakfast, lunch & dinner. Choose from a selection of coffees ,cakes, fresh juices, shakes and meals. Refresh yourself with a real beer,
brewed on site using time-honoured techniques or choose a fine wine . Sit
back on the verandah overlooking Roebuck Bay & watch "Broometime" go by.
Tel : 9193 5811
Noodlefish
Shop 216 Hammersley Street
Best Thai in town , sit on the verandah , have a private party for 12 in thegarden or take it away. It's BYO. All entrees under $10 and mains under $20 .
Open : Man-Sat 5.30pm-late. No credit cards ; No booking . Tel : 9192 5529
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Pure Steel Restaurant & Bar
Tropicana Inn, Robinson Street
Great value counter meals and Governor Bar. Friday night seafood buffet andSunday night carvery. Tel : 9192 1204
Sandbar and Grill
Cable Beach beachfront (close to the CBC)
Casual cafe w ith inexpensive food and drinks. Open 7 Days. No bookings .
Sheba Lane Garden Restaurant
Napier Terrace, Chinatown
Enjoy alfresco dining or airconditioned comfort for lunch and dinner.
Extensive menu ranging from Japanese, Thai dishes, Kimberley steak andfish to Chilli Mud Crab . Fully licensed. Open 7 Days. Tel : 9193 6036
The lcecreamery
Carnarvon Street, Chinatown
Specialising in homemade all natural ice creams, sundaes, smoothies , shakes
and juices. Open 7 days. Tel : 9193 5400
The Old Zoo Cafe
Challenor Drive, Cable BeachOpen for breakfast and lunch 7 days a week. Great sandwiches, cakes andcoffees in the tropical setting of the old Pearl Coast Zoological Gardens. Tel :9193 6200
The Tides Garden Restaurant
Mangrove Hotel, Carnarvon Street
Take in the panoramic views of Roebuck Bay while enjoying a scrumptious
meal , a hot coffee or an ice cold drink. The menu is extensive , fresh andsimply delicious. Open for lunch , Dinner, Coffee & Cake. 7 Days.
Tel : 91921303

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Tours & Attractions
With its exotic history, pearling industry and natural features , you'll find plentyof sights and attractions in and around Broome. Whether your interests lean
toward art and culture, history or exploring the great outdoors, there's
something for everyone.
Most of the attractions listed below are free and open to the public. Others
have specific open hours and may have an entry fee. Where phone numbers
are provided , it's a good idea to check ahead for hours and details.
The Shinju Matsuri Festival of the Pearl runs in the Broome township fromAug 15-24, and the Staircase to the Moon from Aug 12-15.
A visit to the Tour Office at the CBC (phone 9192 0417) , or the Visitor Centre
in the Broome (phone 9192 2222), is a good starting point for expert advice
and information on the sights and attractions. In addition to information, thestaff provide a booking service for all your needs.
Have fun and don't forget a relaxing sunset walk along Cable Beach!
ANASTASIA'S POOL
Located at Gantheaume Point and built by a former lighthouse keeper for his
wife, Anastasia, who was crippled with arthritis and found relief in the pool.
LIONS PIONEER PARK
Located at Town Beach (end of Robinson Street). This is a pleasant picnic
and recreation area, and a great spot to watch the Staircase to the Moon
August 12-15.
ART GALLERIES
Broome is home to a vast array of art galleries specialising in local andindigenous art.
BEAGLE BAY
Located 118 kms north of Broome, the Beagle Bay church was built byPallotine Monks with raw materials from the area and completed in 1918. Itfeatures a unique altar beautifully decorated with pearl shell. Visitors must
contact the office on arrival and a fee of $5 is charged for entry to thecommunity. Access is by 4WD only. Tours are available.
BEDFORD PARK
Situated overlooking beautiful Roebuck Bay on Hamersley Street is the site of
Broome's War Memorial. The park features an array of memorabilia , including
a replica of one of explorer William Dampier's sea chests and an old traincoach once used on a railway that connected the original jetty at Town Beach
to Chinatown.
BROOME BIRD OBSERVATORY
Located 18 kms from Broome on the shores of beautiful Roebuck Bay, visitors
will share the amazing story of Broome's migratory shorebirds from Siberia .
The North West is regarded as the most significant site in Australia for
shorebirds , as over 800 ,000 use the area annually. Self interpretive walks.
Phone 9193 5600.

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BROOME BREWERYBroome's first boutique brewery opened in 1997 and is situated in Matso's
Gallery. It is the only brewery in the Kimberley and the Brewhouse is always
open for viewing . Meals are served all day from 8am . Phone 9193 5811 .
BROOME CROCODILE PARK
The park is home to over 1500 dangerous salt water crocodiles as well asAustralian fresh water crocodiles, New Guinea freshwater crocodiles , SouthAmerican Caimans and American Alligators. Don't miss the afternoon feeding!
Phone 9193 7824 .
BROOME GOLF CLUBThe only 18 hole fully grassed course between Geraldton and Darwin! Opento the public. Hire clubs , club house facilities. Call 9192 2092 .
BROOME HISTORICAL SOCIETY MUSEUM
Definitely one of the best regional museums in Australia - a must see when
visiting! Features a display on pearling and a large collection of photographs
and files that piece together the fascinating history of Broome . Located in the
old Custom's House behind the Seaview Shopping Centre. Phone 9192 2075 .
BUCCANEER ROCK
Broome legend has it that Buccaneer explorer, William Dampier, came to thepresent town anchorage, landed a treasure chest of pirated pieces of eightand buried it at Buccaneer Rock. His ghost is said to be seen there on a misty
night with a lantern looking for the lost loot. A great legend but, alas , thetreasure seems only an often repeated myth . The Rock is located in Roebuck
Bay opposite the Mangrove Hotel.
CAPTAIN GREGORY'S HOUSE
Built in 1917 for Captain A. C. Gregory, who operated one of Broome's mostsuccessful pearling businesses. A fine example of early Broome architectureand has now been converted to an art gallery. Situated on the corner ofHamersley and Carnarvon Streets in the same grounds as Matso's Gallery
and Broome Brewery. Phone 9193 5811 .
CHINATOWN
Take a wander through the original commercial centre of Broome , which wasonce the bustling hub of pearl sheds , billiard saloons, entertainment houses
and Chinese eateries . Chinatown is now home to some of the worlds finest
pearl showrooms , along with a variety of retail outlets . Sidewalk cafes add asplash of colour to the pavements.
CHINESE CEMETERY
The resting place for members of Broome's Chinese community, situated on
Port Drive .
COURTHOUSE and COURTHOUSE MARKETS
Built in distinctive "Broomestyle" architecture, the courthouse was the original
Cable House, where the Broome end of the oceanic telegraph cableterminated . Browse through the gardens or visit the popular CourthouseMarkets held on Saturday mornings from 8am - 1pm all year. Located on thecorner of Frederick and Hamersley streets.
14

CULTURED PEARLING MONUMENT
Mr. Tokuichi Kuribayashi , originally from Nippon Pearl Company, Tokyo , Mr.
Hiroshi lwaki and Keith Francis Dureau from Pearl Prop. Ltd . were pioneers in
the cultured pearl industry in Broome . The three lifesize statues are now ondisplay on the grassed area of Carnarvon Street in Chinatown.
DAMPIER PENINSULAThe Dampier Peninsula is a unique area north of Broome featuring
spectacular red pindan cliffs , azure waters and an amazing variety of flora andfauna . Several Aboriginal communities offer bush tucker walks and mudcrabbing tours. Access is by 4WD only. A variety of day tours are available
from Broome- contact Broome Tourist Bureau for details.
DINOSAUR FOOTPRINTS
Dinosaur footprints over 120 million years old can be seen at Gantheaume
Point at very low tide . As the reef area is very fragile , care must be taken
when exploring this area . For the benefit of visitors , a plaster cast of the tracks
has been embedded at the top of the cliff.
DIVING
Beneath the sparkling tropical waters that surround Broome is a diverse
aquatic habitat that is fast developing a reputation as a unique diving
experience. Half day, full day and extended dive trips are available. Charters
are also available to the Rowley Shoals . Situated approximately 260
kilometres west of Broome on the edge of the Continental shelf, the Rowley
Shoals is one of the best diving areas in the world where the magnificent coralgardens , giant clams and large reef fish astound visitors . For a list of dive
operators contact the Broome Tourist Bureau.
FISHING
Broome waters boast an abundance of different varieties of fish including theelusive sailfish. Full , half day or extended fishing charters available andtournaments are held annually. For a list of fishing charter operators contact
the Broome Tourist Bureau .
FLYING BOAT WRECKS
These wrecks remain as evidence of the flying boats sunk by the Japanese
air raid on Broome during WWII. Located approximately 1 km offshore from
Town Beach and visible only on minus tides. Check with Broome Tourist
Bureau for tide times and viewing information.
GANTHEAUME POINT
Located approximately 6 km from town , this is a scenic area of red , craggy
cliffs providing a stark contrast to the azure water below. Dinosaur footprints
over 120 million years old can be seen here when tides are less than 1.5
metres. As the reef area is very fragile , care must be taken when exploring
this area . For the benefit of visitors a plaster cast of the tracks has been
embedded at the top of the cliff.
HARD HAT DIVER
This life size statue of the Hard Hat Pearl Diver adjacent to the Cultured
Pearling Monument in Chinatown , was erected in 1999 to pay tribute to the15role that the Hard Hat Diver played in establishing Broome as the centre of
the world's pearling industry in the early 1900's. These early Pearl Divers
came from diverse cultural backgrounds, and this resulted in Broome being
exempted from the White Australia Policy, making the town a pioneer ofmulticulturalism in Australia . Around 50 of these divers along with many of
their ancestors still reside in Broome today.
JAPANESE CEMETERY
A testimony to the perils of the early pearl diving and the final resting place ofover 900 pearl divers. Situated on Port Drive .
LIBRARY
Broome boasts a modern library situated in the Civic Centre gardens on
Hamersley Street. Visitors welcome to borrow books. Open hours:
Mon/Wed/Fri 10am-5pm; Tue/Thu 10am-7pm; Sat 9am-12noon ; Closed
Sunday.
MATSO'S GALLERY AND COFFEE HOUSE
Matso's Gallery houses the largest and most diverse collection of artwork in
the Kimberley. The Gallery has a wide range of Aboriginal art and artifacts
with artwork from all of the major art communities in the Western Desert. The
Coffee House serves a range of light meals and drink throughout the day from
Bam. A range of boutique beers is also available from the Broome Brewery
which is also located in Matso's Store . Phone 9193 5811.
PEARL SHOPS
As the home of some of the most precious pearls in the world , Broome has agood selection of pearl shops catering to all budgets .
PEARL LUGGERS
Experience more than 140 years of Broome's unique maritime heritage. Takean historical journey through the life and times of the pearl divers on two of
the last surviving perfectly restored pearl luggers. Brought to life through 1
hour guided tours. Phone 9192 2059.
PIONEER CEMETERY
Located at Lions Pioneer Park, near Town Beach . Resting place of some of
Broome's early settlers.
REDDELL BEACH
This spectacular stretch of beach is an ideal place to observe the red pindan
cliffs of Broome's peninsula coastline . Named after Captain Reddell , who wasmurdered by his mutinous crew in 1899. Great for swimming and picnicking .
Located 8 km from the town centre.
ROWLEY SHOALS
Situated approximately 260 kilometres west of Broome on the edge of theContinental shelf, Rowley Shoals is one of the best diving areas in the world
where the magnificent coral gardens , giant clams and large reef fish astound
visitors. Extended dive charters are available. For a list of dive operators
contact the Broome Tourist Bureau .

16THE SHELL HOUSE OF GUY STREETA museum and retailer of seashells , shell products and mother of pea rl .
Handcrafting of pearl shell carried ou t on the premises. Phone 9192 1423.
No entry fee .
STAIRCASE TO THE MOON (August 12-15)
This natural phenomenon is caused by a full moon rising over the exposed
mudflats of Roebuck Bay at extremely low tides , creating a beautiful optical
illusion of a sta ircase reaching to the moon. Great locations to view the
Staircase include the outdoor bar at th e Mangrove Hotel and Town Beach.
Staircase Markets take place during most sta ircase dates at Town Beach , andfeature a great selection of foods and crafts.
SUN PICTURES
A unique movie experience! Officia lly opened in 1916, it is believed to be th eoldest operating picture ga rd en in the world. Thi s indoor/outdoor theatre has
withstood the ravages of war, cyclones and king tid es. Housed in th e foyer isan excellent display of movie memorabilia . Taking in a movie under the stars
at Sun Pictures is a must do when visiting Broome ! Located in Chinatown .
Current movies are shown every night. Phone 9192 3738 .
TESLING TROPICAL FRUIT & MANGO WINE
An innovative new wine producer, Mango Wine of Broome has enjoyed rapid
expansion to meet the growing demand from locals and visitors ali ke, eager totantalise their palate with th e unique blend of succulent flavour contained
within the Kensington Pride Mango. Situated 19 km from Broome. Tastingavailable for small fee. Phone 9192 1433.
TOWN BEACH
Ideal rel axing picnic and swimming spot located at the end of Robinson
Street. Cafe facilities available . Also a great spot to watch the Staircase to theMoon and enjoy the Staircase Markets.
WILLIE CREEK PEARL FARM
Discover how some of the world's largest and most highly prized gems areproduced. Th e managers of th e pearl farm demonstrate the intricate processof cu ltured pearling , including live oyster seeding . Th ere is a great educational
demonstration for those interested in the pearling industry. Their showroom
houses an extensive display of locally handcrafted jewellery and loose pearls
for purchase at very competitive prices. Located 38 kms north of Broome .
Coach or self drive tours avai lable- times vary dependi ng on the season.
Phone 9193 6000 for tour tim es and deta ils. Bookings are essential.

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AsCA'03/Crystal-23 Program
August10
Sunday8:30

11Monday12
Tuesday

Plenary 1

Plenary 3

Plenary 2

Plenary 4

Coffee/Tea

Coffee/Tea

13
Wednesday

9:00
9:30

AWe1A

AWe1B

10:00
10:30

Coffee/Tea

11 :00

AMo1A

11 :30

AMo18

ATu1A

ATu18

AWe2A

AWe28

12:00
12:30

Lunch

Lunch

Lunch

13:00

------------------------------------

13:30
14:00
14:30

A

B

A

15:00

ASPW

TwinW

MSW

B

A

8

SCANZ

15:30
16:00

Plenary 5

Registration

16:30

Plenary 6

17:00
17:30

POSTERSPOSTERS

18:00
18:30
19:00
19:30
20:00
20:30
21 :00ASPW= Australian Synchrotron Project Workshop; TwinW= Twinning Workshop
MSW= Modulated Structures Workshop ; SCANZ =SCANZ General Meeting

19

20

Monday Aug 11

AsCA'03/Crystal-23
Plenary session
Chair: Mark Spackman
8:30

PL-1

COHERENT X-RAY DIFFRACTION FOR PHASING IN
CRYSTALLOGRAPHY

lan Robinson (Maslen 1987 Fellow)
Chair: Bill Du ax
9:30

PL-2

CONTROLLING THE VANDER WAALS INTERPLAY OF
FULLERENE C60

C. L. Raston , J. L. Atwood , L. J. Barbour, & M. W. Heaven
10:30

Coffee BreakOral session 1A: Nucleic acids and theirprotein complexes

Room A

Chair/Co-chair: Akio Takenaka , Adrienne Adams
Introduction : Adrienne Adams

11 :00
11:10

AMo1A-1

STRUCTURE OF T7 RNA POLYMERASE ELONGATIONCOMPLEX AT 2.9A RESOLUTION

Dmitry G. Vassylyev , Tahir H. Tahirov , Dmitry Temiakov,
Michael Anikin , Vsevolod Patlan , William T. McAllister,and Shigeyuki Yokoyama
11:40

AMo1A-2

CRYSTAL STRUCTURES OF THE REPLICATIONTERMINATION PROTEIN BOUND TO DNA REVEAL A
MODE OF POLAR REPLICATION FORK ARREST

J. P. Vivian , C. J. Porter, J. A. Wilce, and M. C. J. Wilce
12:00

AMo1A-3

TWO CRYSTAL STRUCTURES OF D(GICGAGAGC)SUGGEST THAT POTASSIUM IONS MEDIATE TO FORM
DNA OCTAPLEX WITH I-MOTIF OF GUANINE QUARTET

Jiro Kondo , Shun-ichi Umeda , Tomoko Sunami , and Akio
Takenaka
12:20

AMo1A-4

BACTERIAL OFFENSE AND DEFENSE MECHANISMS
USING NON-SPECIFIC ENDONUCLEASE$

Hanna S. Yuan , Chia Lung Li , Kuo-Chiang Hsia , and
Woei-Chyn Chu
12.40

AMo1A-5

STRUCTURE OF MYCOBACTERIUM TUBERCULOSISSINGLE-STRANDED DNA-BINDING PROTEIN .
VARIABILITY IN QUATERNARY STRUCTURE AND ITSIMPLICATIONS

K. Saikrishnan , J. Jeyakanthan , J. Venkatesh , N.
Acharya , K. Sekar, U. Varshney, and M. Vijayan
13:00

Lunch

21

AsCA'03/Crystal-23

Monday Aug 11

Oral session 1B: Structural chemistry

Room B

Chair/Co-chair: Colin Raston , Yu Wang
11 :00

AMo1 B-1

X-RAY ANALYSIS OF VARIOUS REACTION PATHWAYSOBSERVED FOR UNSTABLE NITRENES

Yuji Ohashi , Takahiro Mitsumori , Terufumi Takayama ,Hidehiro Uekusa, and Masaki Kawano
11 :30

AMo1 B-2

HYDROTHERMAL SYNTHESIS , CRYSTAL STRUCTURES,
AND SOLID STATE NMR SPECTROSCOPY OF METALSILICATES

Kwang-Hwa Lii
11:55

AMo1 B-3

POWDER NEUTRON DIFFRACTION STUDY OF
UNSATURATED THIOAMIDE DERIVATIVE

Takashi Ohhara, Susumu Ikeda , Kenichi Oikawa , Akinori
Hoshikawa, Takash i Kamiyama , Takaaki Hosoya, and Yuji
Ohashi12: 15

AMo 1B-4

PHASE TRANSITION OF DEHYDRATED CALCINED ALP0451NVESTIGATED BY IN-SITU SYNCHROTRON XRD

Hwo-Shuenn Sheu, Jey-Ja u Lee , Khin Win Ph yu , KueiJung Chao12.35

AMo1 B-5

COMPLEXES OF SIMPLE ALKALI METAL SALTS WITH N,N'AROMATIC BIDENTATE LIGANDS

Allan H. Wh ite, Jarrod N. Buttery, Effendy, George A.
Koutsantonis, Siti Mutrofin , Neil C. Placket!, Brian W.
Skelton , and Claire R. Whitaker
13:00

Lunch

14:00

Australian Synchrotron Project Workshop
Convener: Richard Garrett

14:00(see p380 for program)

Twinning Workshop
Convener: Victor Young

Room A

Room 8(see p381 for program)Oral session 2A : Computational biology and methods

Room A

Chair/Co-chair: Janet Smith, Brei Church
20:00

AMo2A-1

CADB : CONFORMATION ANGLES DATABASE OF PROTEINS

K. Sekar, G. Ramya Bhargavi , P. Ananthalakshmi , and S. S.
Sheik

22

Monday Aug 11

AsCA'03/Crystal-23
20:25

AMo2A-2

USING STRUCTURAL INFORMATION IN FUNCTIONALGENOMICS : IDENTIFICATION OF PROTEIN KINASE
SUBSTRATES

Bostj an Kobe , Robert A. Breinl , and Ross I. Brinkworth
20:45

AMo2A-3

CAN YOU PREDICT WHETHER A PROTEIN WILLCRYSTALLISE FROM THE PRIMARY SEQUENCE?

Adrian H. Batchelor
21:05

AMo2A-4

CYSTEINE DISTRIBUTION AND THE EVOLUTION OF SHORTCHAIN OXIDOREDUCTASE ENZYMES : COVARIANCE AND
DISULFIDE BOND POTENTIAL

W. L. Duax , V. Pletn ev, and R. Huether
21:30

Close

Oral session 28 : Supramolecular chemistry &crystal engineering

Room B

Chair/Co-chair: Peter Turn er, Yoshio Matsu i
20 :00AMo2 B- 1

THREE NOVEL POLYMERIC NETWORK OF COPPER(II)CONSTRUCTED WITH SUCCINATO LIGAND AND THE
INFLUENCES OF WEAK INTERACTIONS ON THEIR CRYSTALPACKINGTi an-Huey Lu , G. Mostafa, and N. Ray Chaudhu ri
20:30

AMo2 B-2

NEW BOROPHOSPHATES IN MAIN GROUP ELEMENT AI , Ga
AND In SYSTEMS : SYNTHESES AND STRUCTURES

J.-T. Zhao , and R. Kniep
20:50

AMo2 B-3

IN-SITU SINGLE CRYSTAL X-RAY DIFFRACTION STUDIES OF
GUEST-EXCHANGE IN NANOPOROUS FRAMEWORKMATERIALS

Gregory J. Halder, Cameron J. Kepert, Boujemaa Moubaraki,
Keith S. Murray, and John D. Cahsion
21:10

AMo2 B-4

CHANNELS IN 3-DIMENSIONAL COORDINATION POLYMERS :ZINC SACCHARATE AND LANTHANUM MUCATE

Michael Moylan, Bre ndan Abrahams , Simon Orchard , andRi chard Robson
21:30

Close

23

AsCA'03/Crystal-23

Monday Aug 11

Poster session 17:00-18:30
AMoP-01

VerandaEXPERIMENTAL CHARGE DENSITIES IN STRONGLY HYDROGENBONDED AROMATICS

Ross 0 . Piltz, David E. Hi bbs and Peter Williams
AMoP-02 A WAVEFUNCTION CONSTRAINED JOINTLY TO X-RAY AND POLARISED
NEUTRON DIFFRACTION DATA FOR THE Cs 3 CoCI 5 CRYSTAL

Dylan Jayatilaka
AMoP-0 3 USING THE HIRSHFELD SURFACE TO INVESTIGATE CRYSTAL PACKINGIN POLYMORPHS AND CRYSTALS WITH Z'>1

Joshua McKinnon , and Mark Spackman
AMoP-04 A NEW HYBRID MATERIAL WITH THREE DIMENSIONAL Na-0-Cu
CONNECTIVITY AND ITS NANOSTRUCTURES BY ANNEALING

G . Mostafa, Tian-Huey Lu, and N. Ray Chaudhuri
AMoP-05

PROTEIN CRYSTALLIZATION IN SPACE USING COUNTER-DIFFUSIONTECHNIQUE

Hiroaki Tanaka , Koji lnaka, Sachiko Takahashi, Satoshi Sano , Masaru
Sato , and Susumu Yosh itomi
AMoP-06

PROTEIN CRYSTAL GROWTH WITH STIRRING SOLUTION

Hiroaki Adachi , Kazufumi Takano, Masashi Yoshimura , Yusuke Mori,
and Takatomo Sasaki
AMoP-07

A STRUCTURAL STUDY ON THE POLYMORPH OF ICOSANE-1,20-DIOL

K. Uno, N. Nakamura, andY. Ogawa
AMoP-08

HYDROTHERMAL SYNTHESIS OF SINGLE-PHASE HYDROXYAPATITEWHISKERS AND CRYSTAL STRUCTURE CHARACTERISATION BY
HRTEM AND IMAGE SIMULATION

Z. L. Dong , and T. J. WhiteAMoP -09 THE EFFECT OF MIXED Mn VALENCES ON Li MIGRATION IN LiMn 2 0 4 :MOLECULAR DYNAMICS SIMULATIONS

Kenji Tateishi , Douglas du Boulay, and Nobuo lsh izawa
AMoP-10MECHANISM FOR PIEZOELECTRICITY OF LANGASITE CRYSTAL UNDERHIGH PRESSURE

N. Araki, T. lwataki , K. Kakimoto , H. Ohsato , T. Kuribayashi , Y. Kudoh ,and H. Morikoshi
AMoP-11

IMIDE-AMIDE BETWEEN KEMP'S ACID AND L-PROLINOL AND THE
HYDROGEN BONDING

M. Kawaminami , Y. Odo , T. Shimo , and K. Somekawa
AMoP-12STRUCTURE ANALYSIS BEFORE AND AFTER ACCELERATEDEXAMINATION FOR DETERIORATION OF BAM, BLUE PHOSPHOR

H. lmura, T. Honma , I. Hirosawa , Y. Shimomura , and N. Kijima
AMoP-13

CRYSTAL STRUCTURE OF A STREPTOCOCCAL SUPERANTIGEN , SPE-J

Heather M. Baker, Vickery L. Arcus, Thomas Prof!, Melissa Nicholson ,John D. Fraser, and Edward N. Baker

24

Monday Aug 11

AsCA'03/Crystal-23

AMoP-14 STRUCTURAL GENOMICS OF MOUSE MACROPHAGE PROTEINSNath an Cowieson , Pawel Listwan , Christine Wells , Thomas Huber,
Timothy Ravasi, Anna Aagaard , Bostjan Kobe, and Jenny Martin
AMoP-15

CRYSTALLOGRAPHIC STUDIES ON HEN SERUM TRANSFERRIN

Piyali Guha Thakurta , Debi Choud hu ry , Rakhi Dasgupta , and J. K.
Dattagupta
AMoP-16

BIOPHYSICAL STUDIES OF A NOVEL RNA BINDING PROTEIN

Corrine J. Porter, Lois A. Balmer, Peter J. Leedman , Matthew C. J.
Wilce , and Jackie A. Wilce
AMoP-17DETAILED STRUCTURE OF L-METHIONINE g-LYASE FROMPSEUDOMONAS PUT IDA BASED ON THE RESULT OF 1.8 A RESOLUTION
X-RAY CRYSTAL STRUCTURE DETERMINATION

Shintaro Misaki, Tomoaki Takakura , Takayuki Yoshioka , Robert M
Hofman , Shigeo Yag i, Kenji lnagaki , and Akio Takimoto
AMoP-18

THE EAFP CRYSTAL GROWTH OBSERVED BY ATOMIC FORCEMICROSCOPY

Sheng Wang, Ye Xiang , and Dacheng Wang
AMoP-19

CRYSTAL STRUCTURE OF ESCHERICHIA COLI ATASE N-TERMINALDOMAINYi bin Xu, Rongguang Zhang, Pau l D. Carr, and David L. Ollis
AMoP-20

1.7A AND 2.1A X-RAY STRUCTURES OF HEMOGLOBIN E AND
HEMOGLOBIN A2 , ISOLATED FROM THE BLOOD SAMPLES OF
THALASSEMIC PATIENTS

J. K. Dattagupta , Udayaditya Sen , Debi Choudhury, and Jhimli Dasgupta
AMoP-21

STRUCTURAL AND KINETIC IMPLICATIONS OF SUBSTRATE INHIBITION
IN THE HUMAN SULFOTRANSFERASE 1A1 ENZYME

Niranjali U. Gamage , Ronald G. Duggleby, Amanda C. Barnett, Michael
Tresillian , Catherin e F. Latham , Nancy E. Liyou , and Jennifer L. Martin
AMoP-22

SERA PROTEINS: ARE THEY CYSTEINE OR SERINE PROTEASES?

Robyn L. Malby , Anthony N. Hodder, and Brendan S. Crabb
AMoP-23

STRUCTURAL FEATURES OF MORACEAE LECTINS

AMoP-24

THE CRYSTAL STRUCTURE OF A NOVEL CALCIUM BINDING PROTEIN
ATCBL2 FROM ARABIDOPSIS THALIANA

K. Sekar, J. V. Pratap, A. A. Jeyaprakash , A. Surolia, and M. Vijayan

Masamichi Nagae , Akira Nozawa, Nozomu Koizumi , Hiroshi Sano,
Mamoru Sato, and Tosh iyuki Shimizu
AMoP-25

EXPRESSION , PURIFICATION AND CRYSTALLIZATION OF DEUTERATEDPROTEINS FOR NEUTRON DIFFRACTION

Kyoko Suto , Noritake Yasuoka ,and Hiroshi Mizuno
AMoP-26

CRYSTAL STRUCTURE OF FLINC4, AN INTRAMOLECULAR LM04:LDB1
COMPLEX

Janet E . Deane , Megan Maher, J. Mitchell Guss , and Jacqueline M.
Matthews

25

AsCA'03/Crystal-23
AMoP-27

Monday Aug 11

CATCHING CATALYSIS IN THE ACT : USING SINGLE CRYSTAL KINETICS
TO TRAP METHYLAMINE DEHYDROGENASE REACTION
INTERMEDIATES FOR STRUCTURAL STUDIES

Arwen R. Pearson , Teresa De Ia Mora Rey, Kevin T. Watts , Ed Hoeffner,and Ca rri e M. Wilmot
AMo P-28 AURACYANIN B STRUCTURE IN SPACE GROUP P6 5
Mihwa Lee, Megan J. Maher, Robert E. Blankenship, and Hans C.
Freeman
AMoP-29 THE STRUCTURE OF THE L YSYL OXIDASE FROM PICHIA PASTORIS- A
COPPER-CONTAINING AMINE OXIDASE THAT CAN OXIDISE LYSINECONTAINING PEPTIDES

Anth ony P. Duff, Pau l J. Ellis, Aina E. Cohen , Jason A. Kuchar, David
Langley, David M. Dooley, Hans C. Freeman , and J. Mitchell Guss
AMoP-30

INSECT CELL EXPRESSION OF A PLANT DISEASE RESISTANCE
PROTEIN CF-9 FOR STRUCTURAL STUDIES

T . Teh , S. Lang , and D. A. Jones
AMoP-31

THE COMPARISON OF THE LOOP STRUCTURES OF MEMBRANE
BINDING SITES BETWEEN HUMAN AND BOVINE ANNEXINS IV

Michiko Konno , Yae Kanzaki , Kayoko Mochizuki, Nahomi Fushinobu ,Ayano Sato , Kyoko Aikawa , and lsam u Matsumoto
AMoP-32 THE CRYSTAL STRUCTURE OF 9-AMINO-[N -(2-DIMETHYLAMINO)PROPYL]ACRIDINE-4-CARBOXAMIDE BOUND TO D(CGTACG)2 : A
COMPARISON OF STRUCTURES OF D(CGTACG)2 COMPLEXED WITH
INTERCALATORS IN THE PRESENCE OF COBALT

Adrienne Adams, J. Mitchell Guss , William A. Denny, and Laurence P. G.
Wakelin
AMoP-3 3 STRUCTURAL GENOMICS STUDIES OF MENAQUINONE BIOSYNTHESISPROTEINS FROM MYCOBACTERIUM TUBERCULOSIS : INSIGHTS FROMTHE STRUCTURES OF MENG AND MENB

J . M. Johnston , V. Arcus, and E. N. Baker
AMoP-34

CRYSTAL STRUCTURES OF RESTRICTION ENDONUCLEASE EC001091

Hi roshi Hash imoto, Tsuyoshi lmasaki, Matsuri Kato , Toshi yuki Shimuzu,
Mamoru Sato, and Keiko Kita
AMoP-35 CRYSTAL STRUCTURE OF THERMOSTABLE END0-1 ,5--L-ARABINASE
FROM BACILLUS THERMODENITRIFICANS TS-3

Asako Yamaguchi , Toshiji Tada, Tetsuko Nakaniwa , Makoto Takao ,Takuo Sakai , and Keiichiro Nishimura
AMoP-36

STRUCTURAL BASIS OF LIPID BINDING IN RICE NON-SPECIFIC LIPID
TRANSFER PROTEIN COMPLEXES

Yuh-Ju Sun , Hui-Chun Cheng , Peiyu Peng , and Ping-C hiang Lyu
AMoP-37

REFINEMENT OF THE 7/2-AND 10/3-HELICAL STRUCTURES BASED ON
THE FIBER DIFFRACTION PATTERN FROM NATIVE COLLAGEN

K. Okuyama , X. Xu , and K. Noguchi

26

Monday Aug 11

AsCA'03/Crystal-23
AMoP-38

INTERSUBUNIT SALT BRIDGES AND OLIGOMERIZATION DO NOTCONTRIBUTE TO THE HIGH THERMAL STABILITY OF A
HYPERTHERMOPHILIC PROTEIN FROM PYROCOCCUS FURIOSUS

Jai K. Kaush ik, Yuriko Ya magata , Kyoko Ogasahara , and Katsu hide
Yutan i
AMoP-39

STRUCTURAL CHARACTERISATION OF THE INI OPERON OF
MYCOBACTERIUM TUBERCULOSIS

J. Shaun Lott, Moyra M. Ko men, Tet Ve rn e Lee, Clare Scott, Joel
McKay , Edwa rd N. Baker, and Vicke ry L. Arcus
AMoP-40STUDIES OF PROTEINS OF THE FOLATE BIOSYNTHESIS PATHWAY

Jacque line F. Satche ll , Bria n J. Smith, Jonathan Baell , and Peter M.
Colma nAMo P-4 1 IDENTIFYING ANTAGONISTS TOWARDS A G-PROTEIN COUPLED
RECEPTOR USING THE STRUCTURE OF A HORMONE COMPLEXED TO A
NEUTRALISING MONOCLONAL ANTIBODY

Patricia W . M. Ho , Cra ig J. Morton , Ko h Sato , Etsu ro Onuma , Matthew T.
Gillespie , T . John Martin , and Michael W. Parker
AMo P-42

RECENT DEVELOPMENTS AT ASRP X-RAY DIFFRACTION FACILITIESJames R Hester, and David Cookson
AMo P-43

COMPARISON OF THE FR-E AND RU-H2R X-RAY SOURCES FOR
PROTEIN CRYSTALLOGRAPHY APPLICATIONS

Ka rl A. Byri el , An na Aagaa rd, Christine L. Gee , Nirajali Gamage , andJennife r L. Ma rtin
AMo P-44

EVALUATION OF MICROSTRUCTURE PARAMETERS FROM POWDER XRAY DIFFRACTION DATA

Takashi Ida, and Hideo Toraya
AMo P-45

THEORETICAL AND EXPERIMENTAL STUDY OF THE NEWEST HIGH
BRILLIANCE ROTATING ANODE GENERATORS AND CMF OPTICS

K. F. Tesh, A. R. Criswell , C. Yang , D. A. Courv ille, J. D. Ferrara, M.
Kuri bayashi , B. Ve rm an , and L Jiang
A MoP-46

PHASE TRANSITION OF LANTHANUM TITANATE PEROVSKITES

Masato mo Yashima, Mizuki Mori, Ko h Sa itoh, Kenj i Tsuda , Takashi
Ka miya ma, Ken-ichi O ikawa , A kin ori Hoshikawa , Shuki Torii , Masa hiko
Tanaka , Takeharu Mori, Ke n-ichi Kato, Shinobu Aoyag i, Masaki Takata,an d Eiji Nishibori
AMo P-47

PRECISE MEASUREMENT OF THE LATTICE SPACING OF LaB 6
STANDARD BY POWDER DIFFRACTION AND THE X-RAY EXTENDED
RANGE TECHNIQUE USING SYNCHROTRON RADIATION

AMoP-48ANALYSIS OF THE DEPTH DEPENDENCE ON THE POLY -CRYSTALSTRUCTURE NEAR THE SURFACE BY THE USE OF SCATTERED X-RAY
AT SMALL GLANCING ANGLE INCIDENCE

C. T . C hantler, Z. Barnea , C. Q. Tran, and D. J. Cookson

Y. Fujii , A. Tao , T . Ko mai, and K. Ikeda

27

AsCA'03/Crystal-23

Monday Aug 11

A Mo P-49

THE USE OF PARENT SYMMETRY TO IDENTIFY SPACE GROUP OPTIONSFOR TWINNED/DISORDERED PSEUDO SYMMETRIC CRYSTALSTRUCTURES
A. David Rae

AMoP-50PHASE TRANSITION AND STRUCTURE OF C8 H20 NXn.nCH 4 N2S (X=I , Br, Cl ,n=2, 4, 5)
H . lshiga m i, M . Sumita , Y . Tsun as hima , S. Sato , M. Shi ro, an d T . Hikita

A M o P-5 1 TRANSMISSION ELECTRON MICROSCOPE STUDY OF
RuSr 2Gd, _5 Ce 0.5 Cu 2 0 10., MAGNETO-SUPERCONDUCTORYosh io Matsui , Tadah iro Yokosawa , Vee r Pa l Sing h Awana , Koj i Ki m oto ,Eij i Takayama-Mu romachi , Maarit Ka rppi nen , and Hisao Yamauchi
AMoP-52

X-RAY DIFFRACTION STUDY ON THE PHASE TRANSITIONS OF BaTi0 3
SINGLE CRYSTAL
Y . Yos himura , N . Tokunaga , H . Iwasa ki , A. Koji ma , H . Sasou, an d K.
T ozaki

AMoP-53

ALKALI METAL COMPLEXES OF AROMATIC POL YCARBOXYLATES - A
BALANCE OF PI -STACKING AND COORDINATE BONDING
INTERACTIONS?
G. A. Ko utsa nto nis , S. Burn et, A.K. Ha ll , J.M. Ha rrowfield , V. Sanford , D.
Sauter, B.W. Skelton, and A .H. W hite

AMoP-54COMPLEX COINAGE METAL(I) THIOSULFATES
E. J. C han , B. W. Skelto n , and A. H . WhiteAMoP-55

STRUCTURE DETERMINATION OF ADDUCTS OF LEAD(II) IODIDE WITH
N-METHYL SUBSTITUTED ETHYLENEDIAMINE AT LOW AND ROOMTEMPERATURES (123, 209 AND 295 K)
Hi ros hi Miya m ae , Ko uich irou En o moto , Youhei Ma ruyama, and Goro
Hiha raAMo P-56

UNEXPECTED PIPERAZINE DERIVATIVE LIGANDS FROM A MIXTURE OF
CuC ,2.2H20 , Na2C0 3, AND TRIETHYLENETETRAMINE TETRAHYDRO CHLORIDE
N orih iro Ta mura , Masato Saka i, Katsuya Kudoh , a nd Hiroshi Miyamae

AMo P-57

ANALYSIS OF PHASE TRANSITION MECHANISM OF ACYLUREADERIVATIVE CRYSTAL BY A DETAILED TEMPERATURE RESOLVED
MEASUREMENT OF POWDER X-RAY DIFFRACTION
D aisuke Hashizume , Masaru Ogawa, Yasuhi ro limura , Masa nori Yasu i,
Eiji Nishi bori, Masaki Ta kata , and Fuji ko Iwasaki

AMoP-58

OBSERVATION OF THE PHOTO -EXCITED STRUCTURE OF PLATINUMCOMPLEXES
N obuhiro Yasuda, Hidehiro Uekusa , and Yuji Ohashi

AMoP-59DISORDER IN STRUCTURAL CRYSTALLOGRAPHY
S. Ba ne rj ee, a nd A. K. Mu kherjee

AMoP-60

NOVEL CRYSTAL STRUCTURES OF VANADYL GALLOPHOSPHATES
S ue-Lein Wang

28

Monday Aug 11

AsCA'03/Crystal-23
AMoP-61

ON THE DIELECTRIC CONSTANT OF Ba s-3xRa+2xTi,aOs•(R=Sm ,Nd) SOLID
SOLUTIONS : CRYSTAL STRUCTURAL ANALYSIS
H . Sakashita , H. Ohsato , N . Araki , a nd K. Kakimoto

AMoP-62

DEUTERIUM TRANSFER MECHANISM IN CHIRAL THIOLACTAMFORMATION BY NEUTRON DIFFRACTION MEASUREMENT USING BIX-111
DIFFRACTOMETER
Takaaki Hosoya , Hidehi ro Uekusa , Yuji Ohashi , Takashi Ohhara , lc hiro
Tanaka , and Nobuo Niimura

AMoP-63

STRUCTURE OF THE PSEUDORHOMBOHEDRAL lnFe,_xTi x0 3+x12
COMPOSITE CRYSTAL
Yuich i Michiue , Mitsuko Onoda , Francisco Brown , Noboru Kimizuka , andMamoru Watanabe

AMoP-64

USING THE HREM TO STUDY MORPHOLOGY AND STRUCTURE OF
NANOMATERIAL Ta AND TaN x
Vo Vong , Luu lien Hung , Steffen Schulze , and Michael Hietsc hold

AMoP-65

STRUCTURE-BASED DESIGN OF ANTI-INFLAMMATORY AGENTS :CRYSTAL STRUCTURE OF A COMPLEX FORMED BETWEEN COBRAVENOM PHOSPHOLIPASE A2 AND A DESIGNED POTENT PEPTIDEINHIBITOR VAL-ALA-PHE-ARG -SER- (VAFRS) AT 1.9 A RESOLUTION .
R. K. Singh , J . Makker, P. Vikram , M. Paramsivam , T . Jabeen, S.
Sharma , S. Dey, P. Kaur , A. Srinivasan , and T. P. Singh

29

30

Tuesday Aug 12

AsCA'OJ/Crystal-23
Plenary session
Cha ir: Brendan Kennedy
8:30

PL-3

ULTRA-HIGH SPEED NEUTRON DIFFRACTION STUDIES :COMBUSTION SYNTHESIS OF TI3SIC2 AND RELATEDCOMPOUNDS
Erich H. Kisi , and Daniel P. Riley

Chair: Yuji Ohashi
9:30

PL-4

ELECTRON MICROSCOPY TECHNIQUES : MICROSCOPY ,DIFFRACTION AND SPECTROSCOPY
Michiyoshi Tanaka

10 :30Coffee BreakOral session 1A: Enzyme structure, function & catalysis
Room A
Chair/Co-chair: Jose Varghese , Jenny Martin
11:00

ATu1A-1

CATALYSIS AND ALLOSTERIC REGULATION IN
PHOSPHORIBOSYL DIPHOSPHATE SYNTHASE ; THE
ROLE OF TWO MAGNESIUM IONS
Sine Larsen , and Frank B. Nygaard

11:30

ATu1A-2

ENZYMES OF RIBOSE METABOLISM: STRUCTURE AND
MECHANISM
Sherry L. Mowbray , C. Evalena Andersson , Annette
Roos, and T. Alwyn Jones

11:55

ATu1A-3

CRYSTAL STRUCTURE OF TWO KNOTTED PROTEINS :ACETOHYDROXY ACID ISOMEROREDUCTASE ANDtRNA(m1G37)METHYL TRANSFERASE
Se Won Suh , Hyung Jun Ahn , Jin Kuk Yang , Byung II
Lee , and Hye-Jin Yoon

12:20

ATu1A-4

SUPEROXIDE DISMUTASES FROM
HYPERTHERMOPHILES
Geoffrey B. Jameson , Julian J. Adams , Paul D.
Hempstead , James W. Whittaker, Edward N. Baker, andBryan F. Anderson

12.40

ATu1A-5

X-RAY ANALYSES OF FAMILY 8 CHITOSANASE FROMBACILLUS SP. K17
Wataru Adachi , Shinji Shimizu , Tomoko Sunami , Tesuya
Fukazawa , Mamie Suzuki, Rie Yatsunami, Satoshi
Nakamura , and Ak io Takenaka

13:00

Lun ch31

AsCA'03/Crystal-23

Tuesday Aug 12

Oral session 1 B: Synchrotron and neutron science

Room BCha ir/Co-cha ir: Brendan Kennedy, Y. Kubota
11 :00ATu1 B-1

EXPERIMENTAL SYSTEM FOR X-RAY MAGNETIC
DIFFRACTION UNDER EXTREME CONDITIONS

Etsuo Arakawa , Masahisa Ito, Naoki lshimatsu , Motohiro
Suzuki, Naomi Kawamura, Hiroshi Sakurai, Fumitake ltoh ,Yoshiya Honma , Aki ra Ochiai , Yuichi Akahama , Kazuyuki
Matsuda , Yoh Kohori, Shunji Kishimoto , Keiichi Hirano ,Hiroshi Maruyama , Kazumichi , Namikawa and Osamu
Shimomura
11 :30ATu 1B-2

ELECTRONIC DIPOLE-MOMENT OF HYDROGEN ATOM IN
A HYDROGEN-BOND STUDIED BY X-RAY AND NEUTRON

Yukio Noda , Ryoji Kiyanagi , Masashi Watanabe , Hiroyuki
Kimura , Akiko Kojima , Tomoyuki Mochida , and Tadashi
Sugawara
11 :50ATu1B-3

THREE-BEAM DIFFRACTION ANOMALOUS FINESTRUCTURE OF GALLIUM ARSENIDE

Shih-Li n Chang , Yen-Ru Lee , Yu. P. Stetsko , Sen-Yuan
Cheng ,Guin-Gi Lin and Wen-Shien Sun
12:10

ATu1B-4

THE NEW QUASI -LAUE DIFFRACTOMETER AT THE
REPLACEMENT RESEARCH REACTOR

12.30

ATu1B-5

VALENCE AND STRUCTURAL PHASE TRANSITIONS IN
THE SERIES Ba 2 PrRu 1 .,1r,0 6

Wim T. Klooster

Brendan J. Kennedy , Leqing Li, Christopher J. Howard
and Brett A. Hunter
13:00

Lunch

14:00

Modulated Structures Workshop
Convener: Siegbert Schm id(see p382 for program)

32

Room AAsCA'03/Crystal-23

Tuesday Aug 12

Oral session 2A: Structural genomics

Room A

Cha ir/Co-cha ir: Ted Baker, Bostian Kobe
20:00

ATu2A- 1

STRUCTURE OF THE PUTATIVE ANTITERMINATORPROTEIN RV1626 FROM MYCOBACTERIUM TUBERCULOSIS
J . P. Marth, V. Feng , L. J. Perry , and P. A. Tucker

20:20

ATu2A-2

STRUCTURAL STUDIES OF LATEXIN , A NOVELCARBOXYPEPTIDASE INHIBITOR
Anna Aagaa rd , Pawel Li stwan , Nathan Cowieson , Thomas
Huber, Christine Wells , T imothy Ravasi , Bostjan Kobe , andJennifer Martin

20:40

ATu 2A-3

CRYSTAL STRUCTURE OF AN ANCIENT CONSERVED
DOMAINJ . Shaun Lott, Ma rk J. Banfield , Jill Sigrell , and Edward N.
Baker

21 :00

ATu2A-4

RIKEN STRUCTURAL GENOMICSIPROTEOMICS INITIATIVE
S . Yokoyama

2 1:30C loseOral session 28 : Modulation, disorder & twinning

Room BCha ir/Co-chair: Victor Young , Siegbert Schmid
20 :00ATu2 B-1

DETERMINATION AND REFINEMENT OF A DISORDERED
HOST-GUEST CRYSTAL STRUCTURE USING AN
EVOLUTIONARY ALGORITHM IN COMBINATION WITH
MONTE CARLO METHODS
H .-B . Burgi , and T . Weber

20:30

ATu2B-2

THE IMPORTANCE OF MULTISITE CORRELATIONS INDISORDERED STRUCTURES
T . R. We lberry, and R. L . W ithers

20 :50ATu 2B-3

STRUCTURE SOLUTION AND REFINEMENT OF KNbOB 20 5
A COMMENSURATE MODULATED STRUCTURE
Siegbert Schmid

21:10

ATu2B-4

APPLICATION OF A SIX-DIMENSIONAL TWIN
REFINEMENT TECHNIQUE TO MULTIPLE-TWINNEDCRYSTALS OF Cu 2 Sn 23 , Cu 8 GeS 6 AND Ag 7Ta 6
M .Onoda , H.Wada , X .-a. C hen , A. Sato , and M. Ishii

21:30

C lose33

AsCA'03/Crystal-23

Tuesday Aug 12

Poster session 17:00 - 18:30
ATuP-01

VerandaELECTRON MOMENTUM DENSITY STUDY OF ICOSAHEDRAL Cd 84 Yb 16

Y . Sakurai, J. T. Okada , Y. Wata nabe , S. Nanao , R. Tamura, S.
T akeuchi , Y. Yokoya ma, N. Hiraoka, and M. ltou

=2 MOLECULES . POSSIBILITIESATuP-02

CHARGE DENSITY STUDIES OF Z'
AND LIMITATIONSATuP-03

CRYSTAL EXPLORER: A GRAPHICAL USER INTERFACE FORDISPLAYING AND MANIPULATING HIRSHFELD SURFACES AND
FINGERPRINTS FOR CRYSTAL ENGINEERING APPLICATIONSATuP -04

CRYSTALLIZATION OF SECRETED PROTEIN BY COMPLEXATIONWITH AN ANTIBODY FRAGMENT

Dai Hibbs, Mark P. Wall er, and Jacob Overgaa rd

Dylan Jayatil aka, Daniel Grimwood , and Stephen Wolff

Taro Tamada, Keiko Kurosawa , Uichi Nishiya ma, Tomoaki Kuwaki,
and Ryota Kuroki
ATuP-05

CRYSTALLIZATION OF ALPHA-AMYLASE AS A MODEL PROTEIN FOR
DEMONSTRATING THE EFFICACY OF THE COUNTER-DIFFUSIONTECHNIQUE UNDER MICROGRAVITY CONDITIONS

Masa ru Sato, Hiroaki Tanaka, Koji lnaka , Sachiko Takahashi , Satoshi
Sano, Susumu Yoshitomi , and Hiroshi Komatsu
ATuP-06

INVESTIGATION OF CRYOPROTECTANT CONDITION FOR PROTEINSTRUCTURE ANALYSIS USING CRYOPROTECTANT DATABASE

Sachiko Taka hashi , Takashi Yoshimine , Masa ru Sato, Hiroaki
Tanaka, Kensaku Hamada , and Susumu Yoshitom i
ATuP-07

CRYSTAL STRUCTURE OF NONADECANE-1 ,19-DITHIOL

H. Sh imizu, K. Uno, Y. Ogawa , and N. Nakamura
ATuP-08

A STRUCTURAL STUDY ON THE MONOSUBSTITUTED FERROCENEDERIVATIVES

Y. Kawam ura, Y. Okada , K. Uno , and N. Nakam ura
ATuP -09

CRYSTAL STRUCTURE OF Te 0 .4 Se 0 .6

Yuji Soeji ma , Akie Hoshiko, Hirotoshi Hayashid a, Yoshi nori Ohmasa ,Hiro hisa Endo , and Masaru Kawa minami
ATuP -10

CRYSTAL STRUCTURES OF A BISAZOMETHINE DYE FORMING JAGGREGATES

Shinya Matsumoto, Kazuko Shirai, Kimiko Kobayashi , Tatsuo Wada ,and Motoo Shiro
ATuP -11

STRUCTURAL STUDY OF STRESS -INDUCED LUMINESCENTPARTICLE SrAI 2 0 4 :Eu

Hiroshi Yamada , Hajime Ku saba, Weng-Shen Shi , Keiko Nishikubo,
and Chao-Nan Xu
ATuP-12POSITIONS OF La AND Ba OF BaLa4 Ti 4 0 15 HOMOLOGOUS
COMPOUND

H. Ohsato, Y. Tohdo , K. Kaki moto, T. Okawa, and H. Okabe

34

AsCA'03/Crystal-23
ATuP-13

Tuesday Aug 12

RELATIONSHIPS BETWEEN RUTILE STRUCTURES

Christopher J. Howard, Zhaoming Zhang, and Brendan J. Kennedy
ATuP-14

STRUCTURAL STUDIES ON JACALIN CARBOHYDRATE COMPLEXES

K. Sekar, A. A. Jeyaprakash, P. G. Rani , S. Katiyar, A. Surolia , and
M. Vijayan
ATuP-15PRESENT STATUS OF PHARMACEUTICAL INDUSTRY BEAMLINE AT
SPRING-S

Shintaro Misaki , Kenji Suzuki , Yoshio Katsuya , and Kazumi Nishijima
ATuP -16

REFINEMENT OF THE CRYSTALLIZATION CONDITIONS OF CONGER
EEL GALECTIN , CONGERIN I AND II

Takashi Yamane, Atsuo Suzuki , Yumiko Miyabe , Yuusuke Niwa ,Tomohisa Ogawa , Koji Muramoto , and Mitsuo Ataka
ATuP-17

NEUTRON PROTEIN CRYSTALLOGRAPHY OF CUBIC INSULIN

M. Maeda , T. Chatake , I. Tanaka , A . Ostermann , and N. Niimura
ATuP-18

PREPARATION , CHARACTERIZATION AND CRYSTALLIZATION OF
THE COMPLEX COMPOSED OF GRANULOCYTO COLONYSTIMULATING FACTOR AND ITS RECEPTOR

Eijiro Honjo , Shouhei Mine , Takumi Kosh iba, Tomoyuki Okamoto ,Taro Tamada , Yoshitake Maeda , Yasuko Matsukura , Akane Horie,
Matsujiro Ishibashi , Miharu Sato , Mizue Azuma , Masao Tokunaga ,Katsutoshi Nitta , and Ryota Ku roki
ATuP-19

CRYSTAL STRUCTURE OF DSBG A DISULFIDE BOND ISOMERASEFROM ESCHERICHIA COLI

Begona Heras , Melissa A. Edeling , Jennifer L Martin , and Salish
Raina
ATuP-20

PROTEIN MODEL BUILDING USING IMAGE PROCESSING TECHNIQUE
AND OPTIMIZATION ALGORITHMS

ATuP-21

CRYSTAL STRUCTURE OF TBP-INTERACTING PROTEIN (TK-TIP26)
FROM HYPERTHERMOPHILIC ARCHAEON THERMOCOCCUS
KODAKARAENSIS STRAIN KOD1

Osamu Takahashi , and Shigenobu Kobayashi

T. Yamamoto , T. Matsud a, H. Matsumu ra, T. Inoue, M. Morikawa , S.
Kanaya , and Y. Kai
ATuP-22

TOWARDS A MORE USABLE PROTEIN STRUCTURE DATABASE

W. Bret Church, William M. Shui , Stephen C. Graham, Lawrence K.
Lee , and Raymond K. Wong

ATuP-23DATA BASE OF HYDROGEN AND HYDRATION IN PROTEINS

N. Ni imura
ATuP-24

E. COLI DIHYDROOROTASE : STRUCTURE OF THE ENZYMECRYSTALLISED IN THE PRESENCE OF DIHYDROOROTATE. THE
POSSIBILITY OF COOPERATIVITY BETWEEN SUBUNITS?

Mihwa Lee , J. Mitchell Guss, Richard I. Christopherson , and Megan J.
Maher

35

Tuesday Aug 12

AsCA'03/Crystal-23
ATuP-25

THE CRYSTAL STRUCTURE OF RUBREDOXIN FROMDESULFOVIBRIO GIGAS AT ULTRA-HIGH 0.68 A RESOLUTION

ATuP-26

TUMOUR PEPTIDE PRESENTATION BY MHC CLASS I

Chun-Jung Chen , Yi-Ting Chen , Ming-Yih Liu , and Jea n Le Gall
Michelle A. Dunstone , Andrew Z. Webb, Anthony W. Purcel l, andJamie Rossjohn
ATuP-27

THE CRYSTAL STRUCTURE OF A CORAL POCILLOPORIN

Pasca l G. Wilmann , Travis Beddoe , Mark Prescott, Michael Ling ,Aaron J. Oakley, Sophie Dove , and Rodney J. Devenish
ATuP-28

STRUCTURAL CHARACTERISATION OF MITOCHONDRIAL IMPORTRECEPTORS

Travis Beddoe , Pascal Wilmann , Simon Bushell , Judy Scobie , Diana
Macasev , and Trevor Lithgow
ATuP-29

MHC CLASS I PEPTIDE PRESENTATION A STRUCTURAL INSIGHT

L. K. Ely, W. A. MacDonald , C. S. Clements , A. G. Brooks , A. Purce ll ,J. McCluskey, and J. Ro ssjohn
ATuP-30

THE CRYSTALLIZATION AND X-RAY DIFFRACTION OF THE
HALOACID DEHALOGENASE DEHIVA FROM THE SOIL BORNE
BACTERIUM BURKHOLDARIA CEPACIA MBA4

Jason W. Schmidberger, Matthew C. J. Wilce , Aaron J. Oakley , andColin A. Th ompson
ATuP-31

TRYPTOPHAN BIOSYNTHESIS IN MYCOBACTERIUM TUBERCULOSIS

J. Shaun Lott, Anthony J. Harrison , Emily Parker, Rochelle J.
Ramsay, and Edwa rd N. Baker
ATuP-32

UNDERSTANDING THE FUNCTIONING OF THE COPPER BINDING
DOMAIN OF THE AMYLOID PRECURSOR PROTEIN

G. K. W. Kong , W. J. McKinstry, J. J. Adams, G. Polekhina , N. A.
Williamson , D. Cappai , K. J. Barnham , R. Cappa i, and M. W. Parker
ATuP-33

CRYSTALLOGRAPHIC STUDIES OF THE MITOCHONDRIAL FISSIONPROTEIN FIS1

Michael A. Gorman , Diana Stojanovski, Michael T.Ryan , andJacqueline M. Gulbis
ATuP-34

THE CRYSTAL STRUCTURE OF T84.66FAB AT 2.2 A RESOLUTION
AND MODELLING THE BINDING OF ANTI-CEA ANTIBODYCONSTRUCTS TO THE CEA ANTIGEN

Jennifer A. Carmichael , Barbara Power, Albert van Donkelaar, Mark
Sherman , Paul Yazaki , Anna M. Wu , and Peter J. Hud son
ATuP-35

STRUCTURAL STUDIES OF CP PROTEIN AND ITS FRAGMENTS WITH
ANDROGEN RECEPTOR-MRNA

M. Sidiqi, J. Vivian , J. Wilce , and M. Wilce
ATuP-36

THE SIGNIFICANCE OF INTERACTION BETWEEN 06 HYDROXYLGROUPS OF GLUCOSE RESIDUES OF MALTOORIGOSACCHARIDEAND ji-AMYLASE FROM BACILLUS CEREUS VER. MYCOIDES

Hideo Miyake , Genji Kurisu , Masami Kusunoki , Sigenori Nishimura,and Yasunori Nitta

36

AsCA'OJ/Crystal-23
ATuP-37

Tuesday Aug 12

TOWARDS A CATALYTIC MECHANISM OF AMINOPEPTIDASE P

S. C . Graham , M. H. Lee , M. J. Maher, W.H. Simmons , H. C.
Freeman and J. M. Guss
ATuP-38

CRYSTAL STRUCTURE OF THERMOSTABLE ASPARTASE AND
STRUCTURE-BASED EXPLORATION OF FUNCTIONAL SITES IN THE
ASPARTASE FAMILY

Yasuo Hata , Tomomi Fujii , Hisanobu Sakai , and Yasushi Kawata
ATuP-39

CRYSTAL STRUCTURE OF THE CU-AMINE OXIDASE FROMARTHROBACTER GLOBIFORMIS IN COMPLEX WITH THE SUICIDEINHIBITOR 4-(2-NAPHTHYLOXY)-2-BUTYN-1-AMINEDavid B. Lang ley, Eric M. Shepard , Anthony P. Duff, Hans Freeman ,David M. Dooley, and J. Mitchell Guss
ATuP-40

STRUCTURAL GENOMICS OF NOVEL MACROPHAGE PROTEINSASSOCIATED WITH INFLAMMATORY DISEASE AND CANCER

Pawel Listwan, Nathan Cowieson , Anna Aagaa rd , Robert Serek ,Tim oth y Ravasi , Christine Wells , Th omas Huber, David Hume, andJenny Martin
ATuP-41

A STRUCTURAL GENOMICS APPROACH TO TUBERCULOSIS

Edward N. Baker, Vickery L. Arcus, Kristina Backbro , Graeme L.
Card, Jodie M. Johnston, Moyra Kamen , Nayden Koon , Simon Li ,Andrew A. McCarthy, Rochelle J. Ramsay, Miriam L. Sharpe , and J .
Shaun Lott
ATuP-42

HIGH THROUGHPUT APPROACHES FOR CRYSTALLISATION OF
BIOLOGICAL MACROMOLECULES

Christine L. Gee, Richard D. Kidd , Anna Aagaard , Fiona M. McMillan ,Niranjali U. Gamage , Paul R. Young , and Jennifer L. Martin
ATuP-43

THE STRUCTURE AND FUNCTION OF STREPTOLYSIN 0

Julian J. Adams , Susa nne C. Feil , Rodney K. Tweten, and Michael W.
Parker
ATuP-44

HIGH RESOLUTION ANALYSIS OF THE NEW INHIBITOR PGD-042
BOUND HUMAN HEMETOPOIETIC PROSTAGLANDIN D SYNTASE

N. Katsuyama , T. Inoue, Y. Okano , H. Shish itani , N. Okazaki, H.
Matsumura , Y. Urade , and Y. Kai
ATuP -45

THE ROLE OF PROLINE RESIDUES IN THE HINGE REGION OF Cdc2
KINASE SUBUNIT PROTEINS

J. Kelly, E. A. Williams , and M. J. C. Wilce
ATuP-46

SAD PHASING USING SULFUR ANOMALOUS SCATTERING WITH
CHROMIUM RADIATION

K. F. Tesh , C. Yang , J. W. Pflugrath , C. N. Stence, D. A. Courville ,and J. D. Ferra
ATuP-47

STRUCTURAL CHARACTERIZATION OF TWO PHOSPHOLIPASE A2
PROTEINS FROM THE VENOM OF THE AUSTRALIAN BROWN SNAKE,
PSEUDONAJA AFFINIS AFFINIS

Roopwant K. Judge, Matthew C. J. Wilce , and Jacqueline A. Wilce

37

Tuesday Aug 12

AsCA'OJ/Crystal-23
ATuP-48

X-RAY ANALYSIS OF YEAST LIPOAMIDE DEHYDROGENASECOMPLEXED WITH NAD+

Wataru Adachi , Kao ru Suzuki, Masaru Tsu noda, Takeshi Sekiguch i,
Lester J. Reed, and Akio Takenaka
A TuP-49

A NEW METHOD FOR PROTEIN CRYSTALLIZATION : SAMPLING
PHASE SPACE IN A MICROFLUIDIC ENVIRONMENT

Kyle Self, Ca rl L. Hansen, James M. Berg er, Stephen R. Quake ,Susa nna Ng, Shelley Godley , and Joseph Barco
ATuP- 50

MICROSTRUCTURES OF THE FeSiBNbCu SOFT MAGNETIC
MATERIAL STUDIED BY HIGH RESOLUTION ELECTRONMICROSCOPY (HREM)Vo Vong and Ng.Q .Th ang
A TuP-5 1

MICRO-ARRAY CHIP FOR HIGH-THROUGHPUT PROTEIN
CRYSTALLOGRAPHY

N. Wa tanabe, I. Tanaka , C. Nishiji ma , H. Takeuchi, and T. lseki
ATuP -52

STRUCTURES AND PHASE TRANSITION IN THE LAYEREDPEROVSKITE La 0 .6 Sr 0 ., Ti0 3

Christoph er J. Howard, and Zhao ming Zh ang
ATuP-53

STRUCTURE ESTIMATION OF ORBITAL ORDERED THIN FILMS
USING SYNCHROTRON RADIATION

Y. Wakabayashi , H. Sawa , M. Nakamura , M. Izumi, K. Miyano, andY .
Muraka mi
ATuP-54

THIN-FILM CRYSTAL STRUCTURE DETERMINATION OF Bb Fe 5 0 12
MEASURED WITH VCIP METHOD

K. Tanaka, K. ltatsu , N. Adachi, and T. Okuda
ATuP-55POLYTYPE POSSIBILITIES ARISING FROM PSEUDO SYMMETRIC
CRYSTAL STRUCTURES ALLOWING STACKING FAULTS

Anthony. C. Will is , A. David Rae , Tory N. Cayzer, and Michael S.
Sherburn
ATuP- 56

THE TEMPERATURE DEPENDENCE OF THE CRYSTAL STRUCTURE
OF 3,5-DI-T-BUTYLPYRAZOLE

Alexa ndre N. Sobolev, and All an H. WhiteAT u P-57

EXPERIMENTAL AND THEORETICAL STUDIES OF THE SULFOXIMINEGROUP [R1-S(=O)(=N-R2)R3] : DETECTION OF POSSIBLE LATTICEEFFECTS

Gerh ard Raabe
A TuP- 58

THE PDF-4/FULL FILE AND PDF-4/0RGANICS DATABASES : NEW
DATA MINING TOOLS FOR STRUCTURAL CRYSTALLOGRAPHY AND
MATERIALS CHARACTERISATION

Bria n O'Connor, Camden Hubbard , Ti m Fawcett, and John Faber
ATuP-59

HIGH TEMPERATURE LAUE METHOD WITH POLYCHROMATIC SR: ITSAPPLICATION TO QUARTZ PHASE TRANSITION

Kazumasa Ohsumi , Yoshikazu Miyata, Katsuhiro Kusaka , Takeshi
Nakagawa, and Kenji Hagiya

38

AsCA'03/Crystal-23
ATuP-60

Tuesday Aug 12

X-RAY EXTENDED-RANGE TECHNIQUE FOR PRECISION
MEASUREMENT OF THE X-RAY MASS ATTENUATION COEFFICIENT
AND IM(F) FOR MOLYBDENUM USING SYNCHROTRON RADIATION
C. T . Chantler, M. de Jonge , Z. Barnea , C. Q . Tra n, . B. Dh al, and D.

J . Cookson
ATuP-6 1

X-RAY MASS ATTENUATION COEFFICIENT OF SILICON : THEORYVERSUS X-RAY EXTENDED-RANGE TECHNIQUE AND OTHER
EXPERIMENTS

ATu P-62

THECRYSTALSTRUCTUREOFDOPEDPEROVS~TESDERNED

C. T . Chantler, C. Q. Tran, and Z. Barn ea
FROM ELECTRON SCATTERING TECHNIQUES

C. J. Ma unders, J. E. Etherid ge , C. J. Rossouw, and H. J. Whitfield
ATuP-63

EFTEM AND HRTEM STUDIES OF META-KAOLINITE AND METADICKITE

Sujeong Lee, Youn Joong Kim , Hi-Soo Moon , and Won-Sean Seo
ATuP-64

DEPENDENCE OF THE ACCURACY OF A CONTINUOUS PHASE
TRANSITION TEMPERATURE ON ANGULAR RESOLUTION IN
POWDER DIFFRACTOMETRY

Masatomo Yashima, Mizuki Mori , Roushown Ali , Masa hiko Tanaka ,and Takeharu Mori
ATuP-65

A NEW HIGH-TEMPERATURE FURNACE FOR HIGH-RESOLUTIONSYNCHROTRON RADIATION POWDER DIFFRACTION STUDY UP TO
1900K

Masatomo Yashima, Masahi ko Tanaka, Takeharu Mori , Kenjiro
Ohouchi , and Daiju lshimura
ATuP -66

SUB-SECOND X-RAY DIFFRACTION MEASUREMENT AND
STRUCTURE ANALYSIS BY MSGC

Hidehiro Ueku sa , Yuji Ohashi , Y. Tsuji , Y. Nishi , T. Tajima, and S.
Ad achi
ATuP-67

THE BEAMLINE FOR MACROMOLECULAR ASSEMBLIES OF THE
INSTITUTE FOR PROTEIN RESEARCH

Masa to Yoshimura, Eiki Ya mashita , Atsushi Nakagawa , Masaki
Yamamoto, Shinya Yoshikawa , and Tomitake Tsukihara
ATuP-68

X-RAY MICRODIFFRACTION SURFACE AREA INVESTIGATIONS OFTUNGSTEN CLAD MAGNESIUM ALLOYS

Nata sha Wright, M. Mandag ie, and G. Th eodossiou
ATuP-69

ON THE DESIGN FOR A VERSATILE IMAGING AND HARD X-RAY
BEAMLINE FOR MATERIALS SCIENCE, BIOMEDICAL, AND MEDICALAPPLICATIONS AT "BOOMERANG"

S. W . Wil ki ns, R. A. Lewis, K. K-W. Siu, A . W. Stevenson, K. A.
Nuge nt, and D. J. Parry39

Tuesday Aug 12

AsCA'OJ/Crystal-23
ATuP -70

DIRECT OBSERVATION OF OXYGEN MOLECULES PHYSISORBED IN
A MICROPOROUS COORDINATION POLYMER

Yoshiki Kubota, Masaki Takata, Makoto Sakata, Ryo Kitaura, Ryota ro
Matsuda , Susumu Kitagawa , Tatsuo Kobayashi, Kou ichi Kindo ,Yoshimi Mila, Akira Matsuo , Michihiro Kobayashi , Ho-Chol Chang,
T adashi Oszawa, and Megumi Suzu ki
ATuP-7 1

THE SELF-ASSEMBLED STRUCTURE OF A 2,6 DI(ACYLAMINO)PYRIDINE : FORMATION THROUGH N-H ... .N and N-H .. . O=C
INTER MOLECULAR INTERACTIONS
E. Ma rfo-Owusu and T. Kato

40

AsCA'03/Crystal-23

Wednesday Aug 13

Oral session 1A: Membrane proteins, macromolecularassemblies and receptors
Room A
Chair/Co-chair: Wah Chiu , Jacqui Gulbis
8:30

AWe1A-1

SYSTEMATIC APPROACHES FOR MEMBRANE PROTEINSTRUCTURE DETERMINATION

Ben Hankamer, Rosalba Rothnagel , Alasdair McDowall ,Geoff Ericksson , Francis Clark, Jasmine Banks, Bernard
Pailthorpe, Charles Sennoga , Andrew Heron, John
Seddon , Richard Templer, and David Crout
9:00

AWe1A-2

STRUCTURAL CHANGES IN AN~ T-CELL RECEPTOR
UPON LIGAND BINDING

Craig S. Clements. Lars Kjer-Nielsen , Anthony W. Purcell ,Andrew G. Brooks , James C. Whisstock , Scott R. Burrows ,James McCluskey, and Jamie Rossjohn
9:25

AWe1A-3

A NEW MODE OF PORE ASSEMBLY BASED ON THE
STRUCTURE OF INTERMEDILYSIN , A TOXIN SPECIFIC FOR
HUMAN CELLSGalina Polekhina , Rodney Tweten, and Michael W. Parker
9:50

AWe 1A-4

HIGH-THROUGHPUT PROTEIN STRUCTURE VALIDATIONALSO FOR INTEGRAL MEMBRANE PROTEINS

W. Bret Church, and Lawrence K. Lee
10:10

AWe1A-5

CRYSTAL STRUCTURE OF PEA TOC34- A NOVEL GTPASE
OF THE CHLOROPLAST PROTEIN TRANSLOCON

Chwan-Deng Hsiao, Yu h-Ju Sun , Farhad Forouhar, andHsou-min Li
10:30

Coffee break

Oral session 18: Charge density- experimental &theoretical approaches

Room 8Chair/Co-chair: Mark Spackman , K. Tanaka
8:30

AWe1 B-1

CHARGE DENSITY STUDY OF AN IRON NITROSYL COMPLEX

Yu Wang, and J. J. Lee
9:00

AWe1 B-2

FINDING HYDROGEN BY SYNCHROTRON POWDERDIFFRACTION

Makoto Sakata , Hitomi Sakai , and Eiji Nishibori
9:30

AWe1 B-3

CHARGE DENSITY STUDIES OF POLYMORPHIC ANTIULCER AGENTS. THE APPLICABILITY OF THE
ELECTROSTATIC POTENTIAL IN DRUG DESIGN

Jacob Overgaard , Mark P. Waller, and David E. Hibbs

41

Wednesday Aug 13

AsCA'03/Crystal-23
9:50

AWe1 B-4

ELECTRON DENSITY DISTRIBUTIONS ON WEAK INTERMOLECULAR INTERACTIONS - Br. .. Br INTERACTIONS

Masanori Yasui , Kouki Tamakawa , Fujiko Iwasaki, andOaisuke Hashizume
10:10

AWe1 B-5

CHARGE DENSITY ANALYSIS AND DIPOLE MOMENTENHANCEMENT IN MNA (2-METHYL-4-NITROANILINE)

Andrew Whitten , Mark Spackman , Peter Turner, Wim
Klooster, Ross Piltz, and Masaru Tach ibana
10:30

Coffee break

Oral session 2A: Protein structure, function and evolution
Room A
Chair/Co-chair: Peter Colman , Jamie Rossjohn
11 :00

AWe2A-1

HOW DO TRANSLATION FACTORS CATALYSE PROTEINSYNTHESIS?

Anders Liljas
11:30

AWe2A-2

EVOLUTION OF AN ORGANOPHOSPHATE DEGRADINGENZYME : A COMPARISON OF NATURAL AND DIRECTEDEVOLUTION

P.O. Carr, H. Yang , S. Yu Mcloughlin , J.W. Liu , X. Qiu ,R.J. Russell , J.G. Oakeshott, and D.L. Ollis
11:50

AWe2A-3

CRYSTAL STRUCTURE OF GLUTAMATE-CYSTEINELIGASE FROM ESCHERICHIA COLI B WITH SUBSTRATES

T. Hibi, M. Nakayama ,H. Nii, and J. Oda
12:20

AWe2A-4

CRYSTALLOGRAPHIC ANALYSIS OF THE MECHANISM OF
HMG-CoA REDUCTASE

Cynthia V. Stauffacher, Nicklaus Steussy, John W.
Burgner, Tim Schmidt, and Victor W. Rodwell
12:40

AWe2A-5

STRUCTURE AND SIGNALING IN THE EPIDERMALGROWTH FACTOR RECEPTOR FAMILY

T. P. J. Garrett, M-Z Lou , N. M. McKern , T. E. Adams, G.
0 . Lovrecz, R. N. Jorissen , E. C. Nice, A. W. Burgess, andC. W. Ward
13:00

Lunch

42

AsCA'03/Crystal-23

Wednesday Aug 13

Oral session 28: Materials and nanoscience

Room BCha ir/Co-chair: Ri chard Welberry, Christopher Howard
11 :00AWe2 B-1

SYNCHROTRON X-RAY AND MOLECULAR DYNAMICSSTUDIES OF La 2.,Sr, Cu0• WITH x'=1/8
Nobuo lshizawa, Ke nji Suzuki , Katsu mi Suda , and Douglas
du Boulay

11:30

AWe2 B-2

CORRELATION OF METAPRISM TWIST ANGLE WITHDISEQUILIBRIUM IN CALCIUM-LEAD FLUORO-VANADINITEAPATITES
Z. L. Dong , and T. J. W hite

11 :50AWe2 B-3

NEGATIVE THERMAL EXPANSION IN CYANIDE-BRIDGED
COORDINATION FRAMEWORK MATERIALSKa rena W . Chapman , An drew L. Goodwin , and Cameron
J. Kepe rt

12:20

AWe2B-4

PHASE TRANSITION AND STRUCTURAL CHANGE OF
TRICALCIUM PHOSPHATE AT HIGH TEMPERATURES UP
TO 1900 K
M asatomo Yas hima, Atsushi Saka i, Ke isuke Yama moto ,Yoshisato Ki mura, Yo shin ao Mishima , Masahiko Tanaka,
Takeharu Mori , Kenj i Ohoya ma, and Yasuo Ya mag uchi

12:40

AWe2 B-5

IN-SITU STRUCTURE SOLUTION AND PHASE
TRANSFORMATION STUDIES OF DRUG POLYMORPHS
USING HIGH RESOLUTION SYNCHROTRON POWDERDIFFRACTION
W . I. F. David, and K Shankla nd

13:00

Lunch

14:00

SCANZ General Meeting

Room A

Plenary session
Cha ir: David Rae
16:00

PL-5

THE ROLE OF NON-MEROHEDRAL TWINNING IN SOME
PHASE TRANSITIONS
Victor G . Young , Jr., Maren Pink,Neil R. Brooks , andW illiam Brennessell

Chai r: Sine Larsen
MECHANISMS OF SELF-ASSEMBLY AND SWITCHING OF
THE BACTERIAL FLAGELLUM
Keiichi Namba

17:00

PL-6

18:00

marresearch Sunset Dinner

43

44

Biological Structure Workshop
ProgramAugust13
Wednesday

14
Thu

15

BTh1

BFr1

CoffeeCoffee

BTh2

BFr2

9:00
9:30
10:00
10:30
11 :00
11 :30
12:00
12:30
13:00

---- -

13:30

Lunch
-

I

14:00
14:30
15:00
15:30

CCP4

16:00

Workshop

16:30

Registration

17:00
17:30

45

Lunch
~

-

-

Thursday Aug 14

Biological Workshop
Oral session 1: The need for speed

Room A

Chair: Jenny Ma rtin
9:00

BTh1 -1

CELL FREE PROTEIN SYNTHESIS AND
STRUCTURAL I FUNCTIONAL PROTEOMICS
Shigeyuki Yokoyama and Takanori Kigawa

945

BTh1-2A STRUCTURAL GENOMICS APPROACH TO
TUBERCULOSIS
Edward N. Baker, Vickery L. Arcu s, Kristina Backbro ,Graeme L. Card , Jodie M. Johnston , Moyra Kamen ,Nayden Koon , Simon Li , Andrew A. McCa rth y, Rochelle
J. Ramsay, Miriam L. Sharpe, and J. Shaun Lott

10:10

BTh1-3

STRUCTURAL GENOMICS OF NOVEL MACROPHAGE
PROTEINS ASSOCIATED WITH INFLAMMATORYDISEASE AND CANCER
Pawel Listwan , Nath an Cowieson , Anna Aagaard , Robert
Serek, Carmel Walsh , Tim othy Ravasi , Christine Wells,
Thomas Huber, David Hume, Jenny Martin , and Bostjan
Kobe

10:30

Coffee BreakRoom A

Oral session 2: Clever stuff
Chair: Sine Larsen
11:00

BTh2-1

ELECTRON CRYOMICROSCOPY OF VIRUS
PARTICLES AT SUBNANOMETER RESOLUTION
Wah Chiu , Z. Hong Zhou , Matthew L. Baker, Wen Jiang,
Joanita Jakana, Matthew Dougherty, Brian R. Bowma n,
Florante A. Quiocho, and Frazer J. Rixon

12:00

BTh2-2

CATCHING CATALYSIS IN THE ACT: PROBINGENZYME MECHANISMS USING SINGLE CRYSTALMICROSPECTROPHOTOMETRY AND X-RAY
CRYSTALLOGRAPHY
Arwen R. Pea rson and Carrie M. Wilmot

13:00

Lunch

14:00

CCP4 Workshop

18:00

Close

(see p383 for program)46

Room ABiological Workshop

Thursday Aug 14

Oral session 3: Are we there yet?

Room A

Cha ir: Mitchell Guss
20:00

BTh3-1STRUCTURE MODELLING AND VALIDATION
T. Alwyn Jones, Mark Harris, and Gerard J. Kleywegt

21 :00BTh3-2

THE PROTEIN DATA BANK AND STRUCTURALGENOMICS
Helen M Berman

22 :00

Close

47

48

Biological Workshop

Friday Aug 15

Oral session 1: Synchrotron beamlines and us!

Room A

Chair: Jose Varghese
9:00

BFr1-1CASSIOPEIA- A PROGRESS REPORT FROM THE
DEVELOPMENT OF FIVE BEAMLINES AT THE MAXSYNCHROTRON LABORATORY
Anders Liljas

9:45

BFr1-2BUILDING A USER-FRIENDLY BEAMLINE
Aina Cohen and Paul Ellis

10:30

Coffee BreakOral session 2: Synchrotron beam/ines and us! Part II

Room A

Chair: Matthew Wilce
11:00

BFr2-1NEW BEAMLINES FOR MACROMOLECULARCRYSTALLOGRAPHY
Janet L. Smith , Robert F. Fischetti, L. E. Berman, W. Diete ,R. Signorato, R. Benn , S. Stepanov, R. Sanishvili, S. Xu , A.
Urakhchin, 0 . Makarov, and W. W. Smith

11:45

BFr2-2BIOLOGICAL APPLICATIONS AT THE AUSTRALIANSYNCHROTRONJose Varghese

12:30

Discussion and Q&A with all Friday's speakers

13:00

Lunch

18:00

Rigaku/MSC Aussie BBQ

49

50

Sagamore XIV Program
AugustWed

17
Sunday18
Monday

8:30
9:00

5Th1

SFr1

5Sa1

5Su1

5Mo1

CoffeeCoffeeCoffeeCoffeeCoffee

5Th2

SFr2

5Sa2

5Su2

5Mo2

9:30
10:00
10:30
11 :00
11 :30
12:00
12:30
13: 00
13:30
14:00
14:30
15:00
15:30
16:00

Registration

51

Sagamore XIV

Thursday Aug 14

Oral session 1: Charge density studies onheavy-atom materials

Room B

Chair/Co-chair: Claude Lecomte, Yu Wang
8:30

OPENING REMARKSMark Spackman

8:40

STh1-1

BONDING EFFECTS IN LARGE METAL CLUSTER
MOLECULES
Piero Macchi. and Angelo Sironi

9:10

STh1-2

EXPERIMENTAL RESULTS ON COUPLED ANALYSISOF SPIN AND CHARGE DENSITIES OF Y AND Gd
COMPLEXES
N. Claiser, B. Gillon , M. Souhassou , C. Lecomte , N. K.
Hansen, Y. Pontillon , A. Caneschi , D. Gatteschi , C.
Carbonera , A. Bencini , A. Cousson , and E. LelievreBema

9:40

STh1-3SCATTERING FACTOR CALCULATIONS ANDDISPERSION CORRECTIONS FOR HEAVY ATOMS
Chris Chantler

10:10

STh1-4

MULTI-TEMPERATURE EDD MEASUREMENT IN
RARE-EARTH HEXABORIDES LB 6 (L=La, Ce, Sm)
K. Tanaka , S. Funahashi, and S. Takagi

10:30

Coffee BreakOral session 2: Instrumentation large and small

Room B

Chair/Co-chair: Fumitake ltoh , Steve Wilkins
11:00

STh2-1OPPORTUNITIES FOR RESEARCH AT AUSTRALIA'S
REPLACEMENT RESEARCH REACTOR
R. A. Robinson

11:30

STh2-2

EN PI -THE EUROPEAN NEUTRON POLARIMETRY
NETWORK, A STATUS REPORTFrancis Tasset

12:00

STh2-3CURRENT STATUS AND FUTURE PLANS AT THE
AUSTRALIAN SYNCHROTRON PROJECT
S.W. Wilkins

12:30

STh2-4

CHARGE DENSITIES OF PHOSPHORUS CONTAININGCOMPOUNDS AT 20 K
Marc Messerschmidt, and Peter Luger

52

Thursday Aug 14

Sagamore XIV
13:00

Lunch

Oral session 3: New approaches to measuring magnetisation
densities
Room B
Chair/Co-chair: Rob Robinson, Beatrice Gillon
20:00

STh3-1

EXPERIMENTAL ATTEMPTS TO MEASURE
NONCOLLINEAR LOCAL MAGNETISATION
P.J. Brown

20:30

STh3-2MAGNETIC EXAFS AS A TOOL TO MEASURE RADIAL
DISTRIBUTION OF SPIN AND ORBITAL MAGNETIC
MOMENTS
Andrei Roqalev, and Jose Goulon

21:00

STh3-3TWISTED STATES OF Fe/Tb MULTILAYERS
Katsuyoshi Takano, Kazuhiro lkeuchi , Hiroshi Sakurai ,Hiromi Oike , and Fumitake ltoh

21 :30Close

53

Sagamore XIV

Thursday Aug 14

Poster session 17:00- 18:30

VerandaSThP-01

THE ATOMISTIC ORIGIN OF THE INVERSE PIEZOELECTRIC
EFFECT IN a -Si02 AND a-GaP04
Jav Davaasambuu , Vasili Kochin , Andreas Pucher, Semen V.
Gorfman , Vladimir G. Tsirelson , Peter Blaha and Ullrich Pietsch

SThP-02

SIMULATION OF COMPTON DOUBLE SCATTERING
Yukinobu Kakutani , Akihisa Koizumi and Nobuhiko Sakai

SThP-03

DIRECT PHASE DETERMINATION OF FRACTIONAL REFLECTION
IN CHARGE-DENSITY-WAVE CRYSTALS USING X-RAY MULTIPLE
DIFFRACTION
Shih-Lin Chang , Chao-Hong Du , Mau-Tsu Tang , Yu . P. Stetsko , YenRu Lee , Tsong-Tze Lin , Shih-Chang Wong and Wen-Shien Sun

SThP-04

ELECTROSTATIC PROPERTIES OF THE MOLECULAR SIEVE
AIP04-15
E. Aubert, F. Porcher, M. Souhassou and C. Lecomte

SThP-05

VIRTUAL EXPERIMENTS FOR THE BUILDUP OF ASPHERICAL
ATOM SCATTERING FACTORS OBTAINED BY A NOVELPARTITIONING SCHEME AND APPLICATION TO A TRIVALINESTRUCTURE
Birger Dittrich and Dylan Jayatilaka

SThP-06

THE NEW QUASI-LAUE DIFFRACTOMETER AT THE
REPLACEMENT RESEARCH REACTOR
Wim T. Klooster

SThP-07

NEW IONIC MODEL POTENTIAL FOR SEMICONDUCTORS WITH
APPLICATION TO Si
Teiji Kobayasi and Hisashi Nara

SThP-08

EFFECTS OF ELECTRON CORRELATION ON MAGNETICCOMPTON
Yasunori Kubo

SThP-09

CHARGE DENSITY ANALYSIS AND DIPOLE MOMENTENHANCEMENT IN MNA (2-METHYL-4-NITROANILINE)
Andrew Whitten , Mark Spackman , Peter Turner, Wim Klooster, Ross
Piltz and Masaru Tachibana

SThP-10MOLECULAR ELECTRIC PROPERTIES USING HIRSHFELD
SURFACES: A NOVEL APPLICATION OF SURFACE INTEGRALSMark Spackman , Andrew Whitten , Joshua McKinnon, Xiaoxiong Meng,
and Christopher Radford

SThP-11STUDY OF ANISOTROPY IN MOMENTUM DENSITY OF COBALT
B. K. Sharma , B. L. Ahuja , S. S. Asawat, V. Purvia , Y. Kakutani , A.
Koizumi and N. Sakai

54

Sagamore XIV

Thursday Aug 14

SThP-12

THE STUDY OF THE PHASES OF COWS UNDER THE
APPLICATION OF ELECTRIC FIELDS USING MULTIPLE X-RAY
DIFFRACTION
Chao-Hung Du , Mau-Tsu Tang , Yuri P. Stetsko , Yen-Ru Lee , J. -J . Lee
and Shih-Lin Chang

SThP-13

CHARGE DENSITY STUDIES OF POLYMORPHIC ANTI-ULCERAGENTS. THE APPLICABILITY OF THE ELECTROSTATICPOTENTIAL IN DRUG DESIGN
Jacob Overgaard , Mark P. Waller and David E. Hibbs

SThP-14

CHARGE DENSITY ANALYSIS OF Ji-Si3N4
Doug du Boulay, Nobuo lshizawa and Victor Streltsov

SThP-15

CHARGE DENSITY STUDY UNDER HIGH PRESSURE
Makoto Sakata . Takafumi ltsubo, Eiji Nishibori, Yutakata Moritomo,
Norimichi Kojima , Yasuo Ohishi and Masaki Takata

SThP-16

FERMI SURFACE OF A SHAPE MEMORY ALLOY OF TiNi
N. Shiotani , I. Matsumoto, H. Kawata , J. Katsuyama , M. Mizuno, H.
Araki andY. Shirai

SThP-17PRECISE CHARGE DENSITY STUDY OF CYTOCHROME C-553 BY
MAXIMUM ENTROPY METHOD
Masaki Takata , Kenichi Kato, Hiroshi Tanaka , Atsushi Nakagawa and
Makoto Sakata

SThP-18

AN EXPERIMENTAL CHARGE DENSITY STUDY OF SINGLECOMPONENT MOLECULAR METALS, Ni(TMDT)2 AND Au(TMDT)2
E. Nishibori , Y. Fujishiro, M. Takata, M. Sakata, A. Kobayashi , W.
Suzuki , E. Fujiwara , H. Tanaka and H. Kobayashi

SThP-19

MULTIPOLE REFINEMENTS WITH RIGID-BOND AND LINKCONSTRAINTS
T. Koritsanszky

SThP-20

STRUCTURAL RELATIONSHIP OF Ji-SODIUM (X=0.33) AND p/COPPER (X=0.65) VANADIUM BRONZES MxV20s
Ruslan Ozerov, Victor Streltsov and Alexander Sobolev

SThP-21

VALENCE STATE OF VANADIUM ATOMS IN Ji-NaxV20s BRONZE
Ruslan P. Ozerov, Alexandra A. Alexa and Victor A. Streltsov

SThP-22

DEVELOPMENT OF MEASURING MAGNETIC COMPTONPROFILES BY GRAZING INCIDENT GEOMETRY
Hiroshi Sakurai, Fumitake ltoh, Minoru Ota, Katsuyoshi Takano, Xioxi
Liu and Hiroshi Kawata

SThP-23MAGNETIC COMPTON PROFILES OF MAGNETIC THIN FILMS
AND ANISOTROPY OF Co/Pd MULTILAYER
M. Ota, H. Sakurai , F. ltoh, M. ltou andY. Sakurai

55

Sagamore XIV

Thursday Aug 14

SThP-24

THE ELECTRON DENSITY TOPOLOGY CHANGES DUE TO THE
PHASE TRANSITION IN KMnF 3Yury V. Ivanov and Kiyoaki Tanaka

SThP-25

STRUCTURE ANALYSIS OF GAS MOLECULES ADSORBED IN
THE NANOCHANNEL OF A COORDINATION POLYMER BY THE
MEM/RIETVELD METHOD
Yoshiki Kubota , Masaki Takata , Makoto Sakata , Ryo Kitaura , Ryotaro
Matsuda, Susumu Kitagawa , Tatsuo Kobayashi , Kouichi Kindo,
Yoshimi Mita, Akira Matsuo, Michihiro Kobayashi , Ho-Chol Chang ,Tadashi Oszawa and Megumi Suzuki

SThP-26

MOMENTUM TRANSFER DEPENDENCE OF X-RAY RAMAN
SCATTERING AT THE BERYLLIUM K-EDGE
M. Volmer, C. Sternemann , J. A. Soininen , H. Nagasawa, M. Paulus ,H. Enkisch , G. Schmidt, M. Tolan and W. Schulke

SThP-27

CONSTRAINED DENSITY FUNCTIONAL THEORY USING X-RAY
DIFFRACTION OATA
Daniel J. Grimwood

SThP-28

A WAVEFUNCTION CONSTRAINED JOINTLY TO X-RAY AND
POLARISED NEUTRON DIFFRACTION DATA FOR THE Cs 3CoCI 5
CRYSTAL
Dylan Jayatilaka

SThP-29

CRYSTAL EXPLORER: A GRAPHICAL USER INTERFACE FORDISPLAYING AND MANIPULATING HIRSHFELD SURFACES AND
FINGERPRINTS FOR CRYSTAL ENGINEERING APPLICATIONS
Dylan Jayatilaka, Daniel Grimwood and Stephen Wolff

SThP-30

STUDY OF METAL-INSULATOR TRANSITION IN Rb4C 60 BY
COMPTON SCATTERING, UNDER PRESSURE
Genevieve Loupias, A. A. Sabouri-Dodaran , M. Marangolo, Ch . Bellin ,F. Mauri, S. Rabii , Th . Buslaps , M. Mezouar and W. Crichton

SThP-31

ARE ELECTRON CORRELATION EFFECTS OBSERVABLE IN
ELASTIC X-RAY SCATTERING EXPERIMENTS?
Graham Chandler, lan Bytheway, Brian Figgis , and Dylan Jayatilaka

56

57

Sagamore XIV

Friday Aug 15

Oral session 1: Inelastic X-ray scattering as a probe ofhighly correlated systems
Room BCha ir/Co-chair: Malcolm Cooper, Keijo Hamalainen
8:30

SFr1 -1

INELASTIC MAGNETIC X-RAY SCATTERING FROMHIGHLY CORRELATED ELECTRON SYSTEMS
P. A. Montano,Y . Li , J. F. Mitchell , P. E. Mijnarends, S.
Kaprzyk, B. Barbiellini and A. Bansil

9:1 5

SFr1 -2

ELECTRON CORRELATION EFFECTS IN NOVEL
MATERIALS: RECENT STUDIES OF CUPRATES ,MANGANITES AND 3D QUANTUM DOTS
Arun Bansil

10:00

SFr1-3

SUPERCONDUCTIVITY AND FERROMAGNETISM OF
ZrZn2
Zs. Major, S. B. Dugdale, R. Watts , G. Santi, M. A. Alam , S.
M. Hayden, J. A. Duffy , J. W. Taylo r, T. Jarlborg , E. Bruno,
D. Benea and H. Ebert

10:30

Coffee BreakOral session 2: New perspectives in the theory and computationof the electronic structure of solids
Room B
Chair/Co-chair: Dylan Jayatilaka , Andreas Savin
11:00

SFr2-1

WAVE-FUNCTION-BASED AB INITIO METHODS FOR
ELECTRONIC STRUCTURE CALCULATIONS ON
INSULATORSAl ok Shukla

11:40

SFr2-2

THE SIESTA METHOD: PRESENT STATUS AND FUTURE
PROSPECTS
Julian D. Ga le, Emilio Artacho, Alberto Garcia , Javier
Ju nq uera, Pablo Ordej6 n, Daniel Sanchez-Portal and Jose M.
Solerg

12:20

SF r2-3

SOME NEW DEVELOPMENTS WITH WAVEFUNCTIONSCONSTRAINED TO EXPERIMENTAL SCATTERING DATA
Dylan Jayatil aka

13:00

Lunch

58

Sagamore XIV

Friday Aug 15

Poster session 17:00 -18:30

Veranda(Same posters as Thursday August 14)

18:00

Rigaku/MSC Aussie BBQ

59

Sagamore XIV

Saturday Aug 16

Oral session 1: Density matrices and electron densities: newfunctions and new directions
Room B
Chair/Co-chair: Julian Gale, Bernardo Barbiellini
8:30

SSa1-1POSITION AND MOMENTUM DENSITIESCOMPLEMENTARITY AT WORK, REFINING A QUANTUM
MODEL FROM DIFFERENT DATA SETS
J. -M. Gillet, S. Ragot and P. J. Becker

9:00

SSa1-2

ELF : FOR THE GOOD AND FOR THE BAD
Andrea s Savin

9:30

SSa1-3SINGLE-PARTICLE ORBITALS AND MANY-BODY
COMPTON SCATTERING
Bernardo Barbiellini

10:00

SSa1-4CHEMICAL INFORMATION FROM THE SOURCEFUNCTION
C. Gatti , F. Cargnoni and L. Bertini

10:30

Coffee BreakOral session 2: Pushing the limits of experimental
charge densities

Room B

Chair/Co-chair: Mark Spackman , Masaki Takata
11 :00SSa2-1

THERMAL MOTION ANALYSIS, A MOLECULAR MEAN
FIELD MODEL
Hans-Beat Burgi

11 :30SSa2-2PSEUDOATOM RADIAL FUNCTIONS FROMTHEORETICAL MOLECULAR DENSITIES
T . Koritsanszky and A. Volkov

12:00

SSa2-3

MULTIPOLAR REFINEMENT OF PROTEINS : SUCCESSAND PITFALLS
B. Guillot, C. Jelsch , A. Podjarny and C. Lecomte

12:30

SSa2-4

CHARGE DENSITY STUDIES OF Z' = 2 MOLECULES.
POSSIBILITIES AND LIMITATIONS
Dai Hibbs, Mark P. Wall er and Jacob Overgaard

13:00

Lunch

60

Saturday Aug 16

Sagamore XIV

VerandaPoster session 17:00- 18:30(Same posters as Thursday August 14)

Oral session 3: Collinear and noncollinear spin densities in
Room B
electronic materials
Chair/Co-chair: Jane Brown , Rob Robinson
20 :00SSa3-1SPIN DENSITIES IN MOLECULE-BASED MAGNETICCOMPOUNDS: FIRST STUDY OF A PHOTO-INDUCEDMAGNETIC STATE
B. Gillon

20:30

SSa3-2ENSEMBLE REPRESENTABLE DENSITIES FOR ATOMSAND MOLECULES: ANALYSIS OF POLARISED NEUTRONEXPERIMENTS WHEN SEVERAL ZEEMAN LEVELS ARE
POPULATED
P. Cassam-Chena'i

21 :00SSa3-3OBSERVATION OF ORDERED ORBITAL OF YTi0 3 BY
THE X-RAY MAGNETIC DIFFRACTION EXPERIMENTS
Masahisa Ito, Naruki Tuji , Fumitake ltoh, Hiromichi Adachi,
Etsuo Arakawa , Kazumichi Namikawa, Hironori Nakao,
Youichi Murakami, Yasujiro Taguchi and Yoshinori Tokura

21 :30

Close

61

62

Sunday Aug 17

Sagamore XIV

Oral session 1: Developments in electron momentum
spectroscopy

Room B

Chair/Co-chair: Erich Weigold , Arun Bansil
8:30

SSu1-1

ELECTRON MOMENTUM SPECTROSCOPY OF SINGLECRYSTAL SILICON AND NICKEL TARGETS
M. Vos, C. Bowles , C. Chen , A. S. Kheifets , V. A. Sashin and
E. Weigold

9:10

SSu1-2

ORBITAL MOMENTUM DENSITIES OF CHEMICALLYSIMILAR MOLECULES USING HREMS AND OFT
M. J. Brunger, K. L. Nixon, L. Campbell , F. Wang , B.Appelbe,
M. Hamilton and D. A. Winkler

9:50

SSu1-3

PROBING ELECTRON MOMENTUM DENSITIES IN
MOLECULES USING A NEW MULTICHANNEL (e,2e)
SPECTROMETER
Masahiko Takahashi and Yasuo Udagawa

10:30

Coffee BreakOral session 2: Electronic structure measurements using electron
scattering techniques
Room B
Chair/Co-chair: Joanne Etheridge , Kenji Tsuda
11:00

SSu2-1

CHARGE DENSITY MEASUREMENTS OF TRANSITIONMETAL OXIDES USING CONVERGENT-BEAM ELECTRONDIFFRACTION
K. Tsuda , Y. Ogata and M. Tanaka

11:40

SSu2-2

CALCULATIONS OF ELECTRON ATOMIC SCATTERINGFACTORS AND TEMPERATURE DEPENDENT DEBYEWALLER FACTORS
Lian-Mao Penq

12:20

SSu2-3THE "COMBINATION METHOD" OF QUANTITATIVE CBEDAND X-RAY DIFFRACTION APPLIED TO CORUNDUM
Philip N.H. Nakashima, Victor A. Streltsov and Andrew W.S.
Johnson

13: 00

Lunch

18:00

Asian Buffet

63

64

Sagamore XIV

Monday Aug 18

Oral session 1: Recent developments in Compton scattering
Room B
Chair/Co-chair: Bal Krishna Sharma , Sohrab Rabii
8:30

SMo1-1

RECENT MOMENTUM DENSITY STUDY OF NOVEL
MATERIALS
Y. Sakurai and M. ltou

9:00

SMo1-2SPIN DENSITIES IN MOMENTUM SPACE
J . A. Duffy

9:30

SMo1-3

COMPTON-SCATTERING STUDIES ON ATOMIC AND
MOLECULAR SYSTEMS
S. Huotari, M. Hakala, Sz. Galambosi , S. Manninen, and K.
Hamalainen

10:00

SMo1-4COMPTON SCATTERING ON ALKALI-METAL-DOPEDSILICON CLATHRATES
M. Volmer, C. Sternemann, J. S. Tse , D. D. Klug , M. Paulus ,C. L. Bull , T. Buslaps, N. Hiraoka , and M. Tolan

10:30

Coffee BreakOral session 2: Topological analyses: current state-of-the-art
Room B
Chair/Co-chair: Carlo Gatti , Tibor Koritsanszky
11 :00SMo2-1

TOPOLOGICAL ANALYSIS OF 3D GRIDDED ELECTRONDENSITIES
P. Rabiller, M. Souhassou, C. Kalan, S. Dahoui and C.
Lecomte11 :30SMo2-2

CHARGE-DENSITY STUDY OF THE NON-LINEAR
OPTICAL MATERIAL: ZINC (TRIS)THIOUREA SULPHATE
Jacqueline M. Cole, Shamus L. G. Husheer, Dima S. Yufit,
Judith A. K. Howard and Garry J. Mcintyre

12:00

SMo2-3

TOPOLOGICAL CHARACTERIZATION OF
INTERMOLECULAR INTERACTIONS
Yu Wang , Chi-Rung Lee and Chih-Chieh Wang

12:30

SMo2-4

TOPOLOGICAL FEATURES OF THE ELECTRON DENSITY
AND THE BASIN PROPERTIES IN SOLIDS
A. Martin Pendas

13:00

Closing remarks and Lunch

65

66

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76

Monday August 11

AsCA'03/Crystal-23

ABSTRACTS
ORAL SESSIONS

77

PL-1

COHERENT X-RAY DIFFRACTION FOR PHASING IN CRYSTALLOGRAPHY

ian Robinson
University of Illinois, 1110 West Green St, Urbana, IL 61801 , USA(robinson@mrl.uiuc.edu)

This lecture will demonstrate how the use of a coherent X-ray beam canproduce additional information in a diffraction pattern which can provide phase
information . By solving the phase problem , the diffraction can then be inverted
to produce images of the crystal under investigation . Coherence is a quality
inherent to undulator radiation provided by third-generation synchrotron
sources. The resulting diffraction patterns must be oversampled with respect tothe spatial Nyquist frequency in order to supply sufficient information. Iterative
image reconstruction methods formerly developed by Fienup are then found toconverge on a plausible solution .
Three-dimensional images showing the microstructure inside micron-sizedgold nanocrystals will be presented [1]. It has been since found that thecoherence can be preserved even after moderate focussing of the beam . In thisway the resolution of the method can be greatly enhanced and so applied to awide variety of interesting materials. With the development of X-ray freeelectron lasers, we should one day be able to image individual biomolecules
without having to grow crystals first.
References

I

Williams , G. J., Pfeifer, M. A. , Vartanyants, I. A. and Robinson , I. K. (2003)"Three-dimensional Imaging of Microstructure in Gold Nanocrystals"
Physical Review Letters 90, 175501-1 .

78

PL-2
CONTROLLING THE VANDER WAALS INTERPLAY OF FULLERENE C60

C. L. Raston ,8 J . L. Atwood ,b L. J . Barbour,b and M. W. Heavenb
8

School of Biomedical and Chemical Sciences, University of Western Australia ,Crawley, Perth WA 6009 Australia ; bDepartment of Chemistry, University ofMissouri- Columbia , Columbia USA. (clraston@chem.uwa .edu.au)

Controlling the way fullerenes assemble has potential in building up
material with novel function. Large curved molecules such as calixarenes form
inclusion complexes with C60 whereby the fullerene can reside endo- and/or
exo-relative to the cavity of the calixarene , and this modulates the van der
Waals connectivity and spatial interplay of the fullerenes. The results presented
will focus on the use of calix[5]arene to assemble into different arrays .
Calix[5]arene, with its C5v symmetry cone conformation has complementarity ofsize and curvature relative to C60 , and the principle axis extremities of C10, as
well as potential symmetry matching . A 1:1 C60 /calix[5]arene complex
crystallises from toluene with the fullerenes organised in a one dimensional
zigzag array shrouded by a sheath of calixarenes (endo- and exo-cavity withrespect to each fullerene). The complex forms in the presence of other globularmolecules , including C1o as the major impurity in fullerite , and thus an impurity
facilitates the purification of Cso . This finding has implications in controlling theinterplay of Cso as well as in separation science. Advances in the complexationof C10 with calix[5]arene will also be presented . Remarkably the solid-state
structure of the Cso complex formed from solutions of the pure fullerene has thefullerenes organized in a Z-array comprised of five close packed columns which
are shrouded by a sheath of calix[5]arene molecules [1] .
References
I
Atwood , J. L. , Barbour, L. J. and Raston , C. L. (2002) Crystal Growth &Design , 2, 3-6.

79

AMo1A-1
STRUCTURE OF T7 RNA POLYMERASE ELONGATION COMPLEX AT 2.9A
RESOLUTION
Dmitry G. Vassyl¥ev ."·bTahir H. Tahirov.c Dmitry Temiakov,d Michael Anikin ,dVsevolod Patlan, William T. McAIIister,d and Shigeyuki Yokoyamaa.b,e.ll
acellular Signaling Laboratory; bStructurome Research Group and CHighThroughput Factory, RIKEN Harima Institute at SPring-8 , 1-1-1 Kouto,
Mikazuki-cho , Sayo , Hyogo 679-5148, Japan; dMorse Institute for Molecular
Genetics, Department of Microbiology, SUNY Health Science Center, 450
Clarkson Avenue, Brooklyn , New York, 11203, USA; eRIKEN Genomic
Sciences Center, 1-7-22 Suehiro-cho. Tsurumi , Yokohama 230-0045, Japan;'Department of Biophysics and Biochemistry, Graduate School of Science,
University of Tokyo , 7-3-1 Hongo, Bunkyo-ku , Tokyo 113-0033 , Japan(dmitry@yumiyoshi.harima .riken .go.jp)

The single-subunit bacteriophage T7 RNA polymerase carries out thetranscription cycle in an identical manner to that of bacterial and eukaryotic
multi-subunit enzymes. Here we report the crystal structure of a T7 RNApolymerase elongation complex , which shows that incorporation of an 8 bp
RNA :DNA hybrid into the active site of the enzyme induces a striking
rearrangement of the N-terminal domain . This rearrangement involves
alternative folding of -130 residues and a dramatic reorientation (-130°
rotation) of a stable core subdomain, resulting in a structure that provides
elements required for stable transcription elongation. A wide opening on the
enzyme surface which is likely to be an RNA exit pathway is formed , and the
RNA:DNA hybrid is completely buried in a newly-formed deep protein cavity.
Binding of 10 bps of downstream DNA is stabilized mostly by long-distanceelectrostatic interactions. The structure implies plausible mechanisms for thevarious phases of the transcription cycle , and reveals important structuralsimilarities with the mulitsubunit RNA polymerases.

80

AMo1A-2
CRYSTAL STRUCTURES OF THE REPLICATION TERMINATION PROTEIN
BOUND TO DNA REVEAL A MODE OF POLAR REPLICATION FORKARRESTJ. P. Vivian ," C. J. Porter,b J. A. Wilce ,b and M. C. J. Wilce••school of Medicine and Pharmacology; bSchool of Biomedical and Chemical
Sciences , University of Western Australia, Crawley 6009 , WA , Australia
Uvivian@receptor.pharm.uwa.edu.au)

The final phase of DNA replication in Bacillus subtilis begins with thearrest of the replication forks at a distinct region located approximately opposite
the origin. This terminus region is characterised by replication termination
complexes composed of 30 base pair DNA sequences comprising two
overlapping , inverted repeats of 16 base pairs , each capable of binding one
dimer of the replication term ination protein (RTP). It is thought that the RTPDNA complex is able to affect the arrest of replication forks by impeding the
progression of the leading helicase. Furthermore , the action of the RTP-DNA
complex is polar in nature; that is, it allows the replication fork to pass
unimpeded if it approaches from one direction yet halts its approach from theother. This in effect forms a "replication fork trap", or section of the chromosome
in which the replication forks are forced to fuse. This appears to be essential forthe successful transition and timing of the post-replicative processes . Identifying
the determinant of this polarity and furthermore the mechanism by which thehelicase is impeded has been intensely debated in the literature. Presently, itremains unclear whether polarity emanates through the differential binding
affinity of RTP for the overlapping binding sites or whether there are significant
conformational changes to the protein upon complex formation. Likewise , it is
not well understood whether the terminator complex is acting as a non-specificobstacle to helica se progression or whether the terminator complex may
specifically contact the helicase.
In this study crystal structures of RTP in complex with both a symmetricaland a pseudo-symmetrical DNA binding site have been deduced . Comparisonof these models reveals a mode of generating the structural asymmetry that
underlies the polarity and formation of the functional terminator complex.

81

AMo1A-3
TWO CRYSTAL STRUCTURES OF D(G 1CGAGAGC) SUGGEST THATPOTASSIUM IONS MEDIATE TO FORM DNA OCTAPLEX WITH I-MOTIF OF
GUANINE QUARTET
Jiro Kondo, Shun-ichi Umeda, Tomoko Sunami , and Akio Takenaka•Graduate School of Bioscience and Biotechnology, Tokyo Institute ofTechnology, Midori-ku , Yokohama 226-8501 , Japan Ukondo@bio.titech.ac.jp)
DNA structures have been described in duplex forms, the two strands beingaligned in the anti-parallel fashion, in general. As a special case, the telomeric
DNA is assumed to form quadruplex with G-quartet and intercalated cytosine
motifs (i-motif). In DNA replications, triple helix formation is required. Functional
DNA would have much more complicated structures. In the present study, the twoforms of crystal structures of d(G 1CGAGAGC) have been determined by X-ray
analyses to investigate the structural basis for such specific functions.
The octamer is crystallized in the
(a)
•
(b) .
two different forms , 5GI-1 and 5GI-2.
_,..,.~;- . ·~-........ ~,~;; · --~' .. 1:..!"~
These crystals belong to the same space: . ~ . ·• - f_,ji· -~r:--:~}r'group 1222, but with different unit-cell: · ~- : -~.. "·· -. . - . ~t _ -~ ~dimensions; a= 36.2, b=36.4 , and··· ·~.
'.rc=63.1A for 5GI-1 , and a=34.7, b=42.5 ,- ··: ·~:,.-,.,.
: .~and c=64.1A for 5GI-2 . In the 5GI-1· ~:.- ~--;(' , '/..,.~;,.~:•.:'·.'
crystal, which is obtained at relatively low
Fig . 1. The octaplex (a) and the two
potassium-ion
concentration ,thesplit quadruplexes (b) .
octamers are assembled to form anoctaplex (Fig . 1a) that has never been foundin nucleic acid structures. In the central partof this novel octaplex, the G5 residues areassociated around the crystallographic 2-foldaxis to form the two G-quartets stacked oneach other (Fig. 2a and 2b). A potassium ion
occupies the center of the octaplex forinteractions with the eight 06 atoms of the
G5 residues. Other two potassium ionsinteract to the four 06 atoms above andbelow the double quartets, respectively (Fig.
2a) . The A4 residues form water-mediated A- Fig . 2. The schematic diagram ofoctaplex formation (a), stacking ofquartets (Fig. 2c). Here, it is interesting to intercalated G5-quartets (b) and thenote that the octaplex is composed of the two water-mediated A4-quartets (c).
quadruplexes, each consisting of the fourparallel strands with a G-quartet. The two G-quartets with the opposite strand
polarity are intercalated (Fig . 2a). The present octaplex is characterized as an /motif of G-quartets.
In the 5GI-2 crystal, which is obtained at relatively high potassium-ion
concentration, however, the octaplex is split into two quadruplexes, each of whichcontains two G-duets bound to a potassium ion (Fig. 1b). Above and below them,disordered potassium cations and/or water molecules surround the protruded
bases. The two crystal forms suggest a dynamic formation of an octaplex from two
quadruplexes in solution .

t'·

82

·.i;.

AMo1A-4
BACTERIAL OFFENSE AND DEFENSE MECHANISMS USING NONSPECIFIC ENDONUCLEASES
8

Hanna S. Yuan ,8 Chia Lung li, 8 Kuo-Chiang Hsia , and Woei-Chyn Chublnstitute of Molecular Biology, Academia Sinica, Taipei , Taiwan ; blnstitute ofMedical Engineering, National Yang-Ming University, Taipei, Taiwan .
(hanna@sinica .edu .tw)

8

Restriction enzymes are probably the most well studied bacterial
endonucleases which cleave only short foreign unmethylated DNA with specificsequences and thereby protect the host methylated genome. In prokaryoticorganisms, a variety of other types of endonucleases involved in the protectionof bacterial cells have been identified but differ from restriction enzymes in thatthey cleave DNA in a sequence-independent manner. Examples include
Escherichia coli colicin, ColE?, which is an H-N-H endonuclease that digests
chromosomal DNA to kill target cells so the host cells have better survival
advantage during times of stress. The crystal structures of the endonucleasedomain of ColE? [1, 2] and its complex with DNA demonstrates how the H-N-H
motif mediates its functions in DNA binding and hydrolysis. The structure of theprotein-DNA complex also provides the structural basis for non-specificinteractions between ColE? and DNA.
The Vvn from Vibrio Vulnificus is another example of a non-specificendonuclease involved in defense. Vvn is located in the periplasm , capable ofdigesting DNA and RNA, so that it prevents the uptake of foreign DNA duringtransformation. The crystal structure of the magnesium ion-bound Vvn and thatof Vvn mutant H80A in complex with a duplex DNA and a calcium ion wereresolved both at 2.3 A resolution . Vvn has a novel mixed alb topology bearing
no similarity to other endonucleases, however, a known endonuclease motif
containing a "bba-metal" fold is identified in the central cleft region . The crystal
structure of the mutant Vvn/DNA complex shows that Vvn binds DNA at minor
grooves inducing moderate DNA bending and contacts only the phosphatebackbones. This result suggests the structural basis for Vvn's sequenceindependent recognition of DNA and RNA. In summary , our data provides asolid foundation for a better understanding of the molecular mechanisms of
non-specific endonucleases involved in the protection of bacterial cells and therecognition of DNA by sequence-independent DNA-binding proteins.
References
Cheng, Y. -S., Hsia, K. -C. , Doudeva , L. G., Chak, K. -F. and Yuan, H. S.
I(2002) J. Mol. Bioi., 324, 227-236.
Ko, T. -P ., Liao , C. -C ., Ku , W. -Y. , Chak, K. -F . and Yuan , H. S. (1999)
2
Structure, 7 , 91 -102.

83

AMo1A-5
STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS SINGLE-STRANDED
DNA-BINDING PROTEIN. VARIABILITY IN QUATERNARY STRUCTURE
AND ITS IMPLICATIONS

K. Saikrishnan. 8 J. Jeyakanthan ,8 J. Venkatesh ,b N. Acharya ,b K. Sekar,c U.
Varshney ,6 and M. Vijayan 8
8

Molecular Biophysics Unit; bDepartment of Microbiology and Cell Biology;
cBioinformatics Centre, Indian Institute of Science , Bangalore , 560012 , India(ksai@mbu.iisc.ernet.in)Single-stranded DNA-binding protein (SSB) is an essential protein
necessary for the functioning of the DNA replication , repair and recombination
machineries. The protein binds preferentially to single-stranded DNA (ssDNA).
As part of tuberculosis structural genomics project with specia l emphasis on
repair and recombination , we have solved the structure of the DNA-binding
domain of Mycobacterium tuberculosis SSB (MtuSSB) in four different crystals
distributed in two forms . The structure of one of the forms was solved by a
combination of isomorphous replacement and anomalous scattering. This
structure was used to determine the structure of the other form by molecularreplacement . Like most other SSBs , topologically the DNA-binding domain
contai ns the OB-fold. The globular core of the molecule in different subunits inthe two forms and those in Escherichia co li SSB (EcoSSB) and humanmitochondrial SSB (HMtSSB) have similar structure, although the three loops
exhibit considerable structural variation. However, the tetrameric MtuSSB has
an as yet unobserved quaternary association . This quaternary structure with aunique dimeric interface lends the oligomeric protein greater stability, which
may be of significance to the functioning of the protein under conditions ofstress. Modelling studies indicate a difference in the path adopted by thessD NA to wrap around MtuSSB , in comparison to EcoSS B-ssDNA.

84

AMo1B-1
X-RAY ANALYSIS OF VARIOUS REACTION PATHWAYS OBSERVED FOR
UNSTABLE NITRENES

Yuji Ohashi , Takahiro Mitsumori , Terufumi Takayama , Hidehiro Uekusa and
Masaki Kawano
Department of Chemistry and Materials Science , Tokyo Institute of Technology,
Ookayama , Meguro-ku , Tokyo 152-8551 , Japan (yohashi@cms .titech .ac.jp)

It has been well known that the triplet nitrenes are produced when thephenyl azides are exposed to UV light. However, the structures have not beenreported yet , since they are very unstable and active at room temperature .
Many kinds of reaction products from the triplet nitrene have been obtained .
Recently the structures of unstable carbenes and radicals were observed by Xray analysis , we intended to analyse the structures of nitrenes.
The first example is the nitrene produced from m-carboxylic phenyl azide ,1. Since the crystal of 1 was easily broken when it was exposed to the UV light,
the host-guest complex between 1 and dibenzylamine was produced . The
crystal was irradiated with the Hg lamp through a band path filter. The intensity
data before and after the irradiation were collected at 25 K using the vacuum
camera at the beam line , BL02B2 , at Spring-8. The analysed structure clearly
revealed the structure of the nitrene trapped in the host lattice . The bonddistance of C-N(nitrene) distance is 1.34(4) A, which is in good agreement withthe theoretical calculation .
The second example is the dimer formation from the nitrene. The dimer
formation is most popular pathway when the unstable nitrene is produced in asolution. Since the large molecular motion is necessary to form the dimer, thedimerization is not believed to occur in the solid state. When the polymorphic
crystal of the above host-guest complex was exposed to a Hg lamp and theintensity data were collected at 80 K using the SPART-CCD diffractometer. The
analysed structure revealed that approximately 10 % of the phenyl azide
molecule turned to the dimer structure. In the original crystal lattice , theinteratomic distance between the neighbouring nitrogen atoms , which arechanged to the nitrene, is 4.067 A. Moreover, the produced dimer structure
occupies nearly the same position as those of the monomer molecule before
photo irradiation.
The third example is transformation from a nitrene to a hetero-ring . The
crystal of 2-nitrophenylazide was exposed to the Hg lamp at 80 K and theintensity data were collected using R-AXIS RAPID. The analysed structure
showed no triplet nitrene but the formation of the five-membered ring. However,the characteristic triplet nitrene signal was observed at 5 K, when the ESR
measurement of the crystal was performed upon irradiation with the Hg lamp.
This suggests that the produced nitrene attacked to the neighbouring oxygen of
the nitro group to form the five-membered ring and became benzofuroxan , 2.
These three examples suggest that the in situ crystal structure analysis at
low temperatures make it possible to elucidate the various reaction pathways.
Moreover, the time-resolved structure analysis will be very powerful method tomake clear the complicated reaction pathway.

85

AMo1B-2
HYDROTHERMAL SYNTHESIS, CRYSTAL STRUCTURES, AND SOLID
STATE NMR SPECTROSCOPY OF METAL SILICATES

Kwang-Hwa Lii
Department of Chemistry, National Central University, Chungli , Taiwan 320,
R.O.C. (liikh@cc.ncu.edu.tw)

Organically templated metal phosphates have been extensively studied
because of interesting structural chemistry and potential applications in
catalysis. However, in most cases the organic templates cannot be removed
without collapse of the frameworks. This is in contrast to the high thermal
stability and extensive applications of zeolites in refinery and petrochemical
processes . Therefore , studies have been directed to the synthesis of transition
metal silicates to produce more stable frameworks [1 ,2]. Our synthetic methods
are 2-fold , namely mild hydrothermal reactions in Teflon-lined autoclaves at100-200 °C using organic a mines as templates and high-temperature, highpressure hydrothermal reactions in gold ampoules contained in a high-pressure
reaction vessel at ca . 550 °C and 150 Mpa using alkali metal cations as
templates. In this presentation I shall report the high-temperature, high-pressurehydrothermal synthesis, crystal structures, and solid-state NMR spectroscopy ofseveral new silicates of transition metals and group 13 elements [3-5].
References
1.
Francis, R. , Jacobson, A. J. (2001) Angew. Chem. Int. Ed. 40 , 2879 .
2.
Wang , X., Liu , L. , Jacobson , A. J. (2002) J. Am. Chem. Soc. 124, 7812 .
3.
Li , C.-Y., Hsieh, C.-Y. , Lin , H.-M., Kao , H.-M. , Lii , K.-H . (2002) lnorg. Chem.
41 , 4206.
4.
Kao , H.-M. , Lii , K. -H. (2002) lnorg. Chem. 41 , 5644 .
5.
Hung, L.-1. , Wang , S.-L., Kao , H.-M., Lii , K.-H . lnorg. Chem. in press.

86AMo18-3
POWDER NEUTRON DIFFRACTION STUDY OF UNSATURATEDTHIOAMIDE DERIVATIVE

Takashi Ohhara ," Susumu lkeda.a Kenichi Oikawa .a Akinori Hoshikawa.aTakashi Kamiyama. a Takaaki Hosoya ,b and Yuji Ohashib
alnstitute of Materials Structure Science , KEK, Tsukuba , lbaraki 305-0801 ,Japan; bDept. of Chemistry and Materials Science , Tokyo Institute ofTechnology, Meguro-ku, Tokyo 152-8550, Japan (tohhara@post.kek.jp)
Crystalline-state reaction , which proceeds with retention of single crystal
form , is one of the most interesting topics in crystal chemistry and many reactions
have been analysed mainly by single crystal X-ray diffraction. Recently, author andco-workers proposed a single crystal neutron diffraction (SND) analysis of acrystalline-state reaction as follows ; hydrogen atoms in the reactive part of thereactant molecule are replaced with deuterium atom as markers, then the
crystalline-state reaction is proceeded , and finally the migration of the deuterium
atoms according to the reaction is observed by SND. This analytical method is very
powerful to analyse the mechanism of crystalline-state reaction[1] . However, since
SND requires a very large single crystal , it is much more difficult to keep the single
crystal form during the reaction than single crystal X-ray diffraction study. So, we
proposed to apply powder neutron diffraction (PND) instead of SND. In PND,
retention of a large single crystal form is not necessary. Even though the accuracyof the structure of an organic molecule determined by PND is worse than that by
SND , we expected that the distribution of Hand D atoms in the reactive part, whichis the most important information in the analysis of a crystalline-state reaction ,would be clarified . In this work, we demonstrate that the distribution of H and D
atoms in organic molecule can be clarified by powder neutron diffraction.
As a target compound , we choose an unsaturated thioamide derivative
which is the reactant of the crystalline-state photo-cyclization to form a bthiolactam[2]. For the PND measurements , we prepared a partly deuterated
derivative (Fig. 1). The crystal system is monoclinic, the cell parameter is
a=8.654A, b=10 .156A. c=10.102A, b=98.76 . and the space group is P2 1.
Though the two phenyl groups are not the reactive part, the hydrogen atoms of
those phenyl groups were replaced with deuterium atoms to reduce thebackground . PND patterns were measured by Vega and Sirius TOF powder
neutron diffractometers at KENS with 15K. Rietveld}~coanalyses were carried out with RIETAN-2001T. The
ocf'" 11
I_ /l:DH,
structure of non-hydrogen atoms determined by single.1:-=c:0oc=eo crystal X-ray diffraction was adopted as an initial modelH,(c)H
H,cY'-YN'c--1 'co structure and the ratio of H and D atoms at eachhydrogen/deuterium sites in the reactive part were refined .
o, ~_J,~H,
The ratio of H and D obtained by PND was consistent with!= inthe known structure. This suggests that PND would be a
powerful tool such as SND for analyses of crystalline-state reactions.
References
Ohhara, T., Ikeda, S., lmura, H., Uekusa, H. , Ohashi , Y., Tanaka, 1. , Niimura,1
N. (2002) J. Am. Chern. Soc., 124, 14736-14740.
Hosoya, T., Ohhara, T. , Uekusa, H. , Ohashi. , Y. (2002) Bull. Chern. Soc.
2
Jpn., 75,2147-2151.

o,(

87

AMo18-4
PHASE TRANSITION OF DEHYDRATED CALCINED AIP0 4 -5
INVESTIGATED BY IN-SITU SYNCHROTRON XRD
Hwo-Shuenn Sheu ! Jey-Jau Lee ! Khin Win Phyu ! and Kuei-Jung Chaob
8

National Synchrotron Radiation Research Center, Hsinchu 300 , Taiwan ;bDepartment of Chemistry, National Tsinghua University, Hsinchu 300 , Taiwan(hsheu@srrc.gov.tw)

AIP04-S (IUPAC structure type AFI) was reported to consist of 4 , 6, 12membered rings and forms a hexagonal arrangement of parallel and onedimensional channels. A commensurate modulated structure along c axis wasobserved in the dehydrated , calcined AIP04-S . The commensurate modulated
structure is reversible during hydration and dehydration at room temperature.
The modulation structure of dehydrated AIP0 4-5 was determined to give thewave vector q being one-dimensional and a value of 3/Bc*. In-situ synchrotron
XRD studied found that modulation peaks disappear at the temperature above
70 °C. This phase transition is reversible during heating and cooling between
room temperature and 90°C (Fig. 1). No further phase transition was found up
to 400°C. The crystal structure at gooc was refined by Rietveld method withspace group P6cc. This crystal structure is similar to that of hydration form atroom temperature.

~0

~2

24

20

Fig . 1. Variable temperature synchrotron XRD of dehydrated AIP0 4-5 . The
modulation peaks are marked (*). Baseline of each pattern was shifted for
r.l::~rifv88AMo1B-5
COMPLEXES OF SIMPLE ALKALI METAL SALTS WITH
N,N'-AROMATIC BIDENTATE LIGANDS
Allan H. White , Jarrod N. Buttery, Effendy, George A . Koutsantonis , Siti
Mutrofin , Neil C. Placket!, Brian W. Skelton , and Claire R. WhitakerChemistry, University of Western Australia , Crawley WA 6009, Australia(ahw@crystal .uwa.edu .au)

A wide variety of adducts has been obtained between alkali metal salts
MX , M = Li , Na , K, Rb , (but not , as yet, Cs); X = Cl , Br, I, NCS , N03, CI04, PFe,
F3CS0 3 ( = 'tfs '), and N,N '- aromatic bidentate ligands , 'L' = 2,2'-bipyridyl(' bpy'), 1,1 0-phenanthroline ('phen '), and 2,9-dimethylphenanthroline ('dmp')
MX:L (1 :n), n predominantly 1,2,3 from non-aqueous solvent, S, the form of thecomplex being strongly influenced by the packing of the aromatic ligand planes.
The 1:1 X = oxyanion adducts are infinite one-dimensional anion-bridged
polymers , the unsolvated halide adducts binuclear (one only : [(dmp)Li( ~t­CI)2(dmp)]) , while the solvated adducts commonly have the form [LMSX] or[LMS 2]X (M = Li) , Na , or more complex arrays for larger M. For n = 2 , theadducts are predominantly of the mononuclear forms[XML 2], M = Li , Na , or[ML 2]X ; for M = Li, L = dmp , an isomorphous array is found with discrete
cations , but for L = phen , quasi-square-planar [ML 2f cations form stacks withthe anions in between , with NaPF 6 :phen (6:13) an unusual variant. In the limited
number of 1:3 complexes, the complexes predominantly take unusual forms .
A number of complexes are found with unusual stoichiometries :Kl :dmp :MeOH (6:8:3) is [K6 14(dmp) 8]1 2 .3MeOH , while Ktfs:dmp (4 :3) is adouble-stranded polymer . KCI04: phen :H20
(1 :5:6) is [(phen )3 K( ~t­OH2)2(phen )3](CI04)2. 4phen. 4H20 .

'89

AMo2A-1
CADB: CONFORMATION ANGLES DATABASE OF PROTEINS

K. Sekar. G. Ramya Bhargavi , P. Ananthalakshmi and S.S. Sheik
Bioinformatics Centre and Supercomputer Education and Research Centre ,IndianInstituteofScience ,Bangalore
560
012 ,
India
(sekar@physics.iisc.ernet.in)

CADB (Conformation Angles DataBase) provides an online resource foraccess to data on conformation angles (both main-chain and side-chain) ofprotein structures in two data sets corresponding to 25% and 90% nonredundant protein chains available in the Protein Data Bank. In addition , thedatabase contains the necessary crystallographic parameters . Also , thepackage has several flexible options and a display facility to visualize the mainchain and the side-chain conformation angles for a particular amino acid type .
The package can also be used to study the interrelationship between the mainchain and the side-chain angles . A web based JAVA graphics interface has
been deployed to display the user interested information on the client machine.
The database is being updated at regular intervals and can be accessed over
the
World
Wide
Web
Interfaceatthefollowing
URL :http://cluster.physics .iisc.ernet.in/cadb or http:// 144.16.71.148/cadb/.
The
details and the newly added options will be discussed.
Reference
1
Sheik, S.S ., Ananthalakshmi , P., Ramya Bhargavi , G., Sekar., K. (2003)
Nuc/. Acids. Res. 31(1) , 448-451.

90

AMo2A-2
USING STRUCTURAL INFORMATION IN FUNCTIONAL GENOMICS:IDENTIFICATION OF PROTEIN KINASE SUBSTRATES

Bostjan Kobe , Robert A . Breinl and Ross I. Brinkworth
Department of Biochemistry and Molecular Biology, University of Queensland ,Brisbane , Qld 4072 , Australia (b .kobe@mailbox.uq.edu .au).

Protein structure determines its function. Structural genomics initiatives
take advantage of this relationship, aiming to contribute to the global "functional
genomics" effort to functionally annotate every gene product. We hypothesizedthat for certain large families of proteins , structural information available forsome members of the family can be used in a comprehensive fashion to identify
the functions of all members of the family . We tested this hypothesis on theprotein Ser/Thr kinase family .
Protein kinases are responsible for protein phosphorylation , a posttranslational modification that regulates essentially every cellular processincluding metabolism , growth , differentiation , motility , membrane transport ,learning and memory. To ensure the signalling fidelity , protein kinases must be
specific and act only on a defined subset of cellular targets . Understanding thesubstrate specificity of a protein kinase therefore defines its cellular role.
The large number of protein kinases makes it impractical to determine
their specificities and substrates experimentally . Based primarily on threedimensional structural information on protein kinases , we developed a webinterfaced bioinformatic tool Predikin that predicts an optimal substratesequence for any Ser/Th r kinase, and this optimal sequence can then be used
to search for substrate proteins [1). First, we developed a set of rules governing
the binding of a heptapeptide substrate motif (surrounding the phosphorylationsite) to the kinase, using the available crystal structures, molecular modellingand sequence analyses of kinases and substrates . We then implemented theserules in a web-interfaced program for automated prediction of optimal substrate
motifs , taking only the amino acid sequence of a protein kinase as input. We
adapted the available algorithms (e .g. , Ref. [2]) to search protein databases(using the heptapeptide motif) for putative substrate proteins.
We show the utility of the method by analyzing yeast signal transdu ction
pathways . Our tool also allows us to assign likely kinases to all thephosphorylation sites identified by the yeast phosphoproteome analysis via
mass spectrometry [2) .
Our method is the only available predictive method generally applicable for
identifying possible substrate proteins for protein kinases , and helps in silica
construction of signalling pathways . The accuracy of prediction is comparable tothe accuracy of data obtained from systematic large-scale experimental
functional genomics approaches .
References
1
Brinkworth , R.l, Breinl , R.A . and Kobe , B. (2003) Proc. Nat/. Acad. Sci.
USA. 100, 74-79 .
2
Yaffe , M.B., Leparc G .G., Lai , J., Obata , T. , Volinia , S. and Cantley, L.C .
(2001) Nature Biotech. 19, 348-353 .
3
Ficarra , S.B. , McCieland , M.L. , Stukenberg , P.T., Burke , D.J ., Ross, M.M.,
Shabanowitz, J., Hunt, D.F . and White , F.M. (2002) Nature Biotech. 20 ,301 -305 .

91

AMo2A-3
CAN YOU PREDICT WHETHER A PROTEIN WILL CRYSTALLISE FROM
THE PRIMARY SEQUENCE ?
Adrian H. Batchelor
University of Maryland , School of Pharmacy , Bal timore , USA(abatchel@rx.umaryland.edu)

I'll be presenting a sim ple 'back of an envelope' approach to looking at a
protein sequence and decid ing wheth er it is likely to crystallise . One example inwhich thi s approach proved to be useful was the crystalli sa tion of Apica l
Membra ne Antigen 1 from Pl asmod ium falcipa rum. Work in prog ress towards
solving th is structure will also be discussed .

92

AMo2A-4
CYSTEINE DISTRIBUTION AND THE EVOLUTION OF SHORT CHAINOXIDOREDUCTASE ENZYMES: COVARIANCE AND DISULFIDE BOND
POTENTIAL

W. L. Duax ,"·c V. Pletnev ,b and R. Huether""Hauptman-Woodward Institute, Buffalo , NY 14203, USA; bShemyakin Institute,
Moscow, Russia ; cSUNY@Buffalo , Buffalo, NY, (duax@hwi .buffalo .edu)

The short chain oxidoreductase (SCOR) family of enzymes includes over
5000 members , extending from bacteria and archaea to humans , for which 36
have known crystal structures. The superfamily has at most one fully
conserved residue. One major subgroup of 1651 known and hypotheticalproteins has a highly conserved TGxxxGIG pattern in the first j3a turn of the
Rossmann fold. Approximately 20% of these enzymes have no cysteines, 20%
have two, three and four cysteines each and the remaining 20% have from fiveto eight cysteines . The majority of enzymes having no cysteines are fromprokaryotes. Many of the enzymes having 5 to 8 cysteines are found in plants.
None of the PDB crystal structures contain disulfide bridges. There are 10 sites
with 7% or more Cys occupancy. Covariance analysis reveals that 96 membersof the TGxxxGIG subfamily have Cys in more than one of the ten Cys-rich sites.
Of particular interest is the frequency of covariance of Cys in position 36 and
59 , 119 and 177, and 181 and 238 (3a, 20 j3-HSD sequence numbering). A
model of 1HOC in which C36-C59 , C117 -C179 , and C181-C238 pairs have
replaced the corresponding residues in the observed structure reveals that the
distances between the hypothetical pairs of sulfur atoms are 1.9A , 2.7 A, and
4.4 A, respectively. These distances suggest that little or no change inbackbone conformation would be required for disulfide bridges to form . The 22
SCOR proteins containing C36 and C59 residues include 14 known or putative
tropinone reductases from plants. One of these is PDB structure 2AE2. The
sulfurs of the two cysteines in this crystal structure are within 5 A of one
another. Permissible rotations about the C"-C(S) bonds would reduce theseparation to 2 A. The presence of 1mM dithiothreitol in the crystallization
media may have reduced a disulfide bond in the native structure. Researchsupported in part by NIH Grant No. DK26546.

93

AMo2B-1
THREE NOVEL POLYMERIC NETWORK OF CUPPER(II) CONSTRUCTEDWITH SUCCINATO LIGAND AND THE INFLUENCES OF WEAK
INTERACTIONS ON THEIR CRYSTAL PACKING
Tian-Huey Lu, a G. Mostafa,a and N. Ray Chaudhurib
80epartment of Physics , National Tsing Hua University, Taiwan , R.O.C .;bDepartment of Inorganic Chemistry, lACS, W.B. , India (thlu@phys.nthu.edu.tw)
The crystal engineering of metal organic coordination network is now a
growing field. The key objective of the advanced crystal engineering is thecontrol on manipulation of weak interactions in order to tune the properties ofthe bulk material to design and prepare of new functional materials , such as
molecular-based magnets etc. Thus , to synthesize new solid phases withpredictable stoichiometry and architecture for specific applications , one has tounderstand the underlying factors such as hydrogen bonding , n-n, C-H .. .ninteractions etc. that determine crystal packing . Till date, an accurate predictionof the overall crystal structure currently is almost impossible but it may beachieved in the near future.
With this background , the carboxylate group is one of the most widelyused bridging ligands for designing polynuclear complexes with interesting
magentic properties. The versatility of a carboxylate group can be illustrated by
the variety of bridging conformations , the most important being (a)syn-syn ,(b)syn-anti and (c)anti-anti.

I

0~ 0

I

I

M

M
(a)

(b)

(c)

Of the carboxylate groups , major studies have been done on oxalato
bridged metal complexes with a few examples of terepthalate , fumarate ,maleate , malonate , adipate etc but the reports on succinate and glutarate assuperexchange pathways are scanty in literature. These carboxylates showedwide varieties of the superexchange phenomenon and are closely related to thebridging conformations adopted by the carboxylate group in polynuclear
systems . To design a carboxylate bridged pre-assigned functional material ,hence to achieve a particular bridging conformation , a systematic study andmore examples of carboxylate bridged complexes are needed.
Here, we wish to report the relevance of the weak interactions for theconstruction of novel succinate bridged network structure of Cu(ll) and theirexchange pathway.
Crystal Data:(1) [Cu 2(J.L-OH 2}2(J.L-SUccinate)(bipy)(N0 3 )2]. , Triclinic, Pl , a=7 .0641 (6), b=9.841 0(8),c=1 0.4885(9) A, a=72 .079(2) 0 , ~= 7 3 . 1 76( 2 ) 0 , y=74.6290(10) 0(2) [Cu2(J.L-OH2M1'-succinate)(phen)(N0 3 )2] •. Triclinic,Pl , a=6.9386(8),b=1 0.3463( 14 ), c=1 0.8572(17) A, a =69.734(11 )0 , ~= 8 1 . 354 ( 11 )0 , y =75.687(1 0) 0
(3) [{Cua(J.L-Succinate).(phen) 12}(BF4 )•ln. Triclinic,Pl , a= 12.5769(10), b= 19.3034(15),c=1 9.3348( 16) A, a =60 187(2) 0 , ~=8 6 .864(2 ) 0 , y =80.538(2) 094

AMo2B-2
NEW BOROPHOSPHATES IN MAIN GROUP ELEMENTAL, GA AND INSYSTEMS : SYNTHESES AND STRUCTURES
J.-T. Zhao ," J .-X. Mi , b Y.-X. Huang ,bc M.-R. Li ,"c S.-Y. Maob and R. Kniepc•state Key Laboratory of High Performance Ceramics and Superfine Structures,
Shanghai Institute of Ceramics , Chinese Academy of Sciences, Shanghai
200050 , P.R . China ; bCollege of Chemistry and Chemical Engineering , Xiamen
University, Xiamen 361005 , P.R. China; cMax-Pianck Institute for Chemical
Physics of Solids, Dresden 01187 , Germany Otzhao@mail.sic.ac.cn)
Borophosphates , as potential microporous materials , have drawn muchattention in recent years and shown rich structural chemistry[1) . Although many
compounds with transition metal elements have been reported , compounds withthe p-block main group elements participating in the framework are rare . During
our systematic investigations of borophosphate compounds in systems
containing AI , Ga and In elements , more than ten new phases have beensynthesized by mild hydrothermal methods and structurally characterized by Xray diffraction methods [2) .
1
Although the molar ratio of the main non-oxygen elements (or cations) , A :111
M : B : P, are all the same in different compounds , they form four different
structures belonging to four types. The preferences of the type seem largely
governed by the ratio of the cation sizes of A 1 and M 111 • These four structure
types contain different anion complex of borophosphates . These different anion
111
complexes have different connectivity to the octahedral M 0 6 units, which lead1
to different porosities in these structures . A cations reside inside the channels
with 6- or 8-membered rings of polyhedral units as cross sections.
A 1M 111 [BP207(0H)J] , A 1 = Na , K; M 111 = Ga , In ; monoclinic , C2/c ,NaFe[BP207(0H)3) type [3]. The structure contain isolated anion units[(OH)02P0112-0 112B(OH )20 112-0 112P03{ .Naln[BP20a(OH)] [4], triclinic, P-1 , newtype. The structure contains dimeric [01 t2 0 3P-B(OH)03t2-02t2P02{ units.
A 11n[BP 2 0 8(0H)] , A1 = K, NH4, Rb; triclinic , P-1 , KFe[BP208(0H)) type[3) . The structures also contain dimeric [01120 3P-B(OH)03t2-0 2t2P02t units. It is
an intergrowth structure with the above type .A 1M111 [BP20a(OH)] , A = NH4, Rb ,Cs ; M 111 = AI , Ga ; monoclinic, P2 1/c, RbFe[BP208(0H)] type [5). The structurescontain connected [02P0212-03t2B(OH)-0 1t2P03{ units. References
1 Kniep , R. , Engelhardt, H. and Hauf, C. (1998) Chem. Mater. 10 , 2930-2934 .
2 Zhao, J.-T., Mi , J.-X ., Huang , Y. -X. , Li , M.-R ., Mao , S.-Y ., Kniep, R. et al.
(2001) Z. Kristallogr. NCS 216 , 15-16; (2002) Z. Kristallogr. NCS 217, 38; 163-172; 305-306 .
3 Boy, 1. , Cordier, G. , Eisenmann , B. and Kniep , R. (1998) Z. Naturforsch.
538 , 165-170.
4 Li , M.R ., Master Thesis, Xiamen University, (2002), p.60 .
5 Kniep , R. , Boy , I. and Engelhardt , H. (1999) Z. Anorg. Allg. Chem. 625 ,
1512-1516.

95

AMo28-3
IN-SITU SINGLE CRYSTAL X-RAY DIFFRACTION STUDIES OF
GUEST-EXCHANGE IN NANOPOROUS FRAMEWORK MATERIALSGregory J. Halder," Cameron J. Kepert," Boujemaa Moubaraki ,b Keith S.
Murray,b and John D. Cahsionc
8

Department of Chemistry, University of Sydney, NSW 2006 , Australia ; bSchoolof Chemistry, Monash University, Clayton , VIC 3800 , Australia ; cSchool ofPhysics and Materials Engineering , Monash University, Clayton , VIC 3800 ,Australia (g.halder@chem.usyd.edu.au)
Recently there has been much speculation that molecular frameworkmaterials , like coordination frameworks , may have the potential to emulate
industrially important porous materials such as zeolites. However, to date there
have been few conclusive structural reports , and the question as to what
happens to the frameworks during desolvation and resolvation remains
unanswered . Here we report the first complete crystallographic study ofreversible guest-exchange in one such material , utilising a new type of single
crystal x-ray diffraction experiment.
The robustness of the material M2(bpy)3(N0 3)4.2(g uest) (M = Ni 11 or Co 11 ,bpy = 4.4 '-bipyridine) to guest-exchange has been well documented (1 ,2].
including the first single-crystal structural refinement of the fully desolvatedsystem. Presently we have extended this work with in-situ single-crystal x-ray
diffraction experiments, monitoring the uptake and release of a range of guest
molecules into the host framework (Figure 1). These results represent the firstof their kind and have yielded very unique information on the structuralconsequencesgues~exchange.

A .2(Et0H)~1!1~1111~ A ~ A .2(Me0H)

Figure 1: Electron density difference maps (platon) illustrating the desorption
and resorption of guest species in the framework material M2(bpy )J(N0 3 )• (A) .

This technique has been further implemented to study a range of
nanoporous framework materials , including a system that exhibits guestdependent spin-state switching [3].
References1
Kepert, C.J. and Rosseinsky, M.J. (1999) Chern. Commun., 375-376.
2
Fletcher, A.J ., Cussen , E.J. , Prior, T.J. , Rosseinsky, M.J., Kepert, C.J. andThomas , K.M . (2001) J. Am. Chern. Soc. 123, 10001-10011 .
3
Halder, G.J ., Kepert, C.J. , Moubaraki , B., Murray, K.S . and Cashion , J.D. ,(2002) Science 298 , 1762-1765.

96

AMo2B-4
CHANNELS IN 3-DIMENSIONAL COORDINATION POLYMERS: ZINCSACCHARATE AND LANTHANUM MUCATE
Michael Moylan. Brendan Abrahams, Simon Orchard, and Richard Robson
School of Chemistry, University of Melbourne, Victoria , 3010 , Australia(m .moylan@pgrad .unimelb.edu.au)

Reaction of monopotassium saccharate (figure 1) with zinc acetateproduces a three-dimensional coordination polymer of composition ZnC6Ha0 8.2H20 consisting of pillars of zinc linked by saccharate ligands (figure 2).
Channels with square cross-section are formed with metals occupying thecorners and ligands generating the edges.
There are two types of channels in the structure , and they provide
remarkably different chemical environments . The channels alternate like theblack and white squares on a chessboard. The hydroxy groups attached to thetwo central carbons of the ligands surrounding the first channel are directed intothat channel. The neighbouring channel is lined with the carbons andhydrogens from the ligand. This arrangement renders the first channelhydrophilic and the second hydrophobic in character[1].
Crystals of lanthanum mucate (figure 3) form from hot aqueous mixturesof lanthanum nitrate and monopotassium mucate (figure 4 ). The resulting
coordination arrangement generates channels with hexagonal cross section.
The structure of the two polymers and the successful introduction andcrystallographic detection of several small non-polar guests such as 12,
azobenzene , and cyclooctatetraene into the hydrophobic channel of zincsaccharate is described.

Ht co,:H

Ht co,Ha-<

HO

H

HO

H

HO

H

H

a-t

01

H

H

CO.,K

H
CO.,K

Figure 1:
potassium
saccharate

Figure 4:
potassium
mu ca teFigure 2: zinc saccharate viewed
down the channel axis

Figure 3: lanthanum mucate
viewed down the channel axis

Reference
I
Abrahams , B., Moylan , M., Orchard , S. and Robson , R. Angew. Chern. In
press.

97

98

Monday August 11

AsCA'03/Crystal-23

ABSTRACTS
POSTER SESSIONS

99

AMoP-01
EXPERIMENTAL CHARGE DENSITIES IN STRONGLY HYDROGENBONDED AROMATICS
Ross 0 . Piltz,• David E. Hibbs,b Jacob Overgaardb and Peter Williamsc"Bragg Institute , ANSTO , Lucas Heights, NSW 2234 , Australia ; bSchool ofChemistry, University of Sydney, Sydney, NSW 2006 , Australia ; cBiostructural
and Biomolecular Research Group , University of Western Sydney, Parra malta ,NSW 2150 , Australia (rop@ansto .gov .au)

Conventional strong hydrogen bonds such as 0 - H ... 0 , N - H ... 0 and

0 - H ... N are clearly important in the areas of supramolecular chemistry ,crystal engineering and the study of biological activity . Unfortunately the
position of such hydrogen atoms cannot be located unambiguously inconventional charge density work using X-ray diffraction techniques . To
overcome this limitation combined X-ray/neutron diffraction studies have been
performed using the facilities of ANSTO , Lucas Heights and the University ofSydney on a set of hydrogen-bonded aromatics , including (Z)-N-methyi-Cphenylnitrone and 1-(2-hydroxy-5-nitro-phenyl)-ethanone. The results of these ,and other more recent studies , will be presented .

100

AMoP-02
A WAVEFUNCTION CONSTRAINED JOINTLY TO X-RAY AND POLARISED
NEUTRON DIFFRACTION DATA FOR THE Cs 3CoCI 5 CRYSTAL
Dylan Jayatilaka
Department of Chemistry, University of Western Australia , Crawley, WA 6009 ,Australia (dylan@theochem. uwa.edu .au)

The experimental wavefunction technique [1 ,2] is extended , to implement
the joint refinement of X-ray and Polarised Neutron Diffraction (PND) data .
Results are presented for the CoCI/- ion in the Cs 3CoCI 5 crystal.

ReferencesI
See , e.g., Grimwood , D., Bytheway , I. and Jayatilaka , D., (2003) J. Camp.
Chem . 24, 470-483.
2
Grimwood, D. and Jayatilaka , D. , TONTO: A System for Computational
Chemistry, www.theochern.uwa.edu .au/tonto/index.html.

101

AMoP-03
USING THE HIRSHFELD SURFACE TO INVESTIGATE CRYSTAL PACKINGIN POL YMORPHS AND CRYSTALS WITH Z' > 1

Joshua McKinnon, and Mark Spackman
Chemistry, School of Biological , Biomedical and Molecular Sciences, Universityof New England , Armidale, NSW 2351 , Australia Umckinn4@une.edu .au)

Understanding the differences in the crystal packing of molecules inpolymorphic structures, or differences in the crystalline environment of theunique molecules in crystals with Z' > 1.0 can be extremely difficult, particularly
when packing differences are subtle .
We have previously shown that the Hirshfeld surface of a molecular crystal
offers a remarkable new way of exploring packing modes and intermolecularinteractions in molecular crystals using a novel partitioning of crystal space[1].
Because these surfaces are most effectively utilised in the laboratory where
access to interactive molecular graphics is available , we have also devised a
two-dimensional mapping , called a 20 fingerprint plot , which quantitatively
summarises the nature and type of intermolecular interaction and presents thisinformation in a convenient colour graph[2].
We have found that the combination of the Hirshfeld surface and 20
fingerprint plot for a molecule in a crystal provides a particularly powerful tool
when attempting to investigate subtle differences where a molecule exists indifferent crystallographic environments . Here we present two detailed examples- three polymorphs of p -dichlorobenzene , and two polymorphs oftetrathiafulvalene (TTF), one of which contains four unique molecules.
References
I
McKinnon, J. J., Mitchell , A. S., Spackman , M.A. (1998) Chern. Eur. J. 4 ,2136-2141 ; McKinnon, J. J. , Mitchell , A. S., Spackman , M.A. (1998)
Chern. Commun. 2071-2072
2
Spackman , M. A. , McKinnon , J. J. (2002) CrystEngComm , 4, 378-392

102

AMoP-04
A NEW HYBRID MATERIAL WITH THREE DIMENSIONAL Na-0-Cu
CONNECTIVITY AND ITS NANOSTRUCTURES BY ANNEALING

G. Mostafa,8 Tian-Huey Lu ,8 and N. Ray Chaudhurib
80epartment of Physics, National Tsing Hua University, Taiwan , R.O .C.;
bOepartment of Inorganic Chemistry, lACS, W.B. , India(mostafa@phys.nthu .edu .tw)

There has been considerable interest in recent years in ordered arrays ofmagnetically coupled novel inorganic-organic hybrid framework , both from atechnological and a fundamental point of view. Incorporation of metal ions into
organic systems, functionality can be , introduced either through the inorganic
species or the organic linker molecules . Therefore , rational design andconstruction of new materials with specific networks has become a particularly
important and topical subject. We wish to report here , a new molecularmagnetic system of a heterometallic structure of general formula[Na2Cu(malonate)2( H20 )2]n obtained from a one pot synthesis which consists ofinterlocked anionic [Cu(malonate)2]n and cationic [Na(H20 h ln chains to form 30
coordination-polymeric network where the malonate dianion functions as ahexadentate ligand. To the best of our knowledge this is the first molecularsystem in which malonate functions as hexadentate ligand. The lowtemperature magnetic study reveals that the compound is ferromagneticallycoupled . The high temperature annealing of the 30 array leads to a mixed
metal oxide NaCu0 2 which shows nanowire (Figure) and nanodisks depending
upon annealing temperatures .

103

AMoP-05
PROTEIN CRYSTALLIZATION IN SPACE USING COUNTER-DIFFUSIONTECHNIQUE
Hiroaki Tanaka ,"·b Koji lnaka ,c Sachiko Takahashi ,b Satoshi Sano ,a Masaru
Sato ,a and Susumu Yoshitomia
aspace Utilization Research Center, National Space Development Agency ofJapan (NASDA) , Jbaraki 305-8505 , Japan; bJapan Space Utilization Promotion
Center, Tokyo 169-8624, Japan ; cMaruwa Food Industries, Inc., Nara 6391123, Japan (PXW01674@nifty.ne .jp)

Microgravity environment is known to provide ideal diffusive conditions forprotein crystallization such as reducing convective fluid motions andsedimentations. However it is not widely utilized because flight opportunities
had been limited and irregular. To overcome these problems and to promote
the utilization of microgravity environment , NASDA performs the protein
crystallization experiments twice a year for three years from February 2003
using Russian Service Module. At the first three flights , we use the facilities ,Granada Crystallization Box(GCB) , which is designed as a passive, light,
inexpensive and high-density experimental device for protein crystallization
inside capillaries by counter-diffusion technique , developed by Garcia-Ruiz(http://lec. ugr.es/).
To perform this project effectively, we developed two ingenious methods
as follows . Since most of the protein samples are crystallized by vapourdiffusion technique , we have to optimise the crystallization conditions of eachsample especially for counter-diffusion technique . To carry out this preliminary
study efficiently, we developed a new crystallization device using shorter
capillary and the simple gel in the silicone tube in the test tube (figure 1), which
requires Jess time and less amount of samples. A single capillary cancorrespond to a Jot of vapour-diffusion drops because it scans a wide area of
crystallization conditions. We also developed the simulation program using theempirically estimated diffusion constant values of the protein solution and theprecipitant solution to prospect the position
and the timing of crystallization in thecapillary. Hereby, we can easily find out thesuitable condition of the crystallization foreach sample.
Our first 46 protein samples are now inISS(International Space Station). As far as
the results of the preliminary crystallization
experiments on the ground , combination of
the preliminary experiment and thesimulation program worked very effectively.
We have convinced that the crystallization ini• lbe silico•c lub espace will contribute to the determination of
the protein structure more effectively using
this technique in the very near future . The standardizationof the crystallization conditions is now under Figure 1
consideration.

104

AMoP-06
PROTEIN CRYSTAL GROWTH WITH STIRRING SOLUTION

Hiroaki Adachi ," Kazufumi Takano,b Masashi Yoshimura ," Yusuke Mori ," andTakatomo Sasaki 8
80epartment of Electrical Engineering and Venture Business Laboratory, Osaka
University , 2-1 Yamadaoka, Suita , Osaka 565-0871 , Japan ; bDepartment ofMaterial and Life Science, Osaka University, and PRESTO , JST, 2-1
Yamadaoka , Suita , Osaka 565-0871 , Japan {adachi@ssk.pwr.eng .osakau.ac.jp)

The production of protein crystals with suitable diffraction quality and size is a
rate-limiting step for determining the three-dimensional structure of proteins at
atomic resolution. We propose a protein crystal growth with stirring the solution ,which is entirely different approach compared with the conventional method ,leading to an effective growth of protein crystals. Crystallographers believe that
protein crystal growth must be under a still condition , and it is ultimately performed
under a microgravity condition due to reducing convective flow. It is important thatthe protein solution must be stirred gently in protein crystal growth because directly
stirring a protein solution causes problems such as spontaneous nucleation,
protein denaturation and damaged crystals. We developed two methods for
growing large, high-quality protein crystals. One is FAST (floating and stirring
technique) using the Two-Liquid System[1] and a magnetic stirrer. The other isMicro-Stirring technique using a rotary shaker.
FAST realizes mild stirring suitable for protein crystal growth by stirring theliquid of the lower layer, which is primarily an indirect stirring method. The stirring
intensity is changed to optimize the growth conditions for a specific rotation rate,
shape of stirring bar, and volume of lower liquid. Using this method together withslow cooling, we obtained a 3.0 mm-long lysozyme crystal in 20 days from a seed
crystal[2] . This is larger than the 2.0 mm-long crystal grown without stirring . Whenthe protein solution is kept still , protein concentration gradually increases in thelower part of the solution . Consequently, excess protein solute that is not supplied
to the seed crystal leads to additional spontaneous nucleation. Stirring th e protein
solution accelerates the growth of the protein crystal and prevents additional
spontaneous nucleation.
On the other hand , Micro-Stirring enables to stir multiple micro-scale samples
in the growth of protein crystals by the sitting-drop and floating-drop[3] vapor
diffusion techniques. This is also effective in reducing the number of crystals and ingrowing large crystals compared to the conventional vapor diffusion technique[4] .
We also expect that stirring the solution will improve crystallinity.
References1
Adachi , H., Watanabe, T., Yoshimura , M. , Mori, Y. and Sasaki , T. (2002)
Jpn. J. Appl. Phys. 41 , L726-L728 .
2Adachi , H., Takano , K., Yoshimura , M. , Mori, Y. and Sasaki , T . (2002) Jpn.
J. Appl. Phys. 41 , L1025-L1027 .
3
Adachi , H., Takano , K. , Morikawa , M., Kanaya , S., Yoshimura , M. , Mori, Y.
and Sasaki , T. (2003) Acta. Cryst. 059 , 194-196.
4
Adachi , H., Takano , K., Yoshimura , M. , Mori , Y. and Sasaki , T. (2003) Jpn .
J. Appl. Phys. 42 , L314-L315.

105

AMoP-07

A STRUCTURAL STUDY ON THE POLYMORPH OF ICOSANE-1,20-DIOL

K. Uno,8 N. Nakamura,8 and Y. Ogawab
8

lntegrated Science and Engineering Major, Graduate School of Science andEngineering , Ritsumeikan University, 1-1 -1, Nojihigashi, Kusatsu, Shiga 5258577 , Japan; bDepartment of Chemistry, Faculty of Science . Kumamoto
University, 2-39-1 , Kurokami , Kumamoto 860-8555 , Japan(nakamura@se.ritsumei.ac.jp)

The two different crystal structures of icosane-1 ,20-diol , HO-(CH 2 )2o-OH ,which were obtained under the control of the crystallizing condition , were analyzed
by single crystal X-ray diffraction method. All measurements were made on a
Rigaku AFC-5R diffractometer with graphite monochromatized Cu Ka radiation . All
calculations were performed using Crysta/Structure[1] crystal structure analysis
package.
One of the crystal structures was a monoclinic system (a=9.697(3)A,
b=5 .231(2)A, c=39.674(3)A, (F91 .75(1) . Z=4) with a space group C2/c. The
structure was solved by direct methods with S/R92[2]. The non-H atoms wererefined anisotropically. The H atoms were located from a difference Fourier map
and the positional parameters were allowed to refine for the final refinements. The
isotropic displacement parameters were set at 1.2Ueq of the parent atom. The
R(F2>2o(F2)) value was converged to 0.065 by the final refinement. In themolecular structure, the hydrocarbon skeleton included both terminal hydroxygroups had an all-trans conformation. The long axis of the molecule was inclined tothe ab plane, and the molecules formed layers in a herring-bone arrangement, justas in the tilt-smectic phase of liquid crystals.
Another crystal structure was a monoclinic system (a=5.058(3)A,
b=7.219(4)A, c=27 .746(2)A, (F93.47(2) . Z=2) with a space group P2 1 . The
structure was solved by direct methods with S/R92[2]. The non-H atoms wererefined anisotropically. The methylene H atoms were located from a difference
Fourier map, and were allowed to ride on the parent C atoms. The hydroxy H
atoms were located from a difference Fourier map and the positional parameters
were allowed to refine for the final refinements. All H-atom isotropic displacement22parameters were set at 1.2Ueq of the parent atom . The R(F >2o(F )) value wasconverged to 0.040 by the final refinement. In the molecular structure, one of thehydroxy groups adopted a gauche conformation with respect to the hydrocarbon
skeleton , whereas the other adopted a trans conformation. The long axis of themolecule was normal to the ab plane, and the molecules formed layers which weresimilar to those of the smectic A liquid crystal. In this study, the crystal structuresof icosane-1 ,20-diol are compared with those of other homologues, alkane-a,wdiols. Moreover, we discuss a correlation between the polymorphism and thephase-transition phenomena in alkane-a,w-diols.
References
Rigaku/MSC and Rigaku Corporation . (2001) Crystal Structure Version
1
3.1 0. , Rigaku/MSC , 9009 New Trails Drive , The Woodlands , TX 77381,
USA. Rigaku, 3-9-12 Akishima , Tokyo 196-8666, Japan.
Altomare , A. , Cascarano , G. , Giacovazzo, C., Guagliardi , A. , Burla , M.,
2
Polidori , G. and Camalli , M. (1994) J. Appl. Cryst., 27 , 435.

106

AMoP-08
HYDROTHERMAL SYNTHESIS OF SINGLE-PHASE HYDROXYAPATITEWHISKERS AND CRYSTAL STRUCTURE CHARACTERISATION BY
HRTEM AND IMAGE SIMULATION

Z.L. Dong and T.J.White
Centre for Advance Research of Ecomaterials , Institute of Environmental
Science and Engineering , Innovation Centre , Blk 2, Unit 237 , Nanyang
Technological University, Singapore 637723 (zldong@ntu.edu .sg)

This study reports the crystallographic characterisation of synthetichydroxyapatite (HA) whiskers suitable for both environmental (e .g. toxic metal
capture) and biomedical (e .g. hard tissue replacement) applications. In bothcases , an excellent understanding of HA crystal structure and microstructure is
critical to ensure good chemical durability. In this study, hydroxyapatitewhiskers were synthesised through soft chemical reaction followed byhydrothermal and heat treatments. Powder X-Ray diffraction (XRD) and highresolution transmission electron microscopy (HRTEM) confirmed that either HA
or HA plus tricalcium phosphate (TCP) composite were obtained , depending on
the treatment conditions . Pure HA crystallised after hydrothermal reaction at
200 C. Rietveld refinement was used to determine the hexagonal lattice
parameters and atom positions of P6 3/m HA. Microstructures were investigatedby HRTEM (with cooling holder) and interpreted via multislice image simulation(with JEMS). Further study is needed to control the particle size , morphologies
and HA/TCP ratios , which will subsequently influence the properties offabricated HA coatings or bulk materials , as well as their capacity for heavy
metal removal from waste effluents and in vivo longevity.

107

AMoP-09
THE EFFECT OF MIXED Mn VALENCES ON Li MIGRATION IN LiMnz04:
MOLECULAR DYNAMICS SIMULATIONS

Kenji Tateishi , Douglas du Boulay, and Nobuo lshizawa
Materials and Structures Laboratory, Tokyo Institute of Technology, 4259
Nagatsuta Midori Yokohama 226-8503 , Japan (tateishi@r3401.msl.titech .ac.jp)

Lithium manganese spinels are attractive candidates for cathode materialsof rechargeable lithium ion batteries and have been studied extensively.
LiMn 20 4 presents a first order structural phase transition at 290 K. RodriquezCarvajal et al [1] solved the structure at 230 K and concluded that the transition
results from partial charge ordering on the Mn sites. Verhoeven et al [2] showedthat lithium ions exist at both 8a and 16c interstices of the Fd-3m structure andthat lithium exchange between those sites begins at around 285K andcorrelates with the Mn charge ordering . In our previous x-ray study, it was
revealed that lithium and oxygen atoms are distributed statistically about theirideal positions at room temperature , an effect which we attributed primarily tomixed Mn valences.
Here , molecular dynamics simulations were undertaken to study thecorrelation between local structural disorder and lithium ion migration in
stoichiometric LiMn 20 4. The displacements of oxygen atoms from ideal
3
positions were strongly governed by the arrangement of neighboring Mn • and4
Mn • valences . Consequently , changes of Mn valences with respect to time
directly involve time-dependent Li04 tetrahedral distortions. Simulations weremade assuming two distinct models: a) a model in which the arrangement of Mn
valences do not change with respect to time and , b) a model in which thearrangement of Mn valences change in time keeping but preserving overallcharge neutrality. In the model a) , although lithium atoms occupy both 8a and16c interstices, continuous lithium ion migrations were not observed. On theother hand using model b) , continuous lithium migrations were observed . If we
adopt the charge ordering viewpoint, then these results are quite consistent with
Verhoeven 's report because the lithium exchange commenced near thereported phase transition temperature. That is , we have strong evidence thatlithium migration is indirectly associated with the hopping of 3d electron
4
between Mn 3• and Mn • ions via the displacements of the coordinated oxygen
atoms.
References
Rodriquez-Carvajal , J., et al (1998) Physical Review Letters 81 , 4660I
4663.
Verhoeven, V. W. J., et al (2001) Physical Review Letters 86, 4314-4317 .
2

108AMoP-10
MECHANISM FOR PIEZOELECTRICITY OF LANGASITE CRYSTAL UNDERHIGH PRESSURE

N. Araki ,8 T. lwataki ," K. Kakimoto, 8 H. Ohsato ," T. Kuribayashi ,b Y. Kudoh ,band H. Morikoshic"Nagoya Institute of Technology, Nagoya, Japan; ~o hoku University, Sendai ,Japan; cMaterials Research Centre , TDK Co. , Chiba , Japan(araki@zymail.mse .nitech .ac.jp)

Langasite (La3GasSi0,4 ) is expected to be one of the new materials forsurface acoustic wave (SAW) device, because of its excellent piezoelectric
properties. Langsite belongs to trigonal system with space group P321 andlattice parameter of a 1 =8.1674(4) and c=5.0964(8)A. Figure 1 shows the crystal
structure (a ,-c plane) of langasite. A site containing La 3• forms decahedron , B
and C sites containing Ga 3• form octahedron and tetrahedron , respectively. 0site conta ining Ga3• and Si 4+ with 1:1 ratio forms tetrahedron. We reported thatthe change in the piezoelectric properties of langasite by substitution of thecation shows a close relation to the crystal structure at atmospheric pressure[1] .
In this work , we investigated the mechanism for piezoelectricity of
langasite by single-crystal X-ray analysis under high pressure to confirm themechanism proposed in the previous report.
Langasite crystal was prepared by the Czokralski method. The grown
crystal was formed into sphere. Diffraction intensity data were collected with afour-circle diffractometer. Diamond anvil cell (DAC) was used under highpressure (3.3 , 4.8 and 6.1 GPa) measurement. Refinement of the crystal
structure was performed by the full-matrix least-squares program RADY [2] . The
difference of the crystal structure observed at atmospheric, 3.3 and 6.1 GPa
were investigated.
C I
The a,-axis is preferentially shrunkc I
compared to the c-axis and their change/
depended the applied pressure and followed
liner functions . The cause of preferential
Ulc:::o...V·-...-' cshrinkage observed in a,-axis is shrinkage
of open space surrounded A , B and C sites
under high pressure. The mechanism forpiezoelectricity of langasite is explained , asfollows. Under high pressure , A site is
shrunk in the [1 00] direction accompaniedwith shrinkage of the open space.
Fig . 1 Crystal structure
Polarization in A site was enhanced byof langasite (a,-c plane)
applied pressure . This resulted in large
piezoelectricity.

~"----t[OOI[ReferencesI
lwataki , T ., Ohsato , H., Tanaka , K. , Morikoshi , H., Sato , J. , and Kawasaki ,K. (2001) Journal of the European Ceramic Society 21 , 1409-1412.
2
Sasaki , S. (1982) XL Report, ESS, State University of New York, 1-17.

109

AMoP-11
IMIDE-AMIDE BETWEEN KEMP'S ACID AND L-PROLINOL AND THE
HYDROGEN BONDING

M. Kawaminami. " Y. Odo,b T. Shimo ,b and K. Somekawab"Dept. of Physics , Faculty of Science ; bDept. of Applied Chemistry andChemical Engineering, Faculty of Engineering, Kagoshima University, Korimoto ,Kagoshima-shi 890-0065 Japan (kawamina@sci.kagoshima-u .ac.jp)

Kemp 's acid imide and L-prolinols each has an interesting hydrogenbonding ability. The two molecules were combined to study chiral host-guest
phenomena , and the hydrogen bonding in the new molecule , an imide-amide
were characterized by X-ray crystallography. The synthesis is as follows.
The imide acid chloride (1) derived from Kemp 's triacid was reacted withequimolar L-prolinol (2) in the presence of pyridine in CH2CI2 to give the chiralimide-amide (3) (mp. 237-9oC) [a ] 0 =-47.2°(MeCN) after recrystallization with
MeCN .
X-ray crystal structure analysis of the compound has been determinedusing Enraf-Nonius CAD-4 diffractometer with MoKa radiation . The compound
crystallizes in tetragonal space group P41212, with cell parameters a = 11 .892A,
3
c = 23.749(1) A, z = 8 and V = 3358.3N, the calculated density is 1.28 g/cm .
The structure was solved by direct methods (SIR) and refined with anisotropic
thermal parameters using full-matrix least-squares using Molen for all nonhydrogen atoms to a final R-value of 0.051 for 1898 reflections at Fo>3a(Fo) .
From the X-ray data one imide carbonyl seems to connect with thehydroxyl group in the L-prolinol moiety by a hydrogen bond to make the imidegroup asymmetric. The C=O ···HO distance is 1.65A.

l~
:
\:nj

0~
3

ReferenceI
Bach et al. (2002) J. Am. Chem. Soc. 124, 7982 .

110

AMoP-12
STRUCTURE ANALYSIS BEFORE AND AFTER ACCELERATEDEXAMINATION FOR DETERIORATION OF BAM, BLUE PHOSPHOR
H. lmura ," T. Honma ,b I. Hirosawa ,b Y. Shimomura ,c.d and N. Kijimad
8

Center for Analytical Chemistry and Science , Inc. , 1000 Kamoshida-cho, Aobaku Yokohama , 227-0033, Japan ; bJapan Synchrotron Radiation ResearchInstitute (JASRI), 1-1-1 Koto , Mikazuki-tyo , Sayo-gun , Hyogo, 679-5198 , Japan ;cKasei Optonix, Ltd ., 1060 Naruta Odawara , 250-0862 , Japan ; dMitsubishi
Chemical Corporation , 1000 Kamoshida-cho , Aoba-ku Yokohama , 227-8502 ,Japan. (imura .hiroyuki@mp .m-kagaku .co .jp).
Barium magnesium aluminate doped bivalent europium ions (Eu 2· ) ,BaMgAI1o0 17:Eu 2• (BAM) is known as one kinds of Blue Phosphor that is used inplasma display panel (PDP). The luminescence intensity derived from 5d-4ftransition of activator ion (Eu 2• ) , however, was gradually underlying in repeatedemission . The site-shift of activator ions from the Beevers-Ross(BR) site to theanti-Beevers-Ross(a-BR) site or to the mid-oxygen(m-0) site in intermediate
plane[1], and the partial valence-changes of the activated ion (Eu 2• ) to Eu 3. [2],were suggested as the reasons of deteriorated mechanism , but the mechanism
has not been shown clearly yet. So, in order to observe the structural alternationsin the deteriorated BAM , the accelerated examination for deterioration of BAM wascarried out. X-ray diffraction patterns of the BAM were measured and thestructures before and after the accelerated examination were analysed by Rietveld
method and Maximum Entropy Method (MEM).
The specimen was prepared from a commercial standard BAM (KX501A/Kasei Optonix, Ltd.). Accelerative examination was carried out under thefollowing procedure: the capillary stuffed with BAM was exposed to white x-ray
beam at SPring-8 BL28B2 for a day. X-ray diffraction data was measured at
SPring-8 BL 19B2 installed with Debye-Scherrer camera . The XRD pattern of
BAM-2 (After exposure) was compared carefully with that of BAM-1 (Before
exposure). The specific peak-shifts to higher-angle were observed , that is the
position of the 001 peaks corresponding to c-axis was selectively shifted . The lattice
parameters of BAM-1 and BAM-2 were refined (Table 1.), respectively. It wasobserved that the c-axis of BAM-2 was shorter than the one of BAM-1 .
Table 1. Lattice oarameters of BAM-1 and BAM-2
A
5.630(0)22.644(0)5.630(0)22.628(0)I Soecimens
I BAM-1
I BAM-2c..

IV1621 .62(1 )I 621 .1211 )I
I
I

In order to reveal the reason of the positional sh1fts of 001 peak, Rietveld
analysis and MEM analysis were carried out. The increase of the electron density
around a-BR and m-0 sites was not observed in BAM-2 as a result of MEM
analysis. It means that Eu ions were mostly located on initial BR site after theaccelerated examination . Furthermore it was observed that the atomic coordinates
and the atomic displacement factors (temperature factor) of each element wereslightly changed as a result of Rietveld Analysis. The relationship between thechanges of lattice parameters and atomic parameters will be discussed in detail.
References
I
Carrillo-Cabrera , W ., et al. (1986) Solid State /onics 18&19, 645.
2
Oshio , S., et al. (1998) J. Electrochem. Soc. 145, 3903

111

AMoP-13
CRYSTAL STRUCTURE OF A STREPTOCOCCAL SUPERANTIGEN, SPE-J

Heather M. Baker," Vickery L. Arcus,8 Thomas Proft,b Melissa Nicholson ,b John
D. Fraser,b and Edward N. Baker8
8School of Biological Sciences; bDepartment of Molecular Medicine, Universityof Auckland , Auckland , New Zealand (h.baker@auckland.ac.nz).

Superantigens (SAgs) are potent protein toxins that target the humanimmune system . The best known examples are those secreted by two
significant human pathogens , Staphylococcus aureus and Streptococcus
pyogenes , which are responsible for conditions that range from minor foodpoisoning to severe invasive disease. These SAgs disrupt the cellular immune
response by simultaneously binding to both MHC class II molecules and T-cell
receptors. More than 20 are known , characterised by a highly conserved fold
but relatively weak sequence conservation and much allelic variation.
Intriguingly, their modes of binding are surprisingly diverse [1] ; some have two
MHC-11 binding sites , others only one , some form dimers that can cross-link
MHC-11, and different sites on MHC-11 can also be targeted.
SPE-J (streptococcal pyrogenic exotoxin J) was identified as a potential
SAg from the S. pyogenes genome sequence , cloned , expressed and shown tohave potent SAg activity . It appears to have only one binding site for MHC-11 ,binding to its f)-chain in a zinc-dependent mode , yet it can also cross-link MHC11 [2]. Dynamic light scattering suggests it forms dimers , and this may explain its
cross-linking activity.
Monoclinic crystals of SPE-J were obtained : C2 , a=165.6, b=46 .3, c=72.2
A, [) =90.6°, with two molecules of 209 residues each in the asymmetric unit.
Although very tiny (maximum dimension 0.03 A) , these crystals gave asynchrotron data set to 1.7 A resolution . The structure has been solved bymolecular replacement , using the related SPE-C structure as search model ,followed by model-building with wARP . Intriguingly, SPE-J appears to form
quite a different dimer from that found for SPE-C [3], suggesting the likelihoodof a different mode of MHC-11 and TCR binding . Structure refinement is inprogress , and the details of the structure and its implications for superantigen
activity will be presented.
References
I
Arcus , V.L. , Prof!, T. , Sigrell , J.A. , Baker, H.M. , Fraser, J.D. and Baker,
E.N. (2000) J. Mol. Bioi. 299 , 157-168.
2
Prof! , T., Arcus , V.L. , Handley, V. , Baker, E.N . and Fraser, J.D. (2001)
J.lmmunol. 166, 6711-6719 .
3Roussel , A. , Anderson , B.F. , Baker, H.M., Fraser, J.D. and Baker, E.N.
(1997) Nature Struct. Bioi . 4, 635-643.

112

AMoP-14
STRUCTURAL GENOMICS OF MOUSE MACROPHAGE PROTEINSNathan Cowieson ." Pawel Listwan ,b Christine Wells." Thomas Huber,c Timothy
Ravasi ," Anna Aagaard ," Bostjan Kobe ,b David Hume• and Jenny Martina•1MB , University of Queensland , Brisbane , OLD , Australia ; bBiochemistry andMolecular Biology, University of Queensland , Brisbane , QLD , Australia ;cAdvanced Computational Modelling Center, University of Queensland ,Brisbane , QLD, Australia (n .cowieson@imb.uq .edu .au)

Microarray experiments conducted in the laboratory of David Hume (1MB ,UQ) have identified large numbers of genes that are transcriptionally upregulated when mouse macrophages are challenged with various antigens. The
gene products of many of these are uncharacterised. In an attempt tofunctionally annotate these, several structural biology groups at the Universityof Queensland are collaborating in a structural genomics initiative.
By gradually implementing high throughput or automated techniques totime consuming steps in the structure determination process the group aims tosolve the structures , by x-ray crystallography, of as many of these novel
proteins as possible . In this poster I present preliminary results on a number ofthese structural genomics target proteins.

113

AMoP-15

CRYSTALLOGRAPHIC STUDIES ON HEN SERUM TRANSFERRIN
Piyali Guha Thakurta , Debi Choudhury, Rakhi Dasgupta and J . K. Dattagupta
Crystallography and Molecular Biology Division ,Saha Institute of Nuclear
Physics , 1/AF Bidhanagar. Kolkata-700064, India (piyali@cmb2.saha.ernet.in)

Serum transferrin is the major iron-transport protein in vertebrates having
molecular mass -80 kDa. Its function depends on its ability to bind iron withvery high affinity , yet to release this bound iron at the low intracellular pH. The
three dimensional structure of diferric hen serum transferrin (hST) has been
determined by X-ray crystallography at 2.8 A resolution . The overall fold of thepolypeptide chain of hST is similar to those of hen avo transferrin (hOT) , rabit
serum transferrin (rST) and human lactoferrin (hLF) , being delineated into two
homologous lobes , each containing two dissimilar domains with one Fe 3 + andone col- ion bound at a specific site in each interdomain cleft. However, therelative orientations of the two lobes , which may be related to the classspecificity of transferrins to recepters , is different in hST from that of hOT, rST
and hLF. A number of additional hydrogen bonds between the two domains in
the N- and C- lobes have been identified in this structure that might indicate amore compact structure of hST than that of hOT and hence may be correlatedwith its iron transport function . A pair of hydrogen bonded lysine residues ,Lys209 and Lys301 , close to the N-Iobe iron binding site in the serum and avo
transferrins is termed as a "dilysine trigger". The NZ atoms of two lysine
residues in hST are 2.45 A apart which is comparable to other serumtransferrins but is different from that of hOT. One carbohydrate binding site has
been identified in the N- lobe at Asn52 of hST which is different from thecarbohydrate binding site Asn473 of hOT present in the C- lobe. A fucose
molecule has been modelled at this site. We also have a 3.45 A diffraction data
set of apo- form of hST, the Ca chain trace of which has already been
completed. The apo- and the halo- forms of chicken serum transferrins havebeen compared with each other as also with other proteins of the same family .

114

AMoP-16
TOWARDS THE STRUCTURE OF THE GRB7-SH2 DOMAIN

Corrine J. Porter." Peter J. Leedman,b Matthew C. J. Wilce ,"·c and Jackie A.
Wilce••school of Biomedical and Chemical Sciences, University of Western Australia ,Nedlands, WA 6009 , Australia ; blaboratory for Cancer Medicine, University
Department of Medicine, Royal Perth Hospital, University of Western Australia ,Perth , WA, 6000; cDepartment of Pharmacology, University of Western
Australia , Crawley, WA, 6009. (cporter@chem.uwa.edu.au).

Growth factor receptor bound protein-? (Grb7) is a member of a family ofSH2 domain containing adaptor proteins. SH2 domains are present in a diverse
group of proteins which are implicated in tyrosine kinase signalling . The SH2
domain of Grb7 binds to phosphorylated tyrosine residues located in thecytoplasmic domain of several growth factor receptors including the epidermal
growth factor receptor (EGF-R). Grb7 is co-amplified with EGF-R in a numberof human breast cancers. As it has been shown that breast tumours thatoverexpress EGF-R are generally estrogen-receptor negative and have a poor
prognosis, the Grb7-EGF-R complex provides an attractive target for thedevelopment of novel therapeutics in the treatment of breast cancer.
The aim of this research is to structurally characterise the Grb7 SH2domain . Milligram quantities of the Grb7 SH2 domain has been prepared andused in crystallisation trials. Small crystals have been produced which diffract to
3A and we will present a preliminary analysis of this data.

115

AMoP-17
DETAILED STRUCTURE OF L-METHIONINE y-L YASE FROMPSEUDOMONAS PUTIDA BASED ON THE RESULT OF 1.8 A RESOLUTION
X-RAY CRYSTAL STRUCTURE DETERMINATION
Shintaro Misaki ,8 Tomoaki Takakura ,b Takayuki Yoshioka ,0 Robert M Hofman ,dShigeo Yagi ,a Kenji lnagaki ,e and Akio Takimotob
8

Pharmaceutical Research & Development Division , SHIONOGI & CO. , LTO .
12-4 Sagisu 5-chome , Fukushima-ku , Osaka 553-0002 , Japan ; bDiscovery
Research Laboratories , SHIONOGI & Co. , LTD. 1-3, Kuise Terajima 2-chome ,Amagasaki, Hyogo 660-0813 , Japan ; 0 Strategic Development Department,
SHIONOGI & CO. , LTD . 12-4 Sagisu 5-chome , Fukushima-ku , Osaka 5530002 , Japan ; dAntiCancer Inc. , 7917 Ostrow Street, San Diego , CA 92111 , USA;eDepartment of Bioresources Chemistry, Faculty of Agriculture, Okayama
University, Okayama , Okayama 700-8530 , Japan(shintaro .misaki@shionogi.co .jp)

L-Methionine y-lyase from Pseudomonas putida (MGLpp) has received
much attention as an effective anti-tumor agent to various type of the cancer,
such as lung cancer, colon cancer , kidney cancer and fibre sarcoma [1 ,2].
Therefore the application of MGLpp to the medicine has been desired.
However, the stability of MGLpp in the plasma could be poor for its use of aprotein-drug. To resolve this problem , Tan et al investigated the modification ofthis enzyme with polyethylene glycol [3]. In alternative idea, any site mutation
using protein engineering would be useful. However, information about crystal
structure of MGLpp , especially, regions concerned with stability, is few [4]. To
increase the stability, information about N-terminal , C-terminal and active centre
would be necessary. In this study, detailed structure , recognition and reaction
mechanism of MGLpp would be discussed. Present R-value is 22.4 %.
Geometries of the active site are obtained very clearly.

References
I
Yoshioka , T., Wada , T. , Uchida , N. , Maki , H., Yoshida , H. , Ide , N ., Kasai ,H., Hojo , K. , Shono , K. , Maekawa , R. , Yagi, S. , Hoffman , R. M. , andSugita , K. (1998) Anticancer efficacy in vivo and in vitro, synergy with 5fluorouracil , and safety of recombinant methioninase , Cancer Res. 58 ,2583-2587.
2
Tan , Y. , Sun , X. , Xu , M., Tan , X., Sasson , A. , Rashidi , B., Han , Q., Tan ,X. , Wang , X ., An , Z ., Sun , F. X. and Hoffman , R. M. (1999) Efficacy ofrecombinant methioninase in combination with cisplatin on human colon
tumors in nude mice , Clin Cancer Res. 5 , 2157-63 .
3Tan , Y. , Sun , X. , Xu , M., An , Z. , Tan , X., Tan , X., Han , Q. , Miljkovic, D. A. ,Yang , M. and Hoffman , R. M. (1998) Polyethylene glycol conjugation ofrecombinant methioninase for cancer therapy, Protein Expression Purif.
12, 45-52 .
4Motoshima , H., lnagaki , K., Kumasaka , T. , Furuichi , M. , Inoue, H. ,Tamura , T., Esaki , N. , Soda , K. , Tanaka , N. , Yamamoto , M. and Tanaka ,H. (2000) Crystal structure of the pyridoxal 5'-phosphate dependent Lmethionine y-lyase from Pseudomonas putida , J. Biochem. 128 , 349-354.

116

AMoP-18
THE EAFP CRYSTAL GROWTH OBSERVED BY ATOMIC FORCEMICROSCOPY

Sheng Wanq. a,b Ye Xiang ,b Genpei Li ,b and Dacheng Wangb
Bioen~ineering Institute of Chongqing University, Chongqing , 400044 , P.R.
China ; Institute of Biophysics and National Microgravity Lab., CAS , 100101 ,P.R. China (wtscrystal@sina .com)

8

Eucommia antifungal protein(EAFP) is one kind of antifungal protein[1].
EAFP has 41 residues and crystals of EAFP belong to space group P21 with unitcell parameters a=19.085, b=23.225 , c=30.854 , ~ =98.64 [2]. EAFP crystals grew in
only 4-5 hours much faster than most of other macromolecular crystals. It isnoteworthy that the EAFP crystals diffract to almost the limiting resolution (-0.8 A).
The 30 structure was determined by direct methods with SnB[3,4] and refined with
Shelx-97 [5] .
The EAFP crystals were grown according to the method of Mr. Xiang[2] . The
target crystals grown directly on a glass cover glass were moved onto the AFM
sample stage for the acquisition of AFM images. All the AFM images werecollected on the {100} faces of the EAFP crystals in a fluid cell filled with motherliquor by both the contact and non-contact modes.
Nucleation and dynamic growth were studied by in situ Atomic ForceMicroscopy (Autoprobe CP-Research , Park Scientific Instruments). We found that
EAFP had special aggregates , ring-shaped clusters in original solution . The
diameter varied from about 180nm to 350nm. During AFM experiments we also
found that many linear aggregates sedimented on the surface of EAFP and thenincorporated into the lattice of the crystals. So the ring-shaped aggregates might
be split by precipitator and absorbed on the surface directly or be connected witheach other into longer linear aggregates.
At higher supersaturation we found that the EAFP crystals grew very fast withmacro steps by two-dimensional nucleation. The growing steps developed bygroups which consisted of about 5-6 steps. The step height was about 1.9 nm
corresponding well with the length of one axis. At low-to-moderate supersaturation ,one type of apparently anisotropic single-double-like spiral dislocations was foundon the {1 00} faces of EAFP crystals. After 8-9 screw steps all of them would
automatically grow into a series of whole intact elliptic layers. Thus we concluded
that during the process of growth EAFP molecules had strong ability to adjust
themselves to fit the lattice which perhaps was related to the special character of
EAFP molecules.
This work intended to understand the nucleation of EAFP crystal growth andkinetic mechanisms. This will help and maybe guide us to choose crystal
conditions for obtaining good quality crystals to give higher diffraction ability, andshed light on our knowledge concerning protein crystallization .
References
I
Huang , R.-H ., Xiang , Y. , Liu , X.-Zh ., et al. (2002) FEBS Letters, 521 : 87-90.
2
Xiang , Y., Huang, R.-H ., Liu W. , et al. (2002) Acta Cryst.D58, 1838-1840.
3
Weeks, C.M. & Miller, R. (1999) J. Appl. Cryst. 32 , 120-124.
4
Blessing , R.H. , & Smith , G.D. (1999) J. Appl. Cryst. 32 , 664-670.
5
Sheldrick , G.M.(1997)SHELX97, University of Gi:ittingen , Germany.

117

AMoP-19
CRYSTAL STRUCTURE OF ESCHERICHIA COLI ATASE N-TERMINALDOMAIN

Yibin Xu ." Rongguang Zhang ,b Paul D. Carr. c David L. Ollis.c and Subhash
G.Vasudevana,d•Department of Biochemistry & Molecular Biology, James Cook University,
Townsville , QLD 4811; bStructural Biology Centre , Argonne National
Laboratory, USA; cResearch School of Chemistry, Australian National
Univeristy, Canberra . ACT 2601 ; dPresent address: Novartis Institute forTropical Diseases . 1 Science Park Road , #04-14 The Capricorn , Singapore(yibin .xu@jcu.edu.au)

E.coli glutamine synthetase adenylyltransferase (ATase , EC 2.7 .7.42)
catalyses the adenylylation and deadenylylation of glutamine synthetase (GS) .
The two activities of ATase are mechanistically distinct, but are functionally thereverse of one another and must be carefully controlled by the organism inorder to prevent futile cycling . Growth will occur in a low ammonia environment
if GS is active with the deadenylylation activity of ATase switched on and the
adenylylation activity switched off. Conversely , in a high ammonia environment,
GS activity can be tuned down progressively by adenylylation until it iscompletely switched off when all 12 subunits are converted to the inactive GSAMP form . It has been shown that two activities of ATase reside on separate
domains. AT-N consisted of residues 1 through to 423 and was found to havethe deadenylylation activity but only partially soluble [1] . However ATN440(residues 1 to 440) is soluble and here we report the purification , crystallizationand 3D structure determination of AT-N 440 .
The crystals of ATN-440 belong to space group P3 221 with a=b= 116.6 A.
c=67 .6 A. a= ~=90° and y= 120°. Its crystal structure has been determined by
the MAD method and refined up to a resolution of 2.0 A. The structure reveals
a conserved protein motif present also in kanamycin nucleotidylyltransferase
and human DNA polymerase ~References
1
Jaggi , R. , van Heeswijk, W. C. , Westerhoff, H.V .. Ollis . D.L. andVasudevan , S.G. (1997). EMBOJ 16, 5562-5571.

118

AMoP-20
1.7A AND 2.1A X-RAY STRUCTURES OF HEMOGLOBIN E AND
HEMOGLOBIN A2, ISOLATED FROM THE BLOOD SAMPLES OF pTHALASSEMIC PATIENTS

J. K. Dattagupta , Udayaditya Sen , Debi Choudhury and Jhimli Dasgupta
Crystallography and Molecular Biology Division , Saha Institute of Nuclear
Physics , 1/AF Bidhan Nagar, Kolkata 700 064 , India
Uiban@cmb2.saha .ernet.in)

Hemoglobin A2 (a 262 ) , a minor (2-3%) component of circulating red blood
cells , acts as an anti-sickling agent [1] and its elevated concentration in ~ ­thalassemia is a useful clinical diagnostic. In ~ -thalassemia major, where there
is a failure of ~ -chain production , HbA2 acts as the predominant oxygen
deliverer. Hemoglobin E, another common abnormal hemoglobin caused bysplice site mutation in exon 1 of ~ globin gene , when combined with ~­thalassemia causes severe microcytic anemia. The purification , crystallizationand the structural studies of HbAz and HbE are reported here. HbAz and HbE
are purified by cation exchange column chromatography in presence of KCN
from the blood samples of individuals suffering from ~ -thalassemia minor andE ~-thalassemia. X-ray diffraction data of HbA2 and HbE were collected upto
2.1A and 1.73A respectively. HbA2 crystallized in space group P2 1 with unit cellparameters a=54.33A , b=83.73A , c=62 .87A , ~ =99 . 80 whereas HbE
crystallized in space group P2 12 1 2 1 with un it cell parameters a=60.89A ,b=95.81A , c=99.08A [2]. Asymmetric unit in each case contains one Hb
tetramer in R2 state. The structure of HbAz and HbE were refined to an R fa ctorof 18.3% (Rrree 21 .9%; PDB CODE 1NX5) and 19.1% (Rrree 21 .1%; PDB CODE
1NQP) respectively.

References

2

Nagel, R. L. , Bookchin , R. M., Johnson , J. , Labie , D. , Wajcman , H., lsaacSodeye , W. A., Honig , G. R. , Schiliro , G., Crookston , J. H., Matsutomo, K.
(1979) Proc. Nat/. Acad. Sci. 76(2), 670-672.
Dasgupta , J. , Sen , U. , Choudhury , D., Datta , P. , Chakrabarti , A. , Basu
Chakrabarty, S. , Chakrabarty, A. and Dattagupta , J. K. (2003) Biochem
Biophys Res Commun. 303,619-623.

119

AMoP-21
STRUCTURAL AND KINETIC IMPLICATIONS OF SUBSTRATE INHIBITION
IN THE HUMAN SULFOTRANSFERASE 1A1 ENZYME

Niranjali U. Gamage ,"·c Ronald G.Duggleby ,b Amanda C. Barnett ," Michael
Tresillian ," Catherine F. Latham ,"·c Nancy E. Liyou ," Michael E. McManus ," andJennifer L. Martine"Department of Physiology and Pharmacology , School of Biomedical Sciences ,University of Queensland , Brisbane , Queensland , 4072 , Australia ; bDepartmentof Biochemistry and Molecular Biology , School of Molecular and Microbial
Sciences , University of Queensland , Brisbane , Queensland , 4072 , Australia ;clnstitute for Molecular Bioscience , University of Queensland , Brisbane ,Queensland , 4072 , Australia (n.gamage1 @mailbox .uq .edu .au)

Sulfonation catalyzed by sulfotransferases is an important pathway indetoxification of a broad range of endobiotics and xenobotics , but evidence has
emerged in recent years that sulfonation can lead to bioactivation ofcarcinogens. A major human sulfotransferase , SUL T1 A 1, has been shown toplay a significant role in metabolizing many endogenous compounds and is
implicated in a range of cancers due to its ability to bioactivate carcinogenic andmutagenic xenobiotic compounds. The crystal structure that we report here isthat of SUL T1A1 complexed with PAP and the xenobiotic substrate pnitrophenol (pNP) [1). This is the first sulfotransferase structure complexed witha xenobiotic substrate and unexpectedly it reveals two molecules of pNP in theactive site. The kinetics of SUL T1 A 1with pNP shows slight non-hyperbolic
behaviour at low concentrations and substrate inhibition at higher pNP
concentrations . These kinetic features are fully consistent with the SUL T1 A 1
structure. The extended active site of SUL T1 A 1 revealed by the crystal
structure is also in agreement with binding of the endogenous ligand diiodothyronine but it cannot accommodate its other substrate ~ -estradiol as
easily . This therefore suggests that the binding site is flexible to accept diversehydrophobic molecules of varying sizes and shapes. Therefore , the SUL T1A 1
structure provides the structural basis for substrate inhibition and reveals thefirst clues as to how this enzyme sultanates various liphophlic compounds.
References1
Gamage NU , Duggleby RG , Barnett AC , Tresillian M, Latham CF , Liyou
NE, McManus ME , Martin J (2003) . Structure of a human carcinogenconverting enzyme , SUL T1 A 1: structural and kinetic implications of
substrate inhibition. J Bioi Chern. 278 , 7655-7662.

120

AMoP-22
SERA PROTEINS: ARE THEY CYSTEINE OR SERINE PROTEASES?

Robyn L. Malby ,a Anthony N. Hodder,a Vidana C. Epa ,b and Brendan S. Crabb88Walter and Eliza Hall Institute of Medical Research , Melbourne VIC 3050 ,Australia ; bCSIRO Division of Health Sciences and Nutrition , Parkville VIC 3052 ,Australia (rmalby@wehi.edu.au)

The serine repeat antigen (SERA) of Plasmodium is a candidate forinclusion in a malaria vaccine. The full-length protein of -120 kDa is processed
into several smaller fragments, one of which (P50) has significant homology tothe papain-like cysteine proteases [1 , 2]. Various members of the SERA family
exhibit intriguing differences in putative enzyme active site residues ; forexample , the dominantly expressed member of the P. fa/ciparum gene family ,SERA-5 , has serine substituted for the active site cysteine . A three-dimensionalmodel of the enzyme domain of SERA-5 has been constructed [3] , bycomparison with crystal structures of several cysteine proteases.
The enzyme domain of SERA-5 was produced as a recombinant protein in
E. coli, and purified by affinity and ion exchange chromatography. Small
crystals (ca. 80 !-lm x 40 ~Lm x 20 f.lm) were grown , and were found to diffract to- 3A. Diffraction data were collected [4] from a single cryo-cooled crystal on a
Rigaku R-AXIS IV image plate detector, using a Rigaku RU-300 generator
equipped with monocapillary optics [5] . We are currently attempting to solve thecrystal structure by molecular replacement, with the SERA-5 model and related
crystal structures as search models . We are also continuing to investigate bothsite-directed mutagenesis and altered crystallization conditions with the aim of
optimizing crystal growth.
References
1
Eakin , A .E., Higaki , J.N ., McKerrow, J.H. and Craik , C.S. (1989) Nature
342 , 132.
2
Higgins, D.G., McConnell , D.J. and Sharp , P.M. (1989) Nature 340 , 604 .
3
Hodder, A.N . eta/., manuscript in preparation.
4
We thank Bert van Donkelaar (CSIRO Division of Health Sciences andNutrition) for assistance with data collection .
5
Balaic, D.X. , Barnea , Z. , Nugent, K.A. , Garrett, R.F ., Varghese , J.N. andWilkins , S.W. (1996) J. Synchrotron Rad. 3, 289-295.

121

AMoP-23
STRUCTURAL FEATURES OF MORACEAE LECTINS

K. Sekar, 8 J.V .Pratap ,b A.A. Jeyaprakash ,b A. Surolia ,b and M. Vijayanb
8Bioinformatics Centre and Supercomputer Education and Research Centre ;bMolecular Biophysics Unit, Indian Institute of Science , Bangalore 560 012 ,India (sekar@physics .iisc.ernet.in)

Lectins are carbohydrate-binding proteins , which mediate various
biological processes . The B-prism fold was first discovered in the galactose
specific lectin jacalin from jackfruit seeds. Structural studies on the lectin,
carried out in this laboratory, also established post translational modification asa strategy for generating carbohydrate specificity. The homologous artocarpin ,a second lectin from jackfruit seeds , also assumes a B-prism fold. The absenceof post translational modification and the replacement of aromatic residues inthe binding site , make it mannose specific. Similar structures determined inother laboratories include Maclura fomifera agglutinin (MPA) , Helianthus
tuberosus lectin (heltuba), domain II of /\-endotoxin and the vittelline membraneouter layer protein. These structures among them , define the structuralfeatures of the B-prism fold as indeed those of Moraceae lectins. Among theproteins of the structural family , the structures belonging to the lectin family
Uacalin, MPA and heltuba) have much more similarity amongst themselves thanthose belonging to other types of proteins . In addition , among the lectins, thesimilarity is higher with the Moraceae family (with jacalin and MPA}, even when
their carbohydrate specificities are different. The details will be presented .

122

AMoP-24
THE CRYSTAL STRUCTURE OF A NOVEL CALCIUM BINDING PROTEIN
ATCBL2 FROM ARABIDOPSIS THALIANA

Masamichi Nagae," Akira Nozawa ,b Nozomu Koizumi ,b Hiroshi Sano,b Mamoru
Sato ,8 and Toshiyuki Shimizub
8

Graduate School of Integrated Science, Yokohama City University, 1-7-29
Suehiro-cho , Tsurumi-ku , Yokoham , Kanagawa , Japan; blaboratory of Plant
Molecular Breeding , Research and Education Center for Genetic Information,
Nara Institute of Science and Technology, lkoma, Nara, Japan(nagae@tsurumi. yokohama-cu .ac.jp ).

AtCBL2 is a member of a new family of calcineurin B-like calcium binding
proteins that has recently been identified in Arabidopsis thaliana . These
proteins have been shown to interact with novel family of serine-threonine
protein kinases (AtCIPKs) in a calcium dependent manner. The signal pathwayof AtCBL!AtCIPK plays critical roles in stress response such as salt, drought,
light. Despite the great importance of intracellular signaling pathways in plants ,no structural information has been obtained for AtCBL!AtCIPK system . Here,
we report the crystal structure of AtCBL2 and propose a unique target
recognition mecanizm of AtCBL!AtCIPK. Crystal of calcium bound AtCBL2 was
obtained in space group C222 1 with unit-cell parameters a=83 .9 A, b=118 .1 A,
c=49 .1 A. Using a synchrotron-radiation source , the crystal diffracts to 2.1 A,
with an overall R merge of 6.0 % and a completeness of 98 .8 %. One independent
molecule was estimated to be present in the asymmetric unit, with a solvent
content of 48 %. Phase to 2.5 A was determined by conventional multiple
isomorphous replacement with anomalous scattering method (MIRAS) . The
final model refined to an R value of 20.4 % and free R value of 24 .8 % at 2.1 A
resolution . The three-dimensional structure of AtCBL2 reveals a compact _helical structure with two pairs of EF-hands and the overall fold resembles thatof calcineurin B and neuronal calcium sensor 1, but significant structuraldifferences are observed. The first and fourth EF-hands differ from thecanonical sequence , but calcium ions are coordinated in the EF-hand . The restof the EF-hands are maintained in the open form by internal hydrogen bonds
despite lacking calcium ions. A possible site for the target binding based on thethree-dimensional structure is discussed.

123

AMoP-25
EXPRESSION, PURIFICATION AND CRYSTALLIZATION OF DEUTERATEDPROTEINS FOR NEUTRON DIFFRACTION
Kyoko Suto ." Noritake Yasuoka ,b Masaya Kitamura ,c and Hiroshi Mizuno••National Institute of Agrobiological Sciences , Tsukuba , lbaraki 305-8602, Japan;
bFaculty of Science, Himeji Institute of Technology, Hyogo, 678-1297 , Japan;
cFaculty of Engineering , Osaka City University, Osaka 558-8585, Japan(ksuto@affrc.go.jp)
In cases of most proteins, it is not easy to obtain crystals larger than 2mm 3
necessary for neutron diffraction measurement. Instead of preparation of suchlarge crystals, we tried to prepare and crystallize deuterated proteins.
Replacement of hydrogen atoms by deuterium atoms reduces the backgroundnoise and increases the scattering power in neutron diffraction. In this case, suchlarge crystals may not be required. We 'll show expression , deuteration andcrystallization FMN-binding protein (FMN-bp) using E. Coli system.
FMN-bp from Desulfovibrio vulgaris Miyazaki F is composed of 122 aminoacids and a FMN , which is the smallest among known flavoproteins[1]. The
function of FMN-bp in vivo is unclear at present, however it might take part in theelectron-transfer pathway. Structural studies have been already carried out by Xray crystallography[2].
Crystals of FMN-bp were grown to 2mm x 0.5mm x 0.7mm and diffracted up
to 0.84 A resolution at 100K, and to 1.10 A at room temperature using X-ray. In
the density maps, assignments of the atom species have been easily carried out,
judging from the peak height in electron density map. The 0 , N, C atoms wereidentified even at side chain of aspartic acid and I or threonine. Some peaks in the
difference Fourier map could be assigned for hydrogen atoms when they wereinvolved in the hydrogen bonding , but plurality of hydrogen atoms bonding tooxygen atoms could not be clearly assigned . It was difficult to find hydrogen atoms
particularly bonding to electronegative atoms or high temperature factor atoms[3] .
Neutron crystallography may provide to determine above hydrogen atoms
positions . Oeuteration of FMN-bp was carried out using E. Coli-002 0 medium
made by Silantes. Hi level expression system suitable to the medium was
prepared using pET-20b( +) vector with E. Coli strain BL21 (OE3). The deuterated
FMN-bp expressed without any tags and purified by ion-exchange column and gel
filtration . Purified 5mg holo FMN-bp and 3mg apo FMN-bp were obtained from 1L
medium. The molecular weights of deuterated FMN-bp and non-labeled FMN-bp
were measured by TOFF-MASS spectrum and deuterium ratio was estimated to73%. Firstly crystallization of the deuterated FMN-bp was tried with conditions
similar to the case of non-labeled FMN-bp. Although some crystals appeared ,good crystals could not be obtained. When suitable crystallization condition was
dramatically changed , the unit cell of the crystal changed from non-labeled FMNbp. The crystals obtained in 0 20 solution grew up to 1mm x 0.5mm x 0.3mm. The
X-ray diffraction data was measured up to 1.35A resolution . Preparation of larger
size of crystals is now in progress for neutron diffraction study.
References
I
Kitamura , M., et al. (1994) J. Bioi. Chem. 269 , 5566-5573.
2
Suto, K. , et al. (2000) Acta Crystallogr., D56, 368-371
3Suto, K., et al. (2001) J. Phys. Soc. Jpn., 70, Supplement A, 406-407

124

AMoP-26
CRYSTAL STRUCTURE OF FLINC4, AN INTRAMOLECULAR LM04:LDB1
COMPLEX
Janet E. Deane , Megan Maher, J. Mitchell Guss, and Jacqueline M. Matthews
School of Molecular and Microbial Biosciences , University of Sydney, NSW
2006 , Australia (J.Deane@mmb.usyd.edu.au)
LM04 is a member of a small family of nuclear transcriptional regulators thatis important for both normal development and disease processes. The LMO family
comprises four members, LM01-4 of which two, LM01 and LM02 , are known
oncogenes. LM04 was originally identified as a breast cancer autoantigen [1] andhas recently been shown to be overexpressed in over 50% of primary breast
cancers [2]. LM04 is comprised primarily of two tandemly repeated LIM domains.
These domains each contain two structural zinc ions and have been identified asimportant motifs that mediate specific protein :protein interactions. In particular,
LM04 has been shown to interact directly and simultaneously with BRCA1 , CliPand the ubiquitous nuclear adaptor protein LIM domain binding protein 1 (ldb1) toform a stable complex in vivo [3] . LM04 interacts with ldb1 via a 39-residue region
towards the C-terminus known as the LIM interaction domain (LID). Ldb1 is ofparticular interest as it binds LMOs and related LIM homeodomain (LHX) proteins
with high affinity, and contains an N-terminal homodimerization domain that may
allow the formation of higher order functional complexes [4].
An intramolecular complex consisting of the two LIM domains from LM04
linked to the LID domain of ldb1 has been engineered; FLINC4 (fusion of the !JD
domain of ldb1 and the ~- and ~-terminal LIM domains of LM01). FLINC4 waspurified and crystals belonging to space group P312 with unit-cell parameters a=
61.3 A and c = 93.2 A were grown . There is one molecule of FLINC4 perasymmetric unit (ASU) . Native and multiple-wavelength anomalous dispersion(MAD) data at the zinc edge have been recorded to resolutions of 1.3 A and 1.7 A,
respectively. Anomalous Patterson maps calculated from data collected at thepeak wavelength and showed strong peaks sufficient to determine the positions of
the four zinc atoms per ASU. Initial phases calculated to a resolution of 1.7 A
allowed 154 out of 188 residues of FLINC4 to be traced. Refinement of thisstructure to 1.3 A resolution is underway with current values of R = 20.4 % andRrree = 23.8 %. Analysis of the structure of FLINC4 suggests a mechanism bywhich ldb1 can bind LM04 specifically, and LIM domains from LMO and LHX
proteins in general. Important residues at the interaction interface have been
identified and may help in the design of specific inhibitors of this interaction as
potential treatments for some forms of breast cancer.
References
1
Racevskis , J., Dill , A. , Sparano, J.A. and Ruan, H. (1999) Biochim.
Biophys. Acta, 1445, 148-53.
2
Visvader, J.E ., Venter, D. , Hahm , K. , Santamaria , M. , Sum , E.Y. , O'Reilly,
L. , White , D., Williams , R. , Armes, J. and Lindeman , G.J. (2001) Proc. Nat/
Acad. Sci. USA , 98, 14452-7.
Sum , E.Y., Peng, B. , Yu , X., Chen, J., Byrne, J., Lindeman , G.J. and3
Visvader, J.E. (2002) J. Bioi. Chern. , 277 , 7849-7856.
4
Jurata, L.W., Kenny, D.A. and Gill , G.N. (1996) Proc. Nat/ Acad. Sci. USA ,93, 11693-8.

125

AMoP-27
CATCHING CATALYSIS IN THE ACT: USING SINGLE CRYSTAL KINETICS
TO TRAP METHYLAMINE DEHYDROGENASE REACTION
INTERMEDIATES FOR STRUCTURAL STUDIES.
Arwen R. Pearson , Teresa De Ia Mora Rey , Kevin T. Watts , Ed Hoeffner. andCarrie M. Wilmot
University of Minnesota , Department of Biochemistry, Molecular Biology &Biophysics , Minneapolis, MN 55455 , U.S.A. (pears079@umn .edu)

Methylamine dehydrogenase (MADH) is an a 2 B2 heterotetramer containing
a novel quinone cofactor, TTQ , derived from two modified tryptophan residues.
It is expressed in response to methylamine, allowing certain bacteria to utilise
methylamine as their sole carbon source. MADH catalyses the conversion of
methylamine to formaldehyde and ammonia, leaving the TTQ cofactor in a 2ereduced state. To complete the catalytic cycle , MADH is reoxidised via two
successive electron transfer (ET) events.
In the case of the Paracoccus denitrificans enzyme (PD-MADH) thephysiologic ET chain involves the protein redox partners amicyanin (a bluecopper protein) and cytochrome c551 i. Stable binary (PD-MADH/amicyanin)
and ternary (PD-MADH/amicyanin/cytochrome c551 i) catalytically competentcomplexes can be formed and crystallized , and their structures have beensolved to better than 2.0A resolution in the laboratory of F. Scott Mathews(Washington University Medical School, St. Louis).
MADH (TTQ) , amicyanin (Cu) and cytochrome c551 i (Fe) have spectralfeatures in the visible region that change during catalytic turnover, thus defining
spectrally distinct intermediates that reflect the electron distribution in thecomplex .
Through a novel combination of single crystal visible
microspectrophotometry, X-ray crystallography and freeze trapping , reaction
intermediates of MADH in complex with the physiological redox partners in the
crystalline state have been trapped .
This poster will present the methods used to monitor and trap reaction
intermediates in the crystalline state , as well as some preliminary X-ray
structural data .

126

AMoP-28
AURACYANIN B STRUCTURE IN SPACE GROUP P6s
Mihwa Lee," Megan J . Maher," Robert E. Blankenship,b Hans C. Freeman ," andJ . Mitchell Guss aaSchool of Molecular and Microbial Biosciences , University of Sydney, NSW
2006 , Australia ; bDepartment of Chemistry and Biochemistry, Arizona State
University, Tempe , Arizona 85287-1604 , USA (m .lee@mmb.usyd .edu .au)

Auracyanin B is one of two similar blue copper proteins produced by thethermophilic green photosynthetic bacterium Ch/oroftexus aurantiacus [1] . It is
likely to be involved in photosynthetic electron transfer in this organism . The
structure of auracyanin B has previously been solved and refined in the
hexagonal space group P6422 with a single molecule in the asymmetric unit
(unit cell parameters a= b = 115.7, c = 54 .5 A) [2] .
The protein has now been crystallized in a new crystal form, P6 5 with unit
cell parameters , a= b = 115.9, c = 108.2 A. In the new crystal form theasymmetric unit contains four protein molecules . The structure has been solved
by molecular replacement and refined at 1.9 A resolution . In relation to theearlier crystal structure , the c-axis of unit cell is doubled and the number ofmolecules is increased from one to four . The main-chain structure of auracyanin
B in P6 5 is very similar to that in P6422 but some residues including those
involved in the crystal contacts have slightly different side chain conformations.
The other interesting feature of this structure in P6 5 is that the operation which
relates two pairs of molecules in the asymmetric unit is very close to a formal
crystallographic two-fold axis , which could yield space group P6 522 . Yet thestructure could be refined only in the lower symmetry space group P6 5_ The final
residuals are R = 19.2% and Rrree = 22.0% .
References
1
McManus , J. D ., Brune , D. C., Han , J. , Sanders-Loehr, J. , Meyer, T . E.,
Cusanovich , M . A., Tollin , G., and Blankenship , R. E. (1992) J. Bioi.
Chem. 267, 6531-40.
2
Bond , C. S. , Blankenship, R. E., Freeman, H. C. , Guss, J. M., Maher, M.
J. , Selvaraj , F. M., Wilce, M. C. J. , and Willingham , K. M. (2001) J. Mol.
Bioi. 306 , 47-67.

127

AMoP-29
THE STRUCTURE OF THE LYSYL OXIDASE FROM PICHIA PASTORIS -A
COPPER-CONTAINING AMINE OXIDASE THAT CAN OXIDISE LYSINECONTAINING PEPTIDES

Anthony P. Duff." Paul J. Ellis ,b Aina E. Cohen ,b Jason A. Kuchar,c David
Langley ," David M. Dooley,c Hans C. Freeman ," and J. Mitchell Guss""School of Molecular and Microbial Biosciences , The University of Sydney,
Sydney Australia ; bThe Stanford Synchrotron Research Laboratory, Menlo Park,
California , USA; cDepartment of Chemistry & Biochemistry, Montana State
University, Bozeman , Montana , USA (A.Duff@usyd .edu.au)
We have determined the structure of the lysyl oxidase from Pichia pastoris(PPLO) at 1.65A resolution with R=16.0% and RFree=18 .7%. Crystals belong tospace group C2 , with a=249A b=120A c=152A and [3=125° [1) . The asymmetricunit contains two dimers , thus providing four-fold non -crystallographic
symmetry. The structure was solved by molecular replacement, despite thesearch model having only a 25% identity match to 66% of the sequence .
PPLO is a copper amine oxidase (CuAO) [2). CuAOs catalyse theoxidative deamination of a primary amine to produce an aldehyde , ammonia
and hydrogen peroxide (R-CH2-NH 2 + 0 2 + H20 -7 R-CHO + NH 3 + HOOH).
They contain Cu(ll} and utilise a side chain derived cofactor that is
autocatalytically generated in the presence of Cu(ll) and 0 2.
PPLO is the fifth CuAO to be structurally characterised , after the CuAOs
from the bacteria Escherichia coli and Arthrobacter globiformis, the yeast
Hansenula polymorpha , and a higher plant Pisum sativum. It is like theprevious four in overall architecture , but has some substantially different
features consistent with its unique ability to oxidise the side chains of lysine
residues in peptides - the initial step in the reactions for the cross-linking ofcollagen and elastin . This functional activity (in vitro) relates PPLO to anotherclass of CuAOs , having a different size , sequence and cofactor, known as the
No bona fide lysyl oxidases have been structurally
lysyl oxidases .
characterised to date.
The structure of PPLO explains its unusual substrate specificity. Other
CuAOs can oxidase only small organic amines , such as methylamine or
benzylamine , but are unable to oxidise lysyl peptides since they have buried
active sites and narrow substrate channels. PPLO on the other hand has abroad open funnel leading from the solvent to the active-site cofactor. We havemodelled putative peptide substrates into this site.
A solvent lake lies between the otherwise tightly associated subunits in the
dimers. This lake is larger in PPLO and borders the ligands of the active site
copper ion . This supports the proposal that the smaller reactants and products(0 2, H20 , NH 3 , HOOH and H+) may enter or leave the active site via this lake.
References
1
Lee M, Willingham K, Langley D, Maher MJ , Cohen AE , Ellis PJ , Kuchar
JA, Dooley DM , Freeman HC, Guss JM. (2002) Acta Crystallogr D. 58,
2177-9 "Crystallization of Pichia pastoris lysyl oxidase"2
Dove JE, Smith AJ , Kuchar J, Brown DE , Dooley DM , Klinman JP.(1996)
FEBS Lett. 398 , 231-4 . "Identification of the quinone cofactor in a lysyl
oxidase from Pichia pastoris"

128

AMoP-30
INSECT CELL EXPRESSION OF A PLANT DISEASE RESISTANCE
PROTEIN Cf-9 FOR STRUCTURAL STUDIES
T . Teh a S. Lang ,b D. A. Jones,b and B. Kobe a

aDepartment of Biochemistry and Molecular Biology, University of Queensland ,St. Lucia , Qld 4072 , Australia ; bPiant Cell Biology, Research School of
Biological Sciences , Australian National University, Canberra, ACT 2601 ,Australia (t.teh@mailbox .uq.edu .au) .

Plants have evolved specific mechanisms to recognise individual
pathogens and activate defence systems . The induction of plant defence
responses , which often include a hypersensitive response leading to rap id
localised cell death at the site of infection , requires the interaction of a plantderived resistance protein (R protein) with a specific pathogen -derived
avirulence protein (Avr protein) [1) . The molecular and structural basis of therecognition events involving most R and Avr protein combinations remains
unknown . It has been postulated that R proteins are receptors for Avr
components [2 ,3] and that R and Avr proteins participate in a complex withother proteins to initiate signal transmission and activate host defence
responses [4,5] .
One well established model in which to study molecular aspects of hostresistance and pathogen avirulence is that of the tomato Cf-9 protein which
confers resistance to the leaf mould fungus Cladosporium fulvum throughrecognition of the fungus encoded Avr9 peptide [6) . Cf-9 is a mainly
extracytoplasmic membrane-anchored glycoprotein, composed predominantlyof leucine rich repeats (LRRs) . LRRs are sequence motifs present in a variety
of proteins involved in protein-protein interactions, including many plant R
proteins ; however, their role in disease resistance is unknown. In an effort toprovide the first structural view of a plant R protein and to extend the present
knowledge of the molecular basis of plant disease resistance , the Cf-9 protein isbeing expressed in insect cells. Through optimisation of expression conditions ,it is hoped to produce adequate quantities of protein for crystallisation trials.
References
Flor, H. (1971) Annu. Rev.Phytopthol. 9, 275-296.
I

2
3
4
5
6

Staskawicz, B.J., Ausubel , F.M. , Baker, B.J., Ellis, J.G., and Jones, J.D.G.
(1995) Science 268, 661-667.
Ellis, J. , Dodds, P. and Pryor, T. (2000) Curr. Opin.Piant Bioi 3, 278-284 .
Dixon , M.S., Golstein , C., Thomas , C.M. , van Der Biezen, E.A. , andJones, J.D.G . (2000) Proc. Nat/. Acad. Sci. USA 97, 8807-8814.
Dangl , J.L. , and Jones, J.D.G. (2001) Nature 411, 826-833 .
Joosten, M.H.A.J. , and De Wit, P.J .G.M. (1999) Annu. Rev.Phytopthol. 37,
335-367 .

129

AMoP-31
THE COMPARISON OF THE LOOP STRUCTURES OF MEMBRANE
BINDING SITES BETWEEN HUMAN AND BOVINE ANNEXINS IV

Michiko Konno , Yae Kanzaki , Kayoko Mochizuki , Nahomi Fushinobu , Ayano
Sato , Kyoko Aikawa , and lsamu Matsumoto
Department of Chemistry, Ochanomizu University, 2-1-1 Otsuka , Bunkyo-ku ,Tokyo 112-861 0 Japan (konno@cc.ocha .ac.jp)
Annexins are a ubiquitous family of structurally related eukaryotic proteinscapable of binding phospholipid membranes in calcium-dependent manner [1].
Membrane binding properties of these proteins have suggested that they are
involved in numerous processes such as exocytosis , endocytosis , vesiculartrafficking , membrane fusion , and ion-channel formation . It has been reported
that annexin I, II and IV proteins aggregate synthetic phospholipid vesicles andchromaffin granules. The mRNA of human annexin IV is highly expressed innormal pancreas , lung and kidney and also in various adenocarcinoma celllines. On the basis of idea that a little structural difference between the loops ofannexi ns , which interact with membranes , should reflect a little difference of
circumstances within vesicles, in order to compare in detail with loop structuresof membrane binding sites of reported bovine annexins IV, we have determinedthe crystal structure of recombinant human annexin IV.
Recombinant human annexin IV was crystallized at 20 °C by a hanging
drop vapor diffusion method. Crystals were grown from a drop of 6mgl ml
protein, 6 % PEG 6000 , 1.5mM CaCb, 3 % dioxane, and 50mM tris-HCI (pH7.5) equilibrated against a reservoir of 20 % PEG 6000 , 20 mM CaCb, 6 %dioxane, and 100 mM tris-HCI (pH7 .5). X-ray data were collected at 100 Kat
Photon Factory (Tsukuba). Crystals adopt the space group P2 1 with lattice
distances of a= 44 .223 A, b = 55.132 A, c = 127.147 A, and ~ = 91.45°. The
structure was solved by molecular replacement and refined to Rractor = 23 .3 %,Rrree = 31.1 % at 2.0 A resolution using XPLOR .
In recombinant human annexin a C-terminal core has four domains each
which fold into five a -helices and an N-terminal "tail region " of fifteen residues(MAMATKGGTVKAASG) lies across the concave protein surface. One cal cium
ion is bound in domain II , two in domain Ill and one in domain IV. Three Ca 2+
ions are bound in type 11-binding sites of AB loop and one in type Ill-binding siteof DE loop. The calcium binding groups of AB loop of domain I coordinate Eamino group of L~ s99 of adjacent molecule . On the other hand , in bovine
annexin IV two Ca + ions are bound in the AB loops of domains I and IV [2] . The
conformation of the AB loop of 184GEKKWGTDEV193 of domain Ill bound Ca 2+
ion of human annexin IV is different largely from that of the corresponding loopof the same residues without Ca 2+ ion in bovine annexin IV. In the former theside chain of Trp188 is intruded out, while in the latter that of Trp185 adopts aburied conformation . In human annexin IV the AB loop of domain II is ordered
and binds Ca 2 + ion , while in bovine annexin IV that is totally disordered anddoes not any binds Ca 2 + ion.
References
I
Gerke , V. and Moss, S. E. (2001) Physiol Rev. 82 ,33 1-371 .
2
Sutton , R.B. , and Sprang , S.R. (1996) in Annexin: molecular structure tocellular function (Seaton , B., Ed) pp 31-42 , R.G .Landes Co ., Austin , TX .

130

AMoP-32
THE CRYSTAL STRUCTURE OF 9-AMINO-[N-(2-DIMETHYLAMINO)PROPYL]ACRIDINE-4-CARBOXAMIDE BOUND TO D(CGTACG)2: A
COMPARISON OF STRUCTURES OF D(CGTACG)2 COMPLEXED WITH
INTERCALATORS IN THE PRESENCE OF COBALT

Adrienne Adams,"· J. Mitchell Guss ," William A. Denny,b and Laurence P.G.
Wakelin c"School of Molecular & Microbial Biosciences, University of Sydney , NSW 2006 ,Australia ; bAuckland Cancer Society Research Centre, Faculty of Medicine and
Health Science, University of Auckland , Private Bag 92019 , Auckland , New
Zealand ; cSchool of Medical Sciences, University of New South Wales , NSW
2052 , Australia (a .adams@mmb.usyd.edu .au)
The structure of the complex formed between an inactive derivative of theclinical trial anti-cancer drug and topoisomerase II poison DACA (9-amino-[N-(2dimethyl-amino)propyl]acridine-4-carboxamide) and d(CGTACG)2 has been solved
and refined to a resolution of 1.55 A. The complex crystallised in space group
C222. An asymmetric unit comprises 2 strands of DNA, one disordered drug
molecule, 2 cobalt (II) ions, 2 disordered magnesium ions and 32 water molecules.
The DNA helices stack in continuous columns with their central 4 base pairs
adopting a B-like motif. The terminal GC base pairs engage in different
interactions. At one end of the duplex there is a CpG dinucleotide overlap modified
by ligand intercalation and terminal cytosine exchange between symmetry-related
duplexes. An intercalation complex is formed involving four DNA duplexes, four
disordered ligand molecules, and two pairs of base tetrads. The other end of the
DNA is frayed with the terminal guanine lying in the minor groove of the next
duplex in the column. The structure is stabilised by guanine N7/cobalt (II)coordination. We compare our structure with the six published structures ofd(CGTACG )2 complexed with intercalators in the presence of cobalt [1-4] and findthem all to be very similar. The seven structures appear to be independent of
biological activity and sidechain configuration and dependent mainly on thepresence of an intercalator and cobalt ions. It is likely that many different
intercalators, besides those discussed here, would be capable of forming a similar
structure with d(CGTACG)2 in the presence of cobalt. lntercalators appear todestabilise B-ONA in the presence of cobalt ions and promote formation ofmultistranded DNA structures. Although we find no evidence for biologicalsignificance of this structure in terms of topoisomerase activity, this does not
exclude the possibility that this is an important property of intercalators which may
have an effect on other biological processes.
References
Adams, A. , Guss , J. M., Collyer, C. A. , Denny, W. A. , Prakash , A. S., andI
Wakelin , L. P. G. (2000) Mol. Pharmacal. 58, 649-58.
Thorpe, J. H., Hobbs, J. R. , Todd , A. K., Denny, W. A. , Charlton , P., and2
Cardin , C. J. (2000) Biochemistry 39, 15055-61 .
Yang , X.-1., Robinson , H. , Gao, Y.-G., and Wang , A. H. J. (2000)
3
Biochemistry 39, 10950-57 .
Teixeira , S. C. M. , Thorpe, J . H., Todd , A. K. , Powell , H. R. , Adams, A. ,4
Wakelin , L. P. G., Denny, W. A. , and Cardin , C. J. (2002) J. Mol. Bioi. 323,
167-71.

131

AMoP-33
STRUCTURAL GENOMICS STUDIES OF MENAQUINONE BIOSYNTHESISPROTEINS FROM MYCOBACTERIUM TUBERCULOSIS: INSGHTS FROMTHE STRUCTURES OF MENG AND MENBJ. M. Johnston , V. Arcus , and E. N. Baker
Laboratory of Structural Biology, School of Biological Sciences , University of
Auckland, Auckland , New Zealand Um.johnson@auckland .ac.nz)

Menaquinone plays an important role in anaerobic electron transport in arange of bacteria . Homologs for the menaquinone biosynthesis pathway genes
can be identified in the genome sequence of Mycobacterium tuberculosis
H37Rv strain. Due to the significance of this pathway in anaerobic conditions,combined with the fact that the menaquinone biosynthesis pathway is notpresent in humans, means these genes may be possible drug targets. Six of theseven homologs of menaquinone biosynthesis genes identified in the
Mycobacterium tuberculosis H37Rv strain genome sequence were chosen forstudy. Cloning , expression tests and refolding experiments resulted in threesoluble proteins. Two of these proteins have been crystallized and theirstructures solved. The 1.9 A trimeric structure of refolded protein Rv3853 ,annotated as the S-adenosylmethionine (SAM) dependent methyltransferase
MenG , revealed no structural similarity to other SAM dependent
methyltranferases and posed questions about the validity of its functionalannotation. The discovery of two small molecules bound in this structure
highlight regions of this protein that may be significant for its function . Unlike
Rv3853 , the structure of Napthoate synthase (MenS) solved to 2.15 A, supports
the suggested annotation and confirms its place as part of the crotonasesuperfamily.

132

AMoP-34
CRYSTAL STRUCTURES OF RESTRICTION ENDONUCLEASE EC001091

Hiroshi Hashimoto, a Tsuyoshi lmasaki ,a Matsuri Kato, 8 Toshiyuki Shimuzu ,8Mamoru Sato ,8 and Keiko Kitab
8

Graduate School of Integrated Science , Yokohama City University, Yokohama ,Kanagawa 230-0045 , Japan ; bGraduate School of Agriculture, Kyoto University,
Uji , Kyoto 611-0011 , Japan (hash@tsurumi.yokohama-cu.ac.jp)

Restriction endonucleases in bacteria recognize and cleave foreign DNA
that is unmethylated. Most of the > 3,000 restriction endonucleases discovered
to date belong to the type II class. The orthodox type II restriction endonucleaseis homodimer, which recognize short and usually palindoromic sequences of
4-B base pairs , and in the presence of Mg 2+ cleaves the DNA within or
immediately adjacent to the recognition site to give a 5'-phospahte and a 3'-0Hend. Although type II restriction endonucleases are widely spread withinbacteria , there is generally no sequence similarity among them . Type II
restriction endonucleases comprise the largest family of functionally related
enzymes , but less known about how their specificity.
The restriction endonuclease , Eco01 091 from Escherichia coli forms
functional homodimer and its molecular weight is 62 kDa. The Eco01 091
monomer is made up with 272 amino acids. Eco01091 recognizes and cleaves
the interrupted DNA sequence of 5'-RGIGNCCY-3' and produces 5'-overhang
DNA. To understand the molecular basis of DNA recognition and hydrolysis ofphosphodiester bond , we have studied crystallographic analysis of Eco01 091.
Crystal of Eco01091 (DNA free) was obtained by hanging drop vapour
diffusion method using polyethylene glycol as a precipitant at 277 K. Crystal of
Eco01 091 (DNA free) belongs to space group of /4 with the unit cell parametersof a = b = 175.5 A, c = 44 .6 A. X-ray diffraction experiments for native datacollection of Eco01 091 DNA free crystals were performed with ACSC Quantum
4R CCD deterctor at BL3BB 1, SPring-B . The intensity data consists of 307,433
measurements of 26,765 unique reflections with an overall Rmerge = 4.2% and99.1% of theoretically observable reflections at 2.4 A resolution. Crystal
structure of Eco01091 was determined by MAD method with mercury derivative
crystal using programs SOL VEIRESOL VE. The three-wavelength MAD data
were collected by Rigaku MSC Jupiter 210 CCD detector at BL45PX , SPring-B.
Crystal of Eco01 091 DNA complex was obtained by hanging drop vapour
diffusion method using polyethylene glycol as a precipitant at 293 K. Crystal of
Eco01 091 DNA complex belongs to space group of P2 1 2 12 1 with the unit cellparameters of a = 71.B A, b = 203.2 A, and c = 49 .1 A. Diffraction intensities ofnative and mercury derivative crystals of DNA complex were collected by
Rigaku R-AXIS IV++ imaging plate detector on Rigaku FR-O rotating anode Xray generator. The native diffraction data consists of 202,201 measurements of
55 ,952 unique reflections with an overall R merge = B.B% and 93.5% of
theoretically observable reflections at 1.9 A resolution. Crystal structure of the
DNA complex was determined by SIRAS method using programs
SOL VEIRESOL VE.
Crystallographic structure refinement of Eco01 091 and DNA complex are
now in progress.

133

AMoP-35
CRYSTAL STRUCTURE OF THERMOSTABLE END0-1,5-a-L-ARABINASE
FROM BACILLUS THERMODENITRIFICANS TS-3

Asako Yamaguchi ," Toshiji Tada ," Tetsuko Nakaniwa," Makoto Takao,b Takuo
Sakai ,b and Keiichiro Nishimura•"Research Institute for Advanced Science and Technology, Osaka Prefecture
University, Sakai , Osaka 599-8570 , Japan; biGA Bioresearch , Amagasaki ,Hyogo 660-0805, Japan (asako-y@biochem .osakafu-u .ac.jp)

Arabinan is a common structural component of plant cell wall s. It consistsof a backbone of a-1 ,5-linked L-arabinofuranosyl residues , some of which aresubstituted with a-1 ,3- and a-1 ,2-linked L-arabinosyl side-chains in the furanose
conformation.
End-1 ,5-a -L-arabinase (ABN) hydorolyzes the a-1 ,5-Larabinofuranoside linkage of arabinan . Thermostable ABN (ABN-TS) from
Bacillus thermodenitrificans TS-3 showed optimal activity at 343 K, and its
thermostability was characterized by a half-life of 4 h at 348 K. We haveinitiated an analysis for the crystal structure of ABN-TS to clarify the structuralfeatures participating in thermostability of ABN.
The recombinant ABN-TS was overexpressed in B. subtilis Ml112. The
purified enzyme was crystallized by using sodium citrate as a precipitant. The
crystals were soaked in a cryo-protectant solution containing 40% sucrose andfrozen in a nitrogen-gas stream at 100 K. A native data set was collected to 1.9
A resolution from a frozen crystal using synchrotron radiation of wavelength 0.9
A at SPring-8. A total of 88876 observed reflections were scaled and reduced
to yield a data set containing 22751 unique reflections with an Rmerge of 8.6%.
The data set was 99.2% complete . The crystals belong to the orthorhombic
space group P212121 with unit-cell parameters a = 40 .2, b = 77 .8 and c = 89.2
A. Molecular-replacement calculations were carried out with the program
AmoRe using the structure of a-L-arabinase 43A from Gel/vibrio j aponicus as asearch model (46% homology). A clear peak was found with a correlation
coefficient of 35.2 and R-factor of 47 .3% after translation-function calculationsin the space group P212 121. Refinement of the model was performed , resulting
in an R-factor of 36.7% and an Rrree of 42.1 %. Manual modifications of themodel structure are currently in progress .

134

AMoP-36
STRUCTURAL BASIS OF LIPID BINDING IN RICE NON-SPECIFIC LIPID
TRANSFER PROTEIN COMPLEXES

Yuh-Ju Sun . Cheng Pei-Tsung , Hui-Chun Cheng , Peiyu Peng , and Ping-Chiang
Lyu
Institute of Bioinformatics and Structural Biology, National Tsing Hua University,
Hsinchu , Taiwan 300 , ROC (yjsun@life.nthu.edu .tw)

Non-specific lipid transfer proteins (nsl TPs) bind to a variety of lipid
molecules and catalyze their transfer across membranes [1]. Other biological
functions for nslTPs also have been proposed such as transfer phospholipids
from liposomes or microsomes to mitochondria [2], transport cuticularcomponents for the biosynthesis of surface wax [3], regulate fatty acid betaoxidation in glyoxysomes [4] and exhibit resistance to avirulent and virulent
pathogens in the plant defense system [5] . Nsl TPs have been isolated frommany plants including wheat, rice , barley, maize, peach , and apricot. NslTPs
are basic proteins (PI 8-1 0), disulfide-rich , with molecular weight 9 and 7 kDa(nsl TP1 & nslTP2) [1]. We report here the crystal structures of rice nslTP1
and fatty acid complexes have been determined by X-ray crystallography. We
suggest that the structural plasticity of nslTP1 manages the lipid binding in therice nslTP1 lipid complexes. The tunnel-like hydrophobic cavity inside nslTP1
provides a space large enough to accommodate a long fatty acyl chain. The
hydrophobic and hydrophilic interactions from three key residues , Arg44, Try79
and lle81, were contributed in the lipid binding.
References
I
Kader, J.C. , (1996) Annu. Rev. Plant Physiol. Plant Mol. Bioi. 47 ,627-654.
2
Breu , V., Guerbette, F. , Kader, J. C., Kannangara , C. G ., Svensson , B. &Wettstein-Knowles , P. (1989). Carlsberg. Res. Commun. 54, 81-84.
3
Sterk, P., Booij, H. , Schellekens, G. A. , Van Kammen , A. & De Vries, S.C .
(1991) . TheP/antCe/13 , 907-921.
4Tsuboi , S. , Osafune , T. , Nishimura , M. & Yamada , M. (1992). J. Biochem.
111 ' 500-508.
5
Maldonado , A. M. , Doerner, P. , Dixonk, R. A., Lamb , C. J. & Cameron , R.
K., Nature (2002) 419, 399-403.

135

AMoP-37
REFINEMENT OF THE 7/2-AND 10/3-HELICAL STRUCTURES BASED ON
THE FIBER DIFFRACTION PATTERN FROM NATIVE COLLAGEN
K. Okuyama, X. Xu , and K. Noguchi
Faculty of Technology, Tokyo University of Agriculture and Technology,
Koganei, Tokyo 184-8588, Japan (okuyamak@cc.tuat.ac.jp)
After fifty years since the first proposal of a triple helical structure , there arestill two models for collagen with different helical symmetry and different fiber
repeating period. One is the Rich and Crick model in which three strands form aleft-handed 10/3-helix with an axial repeat of 28.6A [1] . The other is our model inwhich three strands form a left-handed 7/2-helix with an axial repeat of 20A [2] .
The latter model was strongly supported by single crystal analyses of several
collagen model peptides reported so far. On the other hand , the former model has
no such supporting data other than the fiber diffraction analyses of poly(Pro-GiyPro) [3] and native collagen [4]. Since the quality of fiber diffraction pattern frompoly(Pro-Giy-Pro) was very poor compared with that from native collagen , theformer analysis is not a powerful supporting evidence for the 10/3-helical model.
On the other hand , in the latter analysis , only the 10/3-helical structure was refinedby using continuous layer intensities. In this study, we refined both 7/2- and 10/3helical structures by using continuous X-ray diffraction intensities on the layer lines
corresponding to their axial repeat.
The fiber diffraction pattern from kangaroo tail tendon was taken by usingsynchrotron radiation (BL4082, SPring-B) and recorded on an imaging plate(RAXISIV++, Rigaku) . The background subtraction and acquisition of continuous Xray intensities on the corresponding layer lines were performed by using CCP13
softwares. According to the recent single crystal analyses of collagen model
peptides at high resolution, in most of the cases, there are water molecules boundto the carbonyl oxygen of Gly and Pro, and those to the hydroxyl oxygen of Hyp.
Therefore , some of these water molecules were also included in the triple helicalstructures. Refinement calculation was performed by WinLALS , Windows versionof Linked-Atom Least-Squares (LALS) program for fiber diffraction analyses.
In both models , triple-helical structures with no bound water molecules gave
fairly high discrepancy (R-) factor (-0.40) compared with that (0.27) of the previous
analysis [4] . Although Pro-Hyp-Giy triplet was taken as a helical asymmetric unit,
occupancies of Cy, Co and Oo atoms of imino acids were reduced to 1/3 according
to the imino acid occurrences in the amino acid sequence of tendon collagen,which decreased R-factors by several percent. Furthermore, addition of watermolecules decreased R-factors to 0.25 (7/2-helix) and 0.30 (10/3-helix). This fairly
large improvement of the discrepancy factor by addition of water molecules was
also experienced in many single crystal analyses of collagen model peptides. The
obtained result showed that the 7/2-helical model can explain fiber diffraction
patterns from native collagen better than , or at least as well as, the 10/3-helicalmodel can do.
References
I
Rich , A. and Crick, F.H.C. (1961) J. Mol. Bioi. 3, 483-506.

2
3
4

Okuyama , K., Takayanagi, M., Ashida , T. and Kakudo, M. (1977) Polymer J. 9, 34 1-343.
Yonath, A. and Traub, W. (1969) J. Mol. Bioi. 43 , 461-477.
Fraser, R.D.B. , MacRae. T.P. and Suzuki , E. (1979) J. Mol. Bioi. 129 , 463-481

136

AMoP-38
INTERSUBUNIT SALT BRIDGES AND OLIGOMERIZATION DO NOTCONTRIBUTE TO THE HIGH THERMAL STABILITY OF A
HYPERTHERMOPHILIC PROTEIN FROM PYROCOCCUS FURIOSUS
Jai K. Kaushik," Yuriko Yamagata ,b Kyoko Ogasahara ,c and Katsuhide YutanidaMolecular Biology Unit, National Dairy Research Institute, Karnal132001 , India;
bGraduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto,Japan; clnstitute for Protein Research , Osaka University, Japan ; dKwansei Gakuin
University, Sanda City, Hyogo, Japan Uaik@ndri.hry.nic.in)Electrostatic interactions play an important role in the extraordinary highstability of proteins from hyperthermophilic organisms. These proteins contain large
number of ion pairs forming complex networks. However, due to large desolvation
penalty involved in formation of salt bridges and consequent burial in between theinterfaces, their contribution to extraordinary high stability of hyperthermophilicproteins has been controversial. There are numerous experimental results insupport as well as opposing the significant role of salt bridges in protein stability.
Pyrrolidone carboxyl peptidase (PCP) from Pyrococcus furiosus is a
homotetramer and considered to be stabilized by several salt bridges at theinterface of subunits which could eventually be responsible for oligomerization. Its
melting temperature is above 107°C at pH 7. To elucidate the role of inter-subunit
salt bridges in the stabilization mechanism of proteins, the following mutants weregenerated and expressed in E. coli: R80AIK118A (1M2), 087 AIE99AID1 OOA (1M3),
and R80AIK118AID87AIE99AI D100A (IM5). Subunits A and B, and subunits C
and D are located diagonally opposite. The salt bridges in PCP are located atinterfaces between subunits A and D and subunits B and C; whereas, theinterfaces between A and C, and B and D are strengthened mainly by hydrophobic
interactions and some salt bridges. The sedimentation analyses showed that
disruption of salt bridges affect the molecular assembly of the mutants. At pH 3 and
3.8 , PCP exists in dimeric and tetrameric forms, respectively, whereas the ionicmutants are close to monomeric form at both the pH values. It indicates thatalteration of electrostatic interactions at one interface also affects the interactions
at the other interfaces. There seems a cooperativity of interactions forming at two
different interfaces. The formation of dimer and tetramer in ionic mutants takes
place at pH 4.4 and above 5, respectively. DSC results indicated that disruption ofsalt bridges led to changes in thermal stability. The stability of 1M2 (basic residues
replaced) decreased in the acidic as well in the neutral zones, whereas it increased
for 1M3 (acidic groups replaced) in these regions; the stability of IM5 seemed to be
resulting from the additive effect of removal of basic and acidic groups. In theregion near pH 4, all these mutants were more stable than PCP. X-ray structure
analyses indicated that Asp87, Glu99 and Asp1 00 on one subunit are located very
closely causing considerable repulsion among themselves and thus offsetting thecontributory effect due to pairing with Arg80 and Lys118 on the adjacent subunit.
Whereas Arg80 and Lys 118 are well separated and removal of these residues
leads to a decrease in stability due to not only breaking of salt bridges but also
because it leaves the acidic residues at position 87, 99 and 100 unpaired andhence more repulsive. Results indicate that assembly form does not have a direct
relation with the stability of PCP. This could be because the positive effect ofoligomerization is offset by negative effect of desolvation of charged groups due toburying in between the interfaces.

137

AMoP-39
STRUCTURAL CHARACTERISATION OF THE INI OPERON OF
MYCOBACTERIUM TUBERCULOSIS

J. Shaun Lott,a Moyra M. Komen ,a Tet Verne Lee," Clare Scott,a Joel McKay,b
Edward N. Baker,a and Vickery L. Arcusa
alaboratory of Structural Biology , School of Biological Sciences, University of
Auckland , Private Bag 92-019 , Auckland 1020, New Zealand ; bSchool ofMolecular and Microbial Biosciences , University of Sydney, NSW 2006 ,Australia (s.lott@auckland .ac.nz)

Isoniazid(INH) is the primary antibiotic used in the treatment of

M. tuberculosis infection. INH asserts its

toxic activity on the bacterium by
Rv0340inhibiting the biosynthesis of cell wallmycolic acids, rendering it susceptible toreactive oxygen radicals and otherenvironmental factors [1] .
Rv034 1
ORFs from the ini operon haveiniB
been identified by DNA microarray [2]
PATMH
and differential mRNA expression
studies as being strongly upregulated by
Rv0342
in/A
INH and to a lesser extent byethambutol (EMB), another antibiotic
that also inhibits cell wall biosynthesis.
Rv0343
These observations imply that this geneiniC
cluster may be important for bacterial
400
200
600
cell viability when membrane integrity iscompromised by cell wall biosynthesis
inhibitors. None of the ORFs in this cluster show informative amino acid sequencesimilarity to any other proteins, and their biochemical functions remain unknown.
However, they show clear conservation with each other in particular segments of
their sequences (see figure) , which implies that they share conserved structural
domains.
We have defined structural domains in iniA, iniC and iniD using a
combination of sequence analysis, limited proteolysis, mass spectrometry andamino acid sequencing . The structure of the folded domain from iniD is currently
being pursued using high-field heteronuclear NMR spectroscopy, and diffracting
crystals have been obtained of the conserved domain shared by iniA and iniC.
Results of these structural analyses will be presented , which may enablebiochemical functions to be assigned to these proteins to explain their physiologicalroles in antibiotic response.
References
I
Rattan , A., Kalia, A. and Ahmad , N. (1998) "Multidrug-resistant
Mycobacterium tuberculosis: Molecular Perspectives." Emerging Infectious
Diseases 4, 195-209.
Wilson , M. eta/. (1999) "Exploring drug-induced alterations in gene2
expression in Mycobacterium tuberculosis by microarray hybridization."
PNAS 96, 12833-12838 .

; 34%1138

II

AMoP-40
STUDIES OF PROTEINS OF THE FOLATE BIOSYNTHESIS PATHWAY

Jacqueline F. Satchell, Brian J. Smith, Jonathan Baell , and Peter M. Colman
The Walter and Eliza Hall Institute, Structural Biology Division . 1G Royal
Parade , Parkville, Victoria , 3050, Australia (satchell@wehi.edu.au).
Organisms parasitic upon humans , such as Plasmodium andPneumocystis , are responsible for some of the world 's major health problems.
These infections have commonly been treated with a class of compounds
known as antifolates[1]. These inhibitors block the enzymes of the folate
biosynthesis pathway causing decreased pyrimidine synthesis resulting in
reduced DNA , serine and methionine formation , ultimately resulting in growth
inhibition[2].
The structures of several prokaryotic folate biosynthesis enzymes areavailable , and allow for preliminary hypotheses to be drawn regarding likely
inhibitors of this pathway. Docking experiments have been conducted in orderto determine whether DHP-analogues , previously shown in E. coli to be formedby the consensation of the substrate DHPP with sulfa drugs (shown in figure 1),
are capable of inhibiting this pathway . These compounds have been chemicallysynthesised and have shown to have activity against dihydrofolate reductase(DHFR) in yeast[3] .
natural substrate

OHPS

-

0

g<>o

~ HN~Ny,..'v'U ' NHf
J,Jl)

0

H,N-o-~-NHR

H2N

N

~

H

su lfa-OHP

0sulfa drug

Figure 1 - Formation of DHP-analogues in vivo.

Pneumocystis carinii combines enzymes of this pathway in a moreelaborate protein complex , the FAS protein , which incorporates
hydroxymethyldihydropterin pyrophosphokinase (PPPK) , dihydroneopterin
aldolase (DHNA) and DHPS. Existing prokaryotic structures have also provided
useful information with regards to the design of constructs for expression of thisprotein in insect cells. The structure of this protein will provide useful
information from which drugs can be designed to target parasitic organisms.
References
1
Olliaro ,P., Cattani , J. and Wirth , D. JAMA. 1996, 275, 230-234.
2
Volpe, F., Ballantine, S.P. and Delves , C.J. Eur. J. Biochem. 1993 , 216 ,449-458.
3
Patel 0. , Satchell J.F., Coloe P., Baell J. and Macreadie I. Microbial Drug
Resistance. Accepted for publication in 2003 .

139

AMoP-41
IDENTIFYING ANTAGONISTS TOWARDS A G-PROTEIN COUPLED
RECEPTOR USING THE STRUCTURE OF A HORMONE COMPLEXED TO A
NEUTRALISING MONOCLONAL ANTIBODY

Gal ina Polekhina ,"· William J. McKinstry,"· Hannelore Diefenbach-Jagger,aPatricia W. M. Ho, 8 Craig J. Morton,a Koh Sato ,b Etsuro Onuma ,b Matthew T.
Gillespie,aT. John Martin ,8 and Michael W. Parker88
St. Vincent's Institute of Medical Research , 9 Princes Street, Fitzroy, VIC 3065 ,Australia ; bPharmaceutical Research Laboratory , Chugai Pharmaceutical , 1-135
Komakado , Gotemba , Shizuoka , 412-8513 Japan(galinap@medstv.unimelb.edu.au)Both authors contributed equally to the work

G-protein coupled receptors (GPCR) are the most common receptor classin humans controlling critical cell functions and are thus an important class ofdrug targets . They are notoriously difficult to over-express and crystallize , andto date only one high resolution structure (bacterial rhodopsin) is available. We
present a promising new method for discovering GPCR agonists andantagonists using structures of GPCR ligands bound to antibodies.
Parathyroid hormone related protein (PTHrP) was discovered as a
hypercalcemia-causing factor of malignancy [1]Under normal circumstances
PTHrP plays a key role in regulating embryonic development of the skeleton
and other tissuesPTHrP as well as parathyroid hormone (PTH) act upon thesame GPCR , parathyroid hormone receptor (PTH-R) . PTHrP has also beenshown to be one of the main culprits of metastasis into bone of human breast
cancer cells causing bone breakdown.We have crystallized and determined thestructure of the complex between PTHrP and a neutralizing monoclonal
antibody. The humanised version of this antibody is currently in clinical trials(Phase II) in Japan for treatment hypercalcemia , bone metastasis and cachexia[2] . The structure revealed that the residues of PTHrP involved in the interaction
with the antibody are either strictly conserved among PTH and PTHrP
sequences or have been implicated in the binding to the receptor. We therefore
predicted that the binding pocket on the antibody resembles the receptor's.
Using the structural data , we will screen the large library of small "drug-like"molecules for the best fit into the PTHrP binding pocket of the antibody. The top
hits will be screened in cellular assays for inhibition towards action of PTHrP on
PTH-R. The structural biology results and those from the computational screen
and cellular assays will be presented.
References
I
Martin , T. J. (2002) The Journal of Clinical Investigations. 10, 1399-1401.
2
Sato , K. (1999) The Seventh International Forum on Calcified Tissue andBone Metabolism. 32-37 .

140

AMoP-42
RECENT DEVELOPMENTS AT ASRP X-RAY DIFFRACTION FACILITIESJames R Hester, and David Cookson
ANSTO , PMB 1, Menai , NSW 2234 , Australia Qrh@anbf2.kek.jp)

The Australian Synchrotron Research Program (ASRP) has been
operating a high throughput Debye-Scherrer powder diffractometer at theAustralian National Beamline Facility (ANBF) in Tsukuba , Japan , for almost 10
years. The unique design of the instrument enables rapid collection of multiple
datasets in which one or more experimental parameters are varied , forexample , wavelength or temperature . The ANBF has offered as standard a
modular furnace giving a temperature-controlled environment in the 400-1 OOOK
range , with user-constructed furnaces reaching almost 1400K. Recently, acommercial Joule-Thompson refrigerator has been acquired for flat
plate/capillary experiments in the 80-500K range . Early results from this device
are presented together with information on availability for general use in theupcoming (October) beamtime cycle.
The ChemMatCARS project at the APS in Chicago , of which the ASRP isa member, offers micro-crystal single-crystal diffraction using a Bruker CCD
area detector with cryostream cooling and a turnkey data collection andprocessing system. Publishable structures are routinely obtained from crystals
with average dimension < 50 microns and data collection times of around 6-8hours. Typical results from this system are presented [1].
Access to the ANBF is normally by peer-reviewed proposal [2]; users witha small number of powder samples may submit them for 'ad-hoc' data collection
by beamline staff [3] . The ASRP offers the SCrAPS service for microcrystal datacollection at the APS [4].
References
I
Smyth , D. R. , Hester, J., Young , V. G. and Tiekink, E. R. (2002)
CrystEngComm, 517-521 .
2
http://www.ansto.gov.au/natfac/asrp1 001.html
3
http://www.ansto.gov.au/natfac/ANBF/adhoc_final.html
4
http://www.ansto.gov.au/natfac/scraps.html

141

AMoP-43
COMPARISON OF THE FR-E AND RU-H2R X-RAY SOURCES FOR
PROTEIN CRYSTALLOGRAPHY APPLICATIONS

Karl A. Byriela, Anna Aagaard a, Christine L. Geea, Nirajali Gamage ,b andJennifer L. Martina
alnstitute for Molecular Bioscience , The University of Queensland, QLD 4072
Australia ; bDepartment of Physiology and Pharmacology, The University of
Queensland , OLD 4072 Australia (k.byriel@imb.uq .edu .au)

The FR-E Superbright rotating anode generator was designed as a
successor to the FR-D generator. It provides a high brilliance focal spot, 2.0 kW
at 0.07 x 0.07 mm compared to the traditional home source RU-H2R or RUH3R focal spot 5.0 kW at 0.3 x 3 mm or the FR-D focal spot 3.5 kW at 0.1 x 0.1
mm or 5.0 kW at 0.15 x 0.15 mm. The FR-E has the advantage of lower
maintenance and easier handling than the FR-D .
Preliminary data will be presented for the comparison of the RU-H2R
rotating anode generator and MSC Confocal Blue-3 optic against the FR-E
Superbright generator with both MSC Confocal HiRes 2 and MaxScreen optics .
Data in both cases are measured on an R-AXIS IV++ detector and thecryocooling apparatus is the same in each case , the Cryolndustries Cryocool
NFC 1259 XRD.
We will present the results of characterization of the physical properties of
the X-ray beam and data sets collected on the same small frozen lysozyme
crystal from these systems . Results will also be presented for other protein
crystal samples as they become available .

142

AMoP-44
EVALUATION OF MICROSTRUCTURE PARAMETERS FROM POWDER
X-RAY DIFFRACTION DATA
Takashi Ida , and Hideo Toraya
Ceramics Research Laboratory, Nagoya Institute of Technology , Asahigaoka ,Gifu 507-0071 , Japan (ida@crl.nitech.ac.jp)
Recently, we have developed a new method to deconvolute instrumental
aberrations from powder X-ray diffraction data [1]. The effects of spectroscopic
distribution of the source X-ray, axial divergence, flat specimen and sample
transparency are all eliminated by a fast Fourier transform calculations. As
compared with the conventional method of Stokes [2], our method is advantageousat the following points: (i) no measurement of reference sample is needed , (ii)integrated peak intensity is strictly conserved or properly corrected after thedeconvolution , (iii) the systematic peak shifts are automatically corrected , (iv) thewhole diffraction data are simultaneously treated no matter how complicated thepeak pattern may be, and (v) the propagation of statistical errors is properly
evaluated . Those features are particularly useful for evaluation of microstructure
parameters, the finite crystallite size and amount of structural defects in crystallites.
We have also developed an advanced algorithm for numerically evaluating
the theoretical diffraction peak profile from spherical crystallites with log-normal size
distribution (SLN profile) [3]. The algorithm efficiently evaluates the precise model
profiles even for ex1remely broad size distribution , while the method originallyproposed by Langford et a/. [4] and a modified version of Papa and Balzar [5] areonly applicable to restricted widths of distribution . Curve fitting analysis based on
the SLN profile model provides a simple way to estimate both mean and width ofcrystallite size distribution from each of experimental diffraction peak profiles .
Our original methods are applied to estimate microstructure parameters of afine SiC powder sample (JFCC, RP-2). The deconvolution of the instrumental
aberration from experimental powder X-ray diffraction data has revealed the
intrinsic 'super-Lorentzian' line shape [6], which is characteristic of the SLN profilefor broad size distribution. The logarithmic standard deviation of the distribution isestimated at 0.93(3) , wh ich is in good agreement with the value 0.97 estimated bya laser diffraction method . It is also shown that the anisotropic features in shifts ofthe peak positions and also variation of the peak widths dependent upon the Miller
indices indicate the existence of deformation-type stacking fault along 111direction , the frequency of which is estimated at about 0.005(1) based on thePaterson's model for stacking faults [7] .

References
1
Ida , T. and Toraya , H. (2002). J. Appl. Cryst. 35, 58-68.
Stokes, A. R .. (1948) . Proc. Phys. Soc. London 61 , 382-393.
2
Ida , T. , Shimazaki, S. , Hibino, H. and Toraya , H. J. Appl. Cryst. (submitted).
3
4
Langford , J. 1. , Lauer, D. and Scardi , P. (2000). J. Appl. Cryst. 33, 964-974 .
Papa , N.C. and Balzar, D. (2002). J. Appl. Cryst. 35, 338-346.
5
6
Wertheim , G. K., Butler, M.A. , West, K. W. and Buchanan , D. N. E. (1974).
Rev. Sci. lnstrum .. 11 , 1369-1371 .
Paterson , M. S. (1952). J. Appl. Phys. 23 , 805-811 .
7

143

AMoP-45
THEORETICAL AND EXPERIMENTAL STUDY OF THE NEWEST HIGH
BRILLIANCE ROTATING ANODE GENERATORS AND CMF OPTICS
K. F. Tesh ," A . R. Criswell ," C. Yang ," D. A. Courville," J. D. Ferrara ,8 M.
Kuribayashi ,bB. Verman ,c and L Jiangc
8

Rigaku/MSC, Inc. , 9009 New Trails Drive , The Woodlands, TX 77381 , USA;bRigaku Corp ., 3-9-12 Matsubara-Cho, Adisima-Shi , Tokyo 196, Japan ; cosmic,
Inc., 1900 Taylor Rd ., Auburn Hills, Ml 48326 USA (kft@RigakuMSC .com)

The synergistic match of microfocus cathode technology, state of the art
anode development, and confocal optics has produced a new generation of Xray sources unequalled in performance. But, does all this extra flu x, now
available in the home lab , really add to the capabilities previously only
accessible at synchrotron sources?
A careful study of the added flu x benefit for a series of new generators andoptics will be presented . It will be shown that recent data improvements have
led to consideration of collecting high resolution data sets at home, and withmore ease . Flux measurements and real datasets support these revolutionary
advances. Data sets from smaller and more poorly diffracting crystals can now
be attained without a trip to the synchrotron.

144

AMoP-46
PHASE TRANSITION OF LANTHANUM TITANATE PEROVSKITES

Masatomo Yashima ,• Mizuki Mori ,8 Koh Saitoh ,8 Kenji Tsuda ,b Takashi
Kamiyama ,c Ken -ichi Oikawa ,c Akinori Hoshikawa,c Shuki Torii ,d Masahiko
Tanaka ,0 Takeharu Mori ,° Ken-ichi Kato ,e Shinobu Aoyagi ,e Masaki Takata ,' and1
Eiji Nishibori
8

Department of Materials Science and Engineering , Interdisciplinary Graduate
School of Science and Engineering , Tokyo Institute of Technology, 4259
Nagatsuta-cho, Midori-ku , Yokohama , 226-8502 , Japan; blnstitute ofMultidisciplinary Research for Advanced Materials, Tohoku University, Sendai
980-8577 , Japan; 0 lnstitute of Materials Structure Science , High Energy
Accelerator Research Organization , 1-1 Oho , Tsukuba , lbaraki , 305-0801 ,Japan; dSatellite Venture Business Laboratory , lbaraki University, 4-12-1 , NakaNarusawa-cho , Hitachi, lbaraki, 316-8511 , Japan; eSPring-8, JASRI , 1-1 -1
Kouto , Mikazuki-cho , Sayo-gun , Hyogo 679-5198 , Japan; 'Department ofApplied Physics Graduate School of Engineering , Nagoya University Chikusaku , Nagoya , 464-8603, Japan (yashima@materia .titech .ac.jp)

La2,3Ti0 3-based compounds with an A-site deficient perovskite-type
structure AB0 3 are attractive materials with high ionic conductivity at hightemperatures and dielectric constants where A =La2/3±y. B=(Ti 1-x.Mx) and M isdopant cation . Despite of the importance of many perovskite-related oxides athigh temperatures , only a limited number of accurate high-temperature
structural studies have been performed . The Laos4(Tio92, Nbooa)03 andLa 0.68 (Ti 0.95 ,A1 0.05 )0 3 compounds were reported to exhibit a structural phasetransition between the orthorhombic (Prnrnrn) and tetragonal (P4/rnrnrn) phases
at 623 K and 643 K, respectively [1 ,2] . However, the Rietveld analysis of the
low-temperature phase has been carried out by an invalid space group Prnrnrn ,ignoring small diffraction peaks as shown in the present paper. Furthermore ,the previous Lao.s4(Tio92, Nbo.oa)03 sample included a small amount of impurity
phases of LaTiNbOs and La2Ti 20 7. The present paper reports new data on theevolution of the crystal structure of high-purity Laos4(Tio92, Nbooa)0 3 at hightemperatures . High-resolution neutron and synchrotron powder diffraction
measurements are carried out to determine the temperature dependence of
positional parameters. Neutron , synchrotron and electron diffraction analyses
indicate that Lao.s4(Tio.92, Nb 008 )0 3 compound has Crnrnrn space group at room
temperature . We report for the first time that the tetragonal (P4/mrnrn)-toorthorhombic (Crnrnrn) phase transition in Lao64(Tio92, Nbooa)03 is induced by
the tilt of oxygen octahedron around Ti and Nb atoms. The angle of the tilt andthe b/a ratio of cell parameters decrease with an increase of temperature andbecome 0 deg. and unity, respectively, at a transition temperature between 534
and 637 K.
References
1
Ali , R. , Yashima , M., Tanaka , M. , Yoshioka , H., Mori , T. and Sasaki , S.
(2002) J. Solid State Chern. 163, 51 -59.
2
Yashima , M., Ali , R. , Tanaka , M. and Mori , T. (2002) Chern . Phys. Lett.
363 , 129-133.

145

AMoP-47
PRECISE MEASUREMENT OF THE LATTICE SPACING OF LaBs
STANDARD BY POWDER DIFFRACTION AND THE X-RAY EXTENDED
RANGE TECHNIQUE USING SYNCHROTRON RADIATION
C. T. Chantler,8 Z. Barnea ,8 C. Q . Tran ,8 and D. J. Cooksonb
8

School of Physics, University of Melbourne , Parkville , Vic 3010 , Australia;bANSTO, Private Mail Bag 1, Menai , NSW 2234 and Chem-Mat-CARS-CAT(Sector 15, Bldg 434D), Argonne National Laboratory, 9700 S. Cass. Avenue ,Argonne, IL 6043 (chantler@ph.unimelb.edu.au)Some 20% of Australian synchrotron usage involves powder diffraction ,particularly of micro-crystalline organic and inorganic samples for biomedical
and chemical structure determination . A similar percentage applies to world
synchrotron usage. While structures can often be reliably determined directlyfrom the diffraction patterns using Rietveld and other methods , resulting errors
often depend upon the errors of calibrating standards which should be used in
the measurement.
We used the X-ray Extended-Range Technique [1] to measure the latticespacing of LaBs standard powder samples relative to silicon standard powder
samples with an accuracy of 0.4 eV. Measurements were carried out over a 5
keV- 20 keV energy range [2]. Hence the determination was not constrained to
one energy . These measurements used powder diffraction to determine thesynchrotron beam energy; to determine beam divergence ; and to correct thenominal calibrated beam energies. Discrepancies in nominal beam energies
often create difficulties in interpretating aspects of the structural evaluation , andcan involve corrections of 100 eV or more . This technique provides a result
independent of certain energy-dependent systematics and yields the mostaccurate determination of the lattice spacing of LaBs so far undertaken .
References
I
Chantler, C. T., Tran , C. Q. , Paterson , D., Cookson , D. and Barnea , Z.
(2001) Phys. Lett. A286, 338-346.
2
Chantler, C. T., Tran , C. Q. , Barnea , Z., Paterson , D. , Cookson , D. andBalaic, D.X. (2001) Phys. Rev. A64, 062506-1 -15 .

146

AMoP-48
ANALYSIS OF THE DEPTH DEPENDENCE ON THE POLY -CRYSTALSTRACTURE NEAR THE SURFACE BY THE USE OF SCATTERED X-RAY
AT SMALL GLANCING ANGLE INCIDENCE

Y. Fujii ,a A. Tao ,a T. Komai ,a and K. lkedab
aFaculty of Engineering , Kobe University, Rokkodai , Nada , Kobe 657-8501 ,Japan; bMaterials Research Laboratory, Kobe Steel , Ltd., Nishiku, Kobe 651 ,Japan (fujiiyos@kobe-u.ac.jp)

New analyzing method for evaluating the poly-crystal structure near thesurface using X-rays at small glancing angle incidence was studied . When Xrays are applied to the material surface at a grazing angle of incidence , theintensity of X-rays scattered on the surface is the sum of the X-rays thatscattered by the atoms only on the surface, ca. several ten atomic layers deep,
and the contribution of the atoms of each depth to the X-rays intensity varies on
the incidence angles . Since the penetration depth of X-rays changes bychanging an incidence angle , a structural change of the depth direction of amaterial surface layer can be known in analyzing incidence angle dependenceof the information that the scattered X-rays have. So the intensities of thescattered X-rays were measured continuously at the various incidence angles,
and the dependency of the incidence angles was analyzed. The small glancing
angle X-rays scattering on polycrystalline iron surface were measured by usingsynchrotron radiation at Hyogo Prefecture beam line BL24 of SPring-8 . The
polycrystalline surface of pure iron (ferrite , 3nines purity) was mechanicallypolished and annealed at 400 degrees for 5 minutes. The pre-heating forms athin amorphous oxide layer on the iron surface . Angular distributions of thescattered X-rays intensities were measured at several glancing angle
incidences of 1OkeV X-rays . X-rays diffraction patterns in the direction parallelto the surface at the several incident angles of the X-rays show that the peakintensity corresponding to Fe 20 3 is large at an incident angle of 3. 5mrad anddecreases at a larger incident angle , and show that the peak intensity
corresponding to Fe 304 is large at an incident angle of 5.1mrad and decreases
at a larger incident angle, and show that the peak intensity corresponding to Fe
increases at a larger incident angle . Analyzing these intensity profiles as thefunction of the incident angle leads to the contribution of the atoms of each
depth under the surface. The result of this experiment was analyzed with somesurface structure models. Based on these results , we propose a new method of
surfa ce characterization ; a depth profile of the surface structure can bedetectable by this measurement technique .
References
Fujii, Y., Tao , A. , Ikeda, K. , Kusumi, Y., Yanase, E. and Nishio, K. (2001)
1
Proc. ALC01 , 267-270.

147

AMoP-49
THE USE OF PARENT SYMMETRY TO IDENTIFY SPACE GROUPOPTIONS FOR TWINNED/DISORDERED PSEUDO SYMMETRIC CRYSTALSTRUCTURES
A. David Rae

Research School of Chemistry, The Australian National University, Canberra ,ACT 0200 , Australia (rae@rsc.anu .edu.au)
Reflections of many modulated structures can be described as.!::! =§. +mg where §. is a subset of reflections that are strong and can be described by aparticular index condition . A parent structure description based on the Fouriertransform of these reflections alone is necessarily disordered , but may beapproximated using a space group with a higher point symmetry than the true
structure . The identification of this symmetry allows a logical assessment of thepossible twinnings , stacking faults , site symmetries and space groups that may
be initiated by different orderings of this parent structure. The symmetry ofcoherent substructures can be identified , reducing the range of possibilities.
Algebra for the combination of structure factors for ordered substructures canbe used for constrained refinement.
Alternative stackings of substructures allows the possibility of polytypes
and indeed crystals containing coherent blocks of structure of different spacegroups and different orientations [1) .
Twinning allows the overlay of systematic absences and presences . The
true symmetry may induce displacements from the idealised parent symmetry
and corrupt the absences and diffraction symmetry of the idealised parent
structure . However the use of symmetrised components derived using
irreducible representation theory can identify a hierarchy for model
development. An example [2) is the low temperature structure obtained by anon destructive phase transition from a P4/ncc room temperature structure . The
cell volume doubles and P4/ mmm diffraction symmetry is maintained . A
knowledge of the options allowed a twinned Pnca / Pcnb structure to be
determined .
Absences allowed a twinned Pcna! Pncb option imposing different site
symmetries but indistinguishable absences. Stacking faults would lower thesymmetry and the intensity of the extra reflections . A description of the various
options will be given.
References
I
Rae, A. D, and Willis , A. C. (2003) Z. Krist. 218 , 221-230.
2
Sugiyarto, K. H., McHale, W. A. , Craig , D. C., Rae, A. D., Scudder, M. L.,
and Goodwin , H. G. (2003) lnorg Chern. accepted .

148

AMoP-50
PHASE TRANSITION AND STRUCTURE OF CsH2oNX•nCH4N2S (X=I, Br, Cl,
n=2, 4, 5)

H. lshigami ," M. Sumita ,a Y. Tsunashima ,a S. Sato ,a M. Shiro ,b and T. Hikitac
aFaculty of Engineering , Shibaura Institute of Technology , Minuma , Saitama
330-8570 , Japan; bX-ray Research Laboratory, Rigaku Corporation, Akishima ,Tokyo 196-8666, Japan ; cSchool of Engineering , Tohoku University, Aoba ,Sendai , Miyagi 981-8579 , Japan (ishigami@sic.shibaura-it.ac.jp)

The title compounds CsH2o NX•2CH4N2S (X=I , Br, Cl) were prepared byaddition of thiourea to tetraethylammonium salts . The crystal CaH2oNI•2CH4N2S
undergoes a phase transition at 288K . The structure at room temperature
belongs to orthorhombic system with the space group lbca ; the low temperaturephase is orthorhombic Pccb. Both phase are centric. Large differences of thecell dimensions were not found between both phases . The structure consists ofthe tetraethylammonium cations , iodide anions and thiourea molecules . No
short contacts other than van der Waals ones are observed. The maindifference between both structures is that the cations show a disorderedarrangement at room temperature whereas they are ordered in the lowtemperature phase. The disordered cation statistically occupies two sites
relating the two-fold rotation axis with one-half occupancies each. Very recently
we have determined the crystal structure of CaH2oNI•2CH4N2S at 300K. The
dimensions are a=11 .5447(5) A, b=22.605(1) A, c=15 .1038(6) A, V=3941 .6(3) A
3, Z=8 , R=0 .090 . Next, intensity of low temperature phase was measured at
153K. The cell dimensions are a=11.5252(5) A, b=22.3020(9) A, c=14. 7548(6)A, V=3792.5(5) P , Z =8 , R =0.035.
CaH2oNBr•2CH4N2S andC8 H20 NCI•2CH4N2S undergo the phase transitions at 338K and 265K ,respectively.
Previous structure determination have been carried out on
CaH2oNBr•4CH4N2S
andC8H20NCI•5CH4N2S .
The
structureof
C8H20 NBr•4CH4N2S and C8 H20 NC1·5CH4N2S found to be orthorhombic , spacegroup Pna2 1 , and monoclinic , space group P2 ,, respectively.

149

AMoP-51
TRANSMISSION ELECTRON MICROSCOPE STUDY OF
RuSr2Gd1.sCeo.sCu201o-6 MAGNETO-SUPERCONDUCTOR

Yoshio Matsui ," Tadahiro Yokosawa ," Veer Pal Singh Awana ," Koji Kimoto ," Eiji
Takayama-Muromachi ,8 Maarit Karppinen ,b and Hisao Yamauchib
8

Nationallnstitute for Materials Science, 1-1 Namiki, Tsukuba , 305-0044,
Japan; bMaterials and Structures Laboratory, Tokyo Institute of Technology,
Yokohama, 226-8503 , Japan (MATSUI.Yoshio@nims .go.jp)
Coexistence of superconductivity and magnetism in RuSr2(Gd ,Sm ,Eu) 16Ce04Cu20 10.d (Ru-1222) (1) and RuSr2GdCu20 a (Ru-1212) (2) have been oftremendous interest. In this study , we have investigated the microstructure of
RuSr 2Gd15Ce 05 Cu20 10..; (Ru-1222) (3) , by SAED , dark-field electron
microscopy , convergent-beam electron diffraction (CBED) and high-resolution
TEM (4) . The RuSr2Gd1sCeosCu20 10.0 (Ru-1222) sample was synthesized
through a solid-state reaction route from Ru02, Sr0 2, Gd 20 3 , Ce0 2 and CuO.
The block of specimen was crushed and dispersed on a carbon thin film on a
Cu grid for transmission electron microscopy. The SAED and CBED patterns
and conventional dark-field images were taken at room temperature usingtransmission electron microscopes (Hitachi : HF-3000S and HF-3000L) operated
at an accelerating voltage of 300 kV. The SAED and CBED patterns were takenfrom specimen areas of about 100 and 8 nm , respectively. The HRTEM images
were taken by high-resolution high-voltage TEM (H-1500) , with 0.14nm
resolution at 800kV. Figure 1(a) shows a CBED pattern taken with [31 0]
incidence. Sharp superlattice reflections without diffuse streaks are observed at
I= 2n as indicated by a white arrowhead. Figure 1 (b) shows a [310] CBED
pattern taken from a different illumination area than that of Fig . 1(a) . It should
be noted that sharp superlattice reflections without diffuse streaks are observed
at I= 2n+1 as indicated by a white arrowhead. Figures 2(a) and 2(b) show darkfield images by using the superlattice reflections at I= 2n = 4 and I= 2n+1 = 3,
respectively as indicated by the white arrowheads in Figs. 1(a) and 1(b) . The
superlattice domains are clearly seen as many bright striated areas of about 10
nm in width as indicated by white arrowheads. We constructed a model , on thebasis of ordering of rotated Ru0 6 octahedra about the c axis , with A- and Bcentered orthorhombic superlattices (A and 8 superlattices) that correspond to
those of the observed su rlattice domains.

.

'

1*

.

c•~

; .

'f
'.~1u ./ ;.,., ..~ l·t·" "' !- :~:
. .
.

•

~

"'' """' ·. - V''"

'.

;

;

..

.

':

;

:
~

•

•

:

.

.

'· "

:

'

.

. !
. t
'
.

;

•

'

Fig.1 : (310] CBED patte rn s of Ru-1 222 taken from(a)one illuminati o n area , (b)a different illumination area
compared with th at of (a).

Fig.2 : Dark-fi eld images o f Ru-1 222 by using
th e superl attice reflections at (a)/=4 and (b)/=3
in Figs.1(a) and 1(b). respectively.

References
I
Feiner, I. eta/.(1997) Phys. Rev. B 55, R3374 .
2Bernhard , C. eta/.(1999) Phys. Rev. B 59 , 14099.
3
Awana , V. P. S. eta/. (2002) Physica C 249-254, 378.
4
Yokosawa , T. eta/. , Ultramicroscopy In press.

150

AMoP-52
X-RAY DIFFRACTION STUDY ON THE PHASE TRANSITIONS OF BaTiOJ
SINGLE CRYSTAL

Yukio Yoshimura ," Naotoshi Tokunaga ," Hiroshi lwasaki ,8 Akira Kojima ,b Hiroshi
Sasou ,b and Ken-ichi Tozakic
8

Faculty of Science and Engineering , Ritsumeikan University, Kusatsu , Shiga
525-8577 , Japan ; bDepartment of Materials Science , The University of Shiga
Prefecture, Hikone, Shiga 522-8533 , Japan ; cDepartment of Physics , Faculty of
Education , Chiba University, Chiba 263-8522 , Japan (yukio@se.ritsumei.ac.jp)

It is well known that the BaTi0 3 crystal undergoes three phase transitions
at 408 K, 278 K and 183 K. Recently we have made precise measurements ofphysical properties such as heat flow , dielectric constants and displacement
currents at each phase transition on both heating and cooling using the "mKstabilized cell" having fine temperature stability[1). Samples used are single
crystals from three different sources grown by the top-seeded solution growthmethod. Measurements of the heat flow and other physical properties haverevealed that both the 408 K and 183 K transitions are accompanied bycomplicated multi-step anomaly, whereas the 278 K transition showed a single
step.
In order to get structural information related to the results of the physicalproperties mentioned above , the phase transitions in BaTi0 3 have beenreexamined by X-ray single crystal precession method in the temperature range
between 420 K and 90 K. As a temperature is lowered from 420 K, the crystal
transforms at 408 K from the perovskite cubic phase into a room temperaturephase , where a tetragonal and a monoclinic_forms coexist. The crystal furthertransforms its structure at 278 K and 183 K. At 278 K transition , themonoclinic_form , one of the coexistence structure, vanishes and the tetragonallattice changes into another monoclinic_ form with twinned crystal suffering a
shear distortion in the low temperature phase. The lowest temperature phase
below 183 K is an orthorhombic lattice as a single domain with lattice constants
a=0.401 nm, b=0.400 nm , and c=0.402 nm.
ReferenceI
Kojima , Y. Kawakatsu , H. Sasou , Y.Yoshimura , N. Tokunaga , H. Iwasaki
and K. Tozaki , Ferroelectrics, In press .

151

AMoP-53
ALKALI METAL COMPLEXES OF AROMATIC POL YCARBOXYLATES -A
BALANCE OF ~~:-STACKING AND COORDINATE BONDING INTERACTIONS?

George A. Koutsantonis , Stephen Burnet, An neg ret K. Hall, Jack M.
Harrowfield , Vanessa Sanford, Daan Sauter, Brian W. Skelton , and Allan H.
White
Chemistry , School of Chemical and Biomedical Sciences , University of Western
Australia , Crawley, WA 6009 , Australia (gak@chem.uwa.edu.au)

Crystal structure determinations of, in most cases , hydrated alkali metal
derivatives of the dicarboxylic acids , 2,2'-bipyridine-3 ,3'-dicarboxylic acid(H 2 BDC) and chelidamic acid (4-hydroxypyridine-2 ,6-dicarboxylic acid ,H2CHEL) show numerous similarities , such as in the predominance of
coordination in generating solid state polymers in which parallel arrays of theessentially planar ligand ring units are apparent , though not necessarily
indicative of conventional -stacking interactions, and some unanticipateddifferences. In particular, all species derived from chelidamic acid , including its
diammonium compound , appear to be complexes of the partially deprotonatedpyridone form of this ligand. In both systems , close contacts between atoms
constituting the aromatic entities take a variety of forms depending upon theassociated metal.

a-

152

AMoP-54

COMPLEX COINAGE METAL(I) THIOSULFATES
E. J . Chan , B.W. Skelton , and A.H . White
University of Western Australia , School of Biomedical and Chemical Sciences,
35 Stirling Hwy, Crawley, W.A. 6009 , Australia (eric@crystal.uwa.edu.au)

Materials crystallized from aqueous solutions of thiosulfates (i.e . Na , K,
and NH 4) and coinage metal halides, may be relevant to photographic 'fixation '.
Previously known members of the isomorphous , tetragonal l-42d
2
1
2
M\ M 2X2(S20 3)2, M = group 1 cation , M = (Cu , Ag) , series , together withfurther new members, have been isolated as eight complexes , the nitrates andthe potassium /copper adduct all new , containing the complex anion[M 2(SS0 3)4( with quasi tetrahedral S-M-S geometry. Salts of the form M\ 20.
121)M 2 (S20 3)n.XH20 , n = 1-3, have also been defined : For n = 3, M = Cu , M /x =theadduct)K/2. 25 or 1 5/6, NH4/6, (and also for the (NH 4)4Na/4H 20 .MeOH
arrays take the form M\ [Cu(SS0 3)3]. xS with distorted trigonal planar CuS 3
coordination environments ; the silver counterparts take the form
1
M\o[(03SS)2Ag(wSS03)2Ag(SS0 3)2] for M = K, NH4. For n = 2 adducts have
2 = Ag , the anions of the M = Na , K adducts being
only been defined for M
dimeric and polymeric : Na 6 [(0 3 SS )2Ag( ~t-SS0 3 )2Ag(SS0 3 )].3H 2 0 , K 3 [Ag( ~t­SS03)2].H20 ; a polymeric copper 1 counterpart of the latter is found in
Na5Cu(N03)2(S20 3)2 = 2NaNOJ.Na3[Cu(!l-SS03)2]. For n = 1, NaAgS20 3,
isolated as both the known mono and a new anhydrate , exhibit a twodimensional polymeric complex anion in both forms but with different
contributing motifs , 6- and 4- membered rings respectively .
(NH4)1 3Ag 3(S20 3)a.2H20 takes the form (NH 4 ) 13[{(0 3 SS)Ag(~t.-SS0 3 )2 }2Ag]. aInlinear central silver atom linking a pair of [Ag(SS0 3)4( entities .
Na 6 [(0 3 SS)Ag( ~t - SS0 3 )2Ag(SS0 3 )] . 3H 2 0 , two binuclear anions are present assingle clusters , the associated oxygen atoms disposed to one side , sandwichinglayers of sodium ions.

153

AMoP-55
STRUCTURE DETERMINATION OF ADDUCTS OF LEAD(II) IODIDE WITH NMETHYL SUBSTITUTED ETHYLENEDIAMINE AT LOW AND ROOMTEMPERATURES (123, 209 AND 295 K)

Hiroshi Miyamae, Kouich irou Enomoto , Youhei Maruyama, and Goro Hihara
Department of Chemistry, Josai University, Saitama 350-0295 , Japan(miya@josai. ac.jp)
We have reported that a series of N-methyl substituted ethylenediamines
forms 1:1 adducts with lead( II ) halides [1) . Among them N,N'-dimethyl- and
N,N,N'- trimethyl-ethylendiamine (N,N'-en and N,N,N'-en) with Pbl 2 crystallize intetragonal forming 4 1 spiral with bridging two of iodides. We examined whichpart contributes mainly volume contraction upon cooling.
X-ray data were taken at three different temperatures, 296 , 209 and 123K.
The variation in cell volume
and axes are gathered inTable 1. Cell parameters at different temperatures .
Tab le 1.
Th e cel l Pbi -NNN'en
123K
209K
296 K
2
parameters do not vary a(pm )848.16(6)853.96(3)855 .98(3)linearlyoncooling , b(pm)165 1.4(2)1669.15(8)1659 .73(7)especial ly for N ,N ,N'-en . V(x 10-6pm 3 )11 88.0(2)1217.22(8)1216.09(8)However, the co ntra cti on
Pbi 2-NN'en
123K
209K
296K
880.26(5)879.34(4)879.4 3(7)could relate to reduction of a(pm )b(pm )
1499 .04(6)1509.89(9)1521.20(7)the nonbonding contacts
63
11 59 .12(8)1167.7( 1)1178.7(1)between the spirals o r V(x 10' pm )period of a spira l (Fig . 1).
Thus it appea rs that the ord inal bonds are qu ite rigid for temperature variation .

(a

F ig . 1. C rysta l packings view ed alo ng a for Pbl 2- NNNen (a )a nd Pbb -NNen (b) at 123K.

References
I
Miyamae, H. , Hatanaka , Y., liji ma , Y., Hihara , G. and Nagata, M. (1992)
AsCA Program Abstracts, 16S 44 .

154

AMoP-56
UNEXPECTED PIPERAZINE DERIVATIVE LIGANDS FROM A MIXTURE OF
CuCb.2H 20, Na2C03, AND TRIETHYLENETETRAMINE TETRAHYDROCHLORIDE

Norihiro Tamura ," Masato Sakai ,b Katsuya Kudoh ,b Goro Hihara ,b and Hiroshi
Miyamaeb•school of Dentistry , Meikai University, Saitama 350-0283, Japan; bDepartmentof Chemistry, Josai University, Saitama 350-0295 , Japan (miya@josai.ac.jp)

We have already reported that PbCh can remove contaminated 2,2' ,2"triam inotriethylamine (tren) from commercially available triethylenetetramine(trien) [1]. There are another stories of impurities in trien .
One of us mixed CuCI 2.2H 20 with trien in water, the mixture gave acomplex cation as shown in Fig. 1(1) with [CuCI3t anion. There is a ligand , 1(6 ,3-diaza- hexyl)piperazine , which act as a tridentate with the terminal N of thepiperidine ring being protonated. The starting Cu compound contains Cu(ll) ion ,but in the anion the Cu atom should be oxidation state of +1. The result
indicates that the reaction must contain a redox step which might has relation toform a new ligand. The other trial to produce compound 1 gave us two nuclear
Cu complex as shown in Fig . 2(~) . when we had used excess of Na2C03. The
ligand is 1,4-bis(2-aminoethyl)piperazine which act as bidentate to each Cu andmake bridging. There is no indication for redox process , but the excess ofco}· ion seems to compensate the positive charge of the Cu(ll) ions.
It is uncertain whether the organics come originally from impurities or fromreaction products of the complex formation . However it is one of the good
procedures to get the ligands , which are not commercially available.

Fig . 1. The structure of 1-

Fig . 2. The structure of~-References
I
Miyamae, H., Yoshinari , K., Hihara , G. and Nagata, M. (1988) Acta Cryst.
C44, 1528-1530.

155

AMoP-57
ANALYSIS OF PHASE TRANSITION MECHANISM OF ACYLUREADERIVATIVE CRYSTAL BY A DETAILED TEMPERATURE RESOLVED
MEASUREMENT OF POWDER X-RAY DIFFRACTION
Daisuke Hashizume ,"·b Masaru Ogawa ,b Yasuhiro limura ," Masanori Yasui ,b Eiji
Nishibori ,c Masaki Takata ,d and Fujiko lwasakib"Advanced D & S Center, RIKEN , Wako , Saitama 351-0198 , Japan ;bDepartment of Applied Physics and Chemistry, The University of ElectroCommunications, Chofu , Tokyo 182-8585, Japan; cDepartment of Applied
Physics , Nagoya University, Chikusa , Nagoya 464-8603 , Japan ; dMaterials
Science Division , JASRI/SPring-8, Mikazuki , Hyogo 679-5198 , Japan(hashi@postman .riken .go.jp)
Crystal of 1-(2-chloroacetyl)-3-pentylurea shows a solid-to-solid first orderphase transition at 347K with heat absorption of 17 kJ mol" 1 . During the phasetransition , the single crystalline form of the crystal is collapsed . To elucidate
mechanism of the transition , we performed powder diffraction analysis to obtainthe structures at high temperature phase.
Diffraction data were collected withlarge Debye-Scherrer camera installed on
BL02B2 beam line at SPring-8 using X-raysof 12.398 keV (1 .0 A) at 15 temperaturepoints in the range of 300 to 350K , 1-1?-r.hlnrn,r.P.Ivl\-:1-nP.nlvl "r""especially the data from 340 to 350K werecollected at every 1K. The phase transition was started from 340K andcompleted at 346K . Both phases were coexisted at the temperature range .
Space group was changed from P2 1/a to P-1 and periodicity along the a axis
became a half with the transition.
The structure at high(a)temperature phase was solved bya simulated annealing method
following Pawley refinements . At
lowtemperaturephase ,
carbonylurea moieties form onedimensional hydrogen bonding
ribbon structure and the pentylgroup at the N-terminal of the
carboxyurea moiety sticks out
from the ribbon. After thetransition , the ribbon structure ismaintained but relative positionsof the ribbons are changed withrotation of whole the ribbon
structures. Conformation of thepentyl group is drasticallyFig. Crystal Structures of (a) LTP and (b) HTP.
changed . The conformationalvariations may be coupled with the change of relative position between the
ribbon structures.

156

AMoP-58
OBSERVATION OF THE PHOTO-EXCITED STRUCTURE OF PLATINUMCOMPLEXES
Nobuhiro Yasuda , Hidehiro Uekusa. and Yuji Ohashi
Department of Chemistry and Materials Science, Tokyo Institute of Technology,
Ookayama . Meguro-ku , Tokyo 152-8551 , Japan (nyasuda@chem .titech.ac.jp)
It was reported that the crystal lattice of the platinum complex. [Bu4N]4[Pt2(pop)4] (pop = [P20 sH2f). contracted on exposure to visible light and back toth e original cell dimensions when the irradiation was stopped [1] . The contraction
was assumed to be due to the formation of the excited state by photo irradiation .
In order to examine the photo-excited structure of the platinum complex anion. thestructures of several related platinum complex crystals during the irradiation wereanalyzed by X-ray diffraction method at low temperatures [2]. The crystals havetetrabutylammonium(l) , tetrapentylammonium(ll) . benzyl(triethyl)ammonium(lll),
benzyl(tributyl)ammonium (IV) and benzyl(dimethylphenyl)ammonium(V) as cation.
In some crystals, solvent molecules are included and polymorph structures were
found .
The preliminary structure analysis by X-rays revealed that the chemical
formula of the platinum complex (I-IV) is not [Pt2(pop)4] but [PbH 2(pop)4]. as shownin Figure 1. This means that two protons are attached to the phosphate groups,
which are clearly assigned by the differential density map or the P-0 distances.
Each crystal was irradiated with the filtered xenon light (Am,,=470nm) at low
temperatures (173 and 103 K) and the three dimensional crystal structures wereanalyzed before and during the irradiation . The unit-cell volume decreased ,3~ V=20.33(24) and 13.86(23) A for II and Ill , respectively (Table 1). Comparing thethe Pt-Pt and Pt-P distances decreased significantly
off,
and
on
betweenstructuresby the light irradiation (Table 2). These results clearly indicate that photo-excitedstructures were observed by laboratory X-ray analysis.
Table.1 Unit-ce ll volume before and during the irradiation!'. (ON -OFF)
Light ON (A ' )Light OF F (A )-8 .02(8)13 12 .16(5)1320 .18(3)-20.33 (24)3025 .12(17)3046 .45(7)II-13 .86(23)2094 .92(1 1)2108 .78( 12)I ll-5 .15(28)2691 27(12)2696.42( 16)IV-5 .86(12)3607.44(6)36 13.30(6)v
Table.2 The difference of avera!Jed bond distance (C. (on -off))

Figure 1[Pt 2 H 2(pop).f anion

P-0( -H) (A)
Pt-P (A)Pt-Pt (A)
-0.003(3)I -0 .0038 (3) -0.0060(1 0)
II -0 .0082(3) -0.0053(11) -0 .00 3(4)Ill -0.0127(5) -0.0085( 16) -0.007(5)0.001 (4)IV -0 .00 30 (3) -0.0019(1 2)v -0 .001 9(2) -0.0033(8) -0.003(3)P-0(-P) (A)-0.003(3)-0.003(3)-0.009( 5)-0.00 1 (4)-0.002(3)P= O (A)-0 .003(3)0 .002(3)-0 .002(5)-0.005(4)-0.001(3)Referenceslkagawa , T .. Okumura. T., Otsuka, T. and Kaizu . Y. (1997) Chem. Lett. 26 ,1
829-830 .
Yasuda, N .. Kanazawa . M .. Uekusa. H. and Ohashi , Y. (2002) Chern. Lett.
2
31 , 1132-1133.

157

AMoP-59
DISORDER IN STRUCTURAL CRYSTALLOGRAPHY
S. Banerjee , and A. K. Mukherjee
Department of Physics, Jadavpur University, Calcutta- 700 032 , India(surajit@juphys .ernet.in)

Structural disorder is a long standing problem in X-ray crystallography andthe accuracy and reliability of final results of structure analysis depend largelyon the degree of disorder present in the system. A disorder in a crystal is often
associated with poor quality of diffraction data leading to an apparently highfinal R factor. But certain types of disorder are potentially informative about thebonding and the chemistry of the compounds in which they occur. A disorderusually occurs when there are more sites available to a set of atoms in aparticular structure than the number of atoms to fill them. Three common typesof disorder encountered in structural crystallography are (i) solvent disorder (ii)positional disorder (iii) orientational disorder. Here we present the positional
disorder of three oxo-peroxo tungsten complexes which are important for theircatalytic activity as a part of our ongoing study of molybdenum/tungsten
complexes of organic ligands. All complexes crystallize in same monoclinic
system with different space groups having disorder in the oxo-peroxo sites withoccupancies (66%, 34% ), (53 %, 47 %) and (51 %, 49%), respectively. The
geometry around the W atom can be best described as distorted pentagonal
bipyramidal with the axial sites being occupied by one oxo and one ligand
oxygen atoms[1 ,2). All the structures are stabilized by Van der Waals forces.

References
I
Gresley , N. M. , Griffith, W. P., White , A. J. P. and Williums, D . J. (1997), J.
Chern. Soc., Dalton Trans .. 89-92 .
2
Griffith , W. P. , Parkin , B. C. , White, A. J. P. and Williums, D. J. (1995), J.
Chern. Soc., Chern. Commun ., 2183-2184 .

158

AMoP-60
NOVEL CRYSTAL STRUCTURES OF VANADYL GALLOPHOSPHATES

Sue-Lein Wang
Department of Chemistry, National Tsing Hua University, Hsinchu , Taiwan 300(slwang@mx .nthu .edu .tw)
3

Substitution of the first-raw transition metal (TM) ions for Al + in theframeworks of aluminum phosphates is of particular interest for theenhancement of catalytic activity and the design of novel catalysts . The locationand environment of the TM ion site is of considerable importance forunderstanding the catalytic and adsorptive properties of molecular sieves. As
only few single-crystal data available for most of the MAIPO-n samples, actual
incorporation of TM ions into the tetrahedral frameworks is difficult to prove [1]Owing to the similarity in the framework topology, the search for gallium
phosphates adopting microporous structures has attracted much attention [2 ,3]
By employing hydrothermal crystallization, we have prepared a series of novel
open frameworks including the first 24-ring containing gallium phosphate phase[4] which exhibits large channels with a measured pore diameter of -11.2 A. In
this presentation , the crystal structures and magnetic properties of several
large-channel containing VGaPO frameworks shall be described and discussed .
References
Hartmann , M. , Kevan , L. , (1999) Chem . Rev. 99 , 635 , and referencesI
therein.
Cheetham , A. K., Ferey, G., Loiseau , T. (1999) Angew. Chem. Int. Ed. 38 ,23268 .
Lin , C. H., Wang, S. L. (2000) Chem. Mater. 12 , 3617 , and references3
therein.
Lin , C. H., Wang , S. L. , Lii , K. H. (2001) J. Amer. Chem. Soc. 123, 4649 .
4

159

AMoP-61
ON THE DIELECTRIC CONSTANT OF Bas-3xRs+2xTi1sOs4(R=Sm,Nd) SOLID
SOLUTIONS: CRYSTAL STRUCTURAL ANALYSIS

H. Sakashita , H. Ohsato , N. Araki , and K. Kakimoto

Nagoya Institute of Technology, Nagoya 466-8555, Japan(ohsato@mse. nitech .ac.jp)

Recently, microwave telecommunication technology, for example portable
telephones and satellite broadcasting, has been developing rapidly. In thedevelopmental process , microwave dielectric ceramics with high dielectric
constant have contributed to the miniaturization of the resonators. Especially,tungstenbronze type-like Ba 6. 3xRs•2xTi18 0 54 solid solutions have large
permittivity in addition to the high quality factor and nearly zero temperature
coefficient of resonant frequency. We have reported the results of the extensive
crystal structural investigations on tungstenbronze type-like solid solutions
formed with many rare-earth ions . Presently , we report the structural
correlations with the dielectric constant in the tungstenbronze type-like solid
solutions formed with Sm and Nd. Single crystals of solid solutions were grownby self-flux method . Structural data were deduced by performing crystal
structure analysis on the raw data obtained from x-ray 4-circle goniometer (w-20
scan and 1-.=0 .71 073) .
The structural network of this solid solutions are composed of squares(A1 -site : Sm/Nd) , pentagons (A2-site: Ba & Sm I Ba & Nd) and octahedrons(Ti). Individual site-volumes and the octahedral tilting angles are calculated fromthe precision structural data . It is found that there is an explicit correlation
between the site-volumes and dielectric constant in the series of solid solutions
synthesized and analyzed . The volume of A 1-site and octahedron at x= 0.5 ishigher than that of at x= 0.71 with an exception only for A1(4)-site for Sm solid
solutions . Also , the tilting angle of Ti0 6 along the c-axis is smaller at x=0 .5 incomparison to that of at x=O. 71 . A similar trend is also observed in solid
solutions prepared with Nd. These structural correlations with dielectric constantof solid solutions will be presented in detail.

160

AMoP-62
DEUTERIUM TRANSFER MECHANISM IN CHIRAL THIOLACTAMFORMATION BY NEUTRON DIFFRACTION MEASUREMENT USING
BIX-111 DIFFRACTOMETER

Takaaki Hosoya ," Hidehiro Uekusa ," Yuji Ohashi ," Takashi Ohhara ,b lchiro
Tanaka ,c and Nobuo Niimurac
80epartment of Chemistry and Materials Science , Tokyo Institute ofTechnology , 0-okayama , Meguro , Tokyo 152-8550, Japan ; blnstitute ofMaterials Structure Science, High Energy Accelerator Research Organization ,Oho , Tsukuba , lbaraki 305-801 , Japan; cNeutron Structural Biology, Advanced
Science Research Center, Japan Atomic Energy Research Institute, Tokaimura , Naka-gun , lbaraki 319-1195, Japan (thosoya@chem .titech.ac.jp)
It has been found that N,N-dibenzyl-1-cyclohexenecarbothioamide 1 a isphoto-isomerized to optically active [3-thiolactam 2a in high optical yield in the
Although X-Ray diffraction study of crystalline-statesolid state [1] .
photoreaction from 1 a to 2a revealed the mechanism of chiral [3 -thiolactam
formation , the hydrogen transfer process remained unsolved. In order to makeclear the mechanism , the neutron diffraction technique was applied to a newcompound 2a with all benzyl hydrogen atoms of 1 a were replaced with
deuterium atoms. The photo-product 2b from 2a has a methylene carbon atomwith a hydrogen and a deuterium atoms , "chiral methylene". The absoluteconfiguration of this "chiral methylene" indicates the direction of deuteriumtransfer, i.e. , via intramolecular or intermolecular. We used neutron-IP
diffractometer BIX-111 to determine the absolute configuration of this chiralmethylene . The difference Fourier map clearly showed negative and positive
peak around the chiral methylene , corresponding to a hydrogen and a
deuterium , respectively. This result revealed that a deuterium atom bonded tothe benzyl carbon atom was transferred to the intramolecular cyclohexene
carbon to occupy the equatorial position of the produced cyclohexyl ring.
In·~
Crystall ineState~"."'rh

-- ~
'

. _-S

'-CIIzl'h'"Ia~,,,.,"'.·

N..._

CDl i'I HIJ

hi'Crysta lline
State

s

'"
Because the deuterium should occupy the axial position if it was transferredfrom the neighboring benzyl carbon .
References
I
Sakamoto , M., Takahashi , M ., Kamiya , K., Yamaguchi , K., Fujita , T. and
Watanabe , S. (1996) JAm. Chern. Jpn. 118, 10664.
2
Hosoya , T. , Ohhara , T. , Uekusa, H. and Ohashi , Y. (2002) Bull. Chern.
Soc. Jpn. 75, 2147.

161

AMoP-63
STRUCTURE OF THE PSEUDORHOMBOHEDRAL lnFe, _xTixOJ+x/2
COMPOSITE CRYSTAL
Yuichi Michiue, 8 Mitsuko Onoda ,8 Francisco Brown ,b Noboru Kimizuka ,c andMamoru Watanabe 88Advanced Materials Laboratory, National Institute for Materials Science, 1-1
Namiki , Tsukuba, lbaraki, 305-0044 , Japan ; bDepartamento de Investigaciones
en Polimeros y Materiales, Universidad de Sonora , Rosales s/n Hermosillo ,Sonora , C.P.83000 , Mexico; cceramic Materials Research Institute, Hanyang
University, 17 Haengdang-dong , Seongdong-gu , Seoul 133-791 , Korea(MICHIUE .Yuichi@nims .go .jp)
In pseudobinary systems lnA0 3-In 2Ti 20 7 (A :Fe , Ga , AI , Cr) , composite
crystals lnA ,_x Tix0 3+x12 with two types of layered structures were found [1] . The
one obtained in the Ti-rich region has the pseudorhombohedral (p-R) structure
and the other in the A-rich region does the pseudohexagonal (p - H) . The
incommensurately modulated structure of the p-H lnFe, _xTix0 3.xl2 was clarified
by the 4-dimensional superspace group analysis for diffraction data of a single
crystal [2] . In this paper th e structure of the p-R form is discussed on the basisof the profile fitting of X-ray diffraction patterns .
The structure of a commensurate (x=2/3 ) p-R form for A=Fe is shown in
Fig . 1. In analogy with the p-H form , the p-R phases are also described as thecomposite crystal con sisting of the two subsystems with different periods along
the b-a xis. The first subsystem is constructed by ln06 octahedral sheets and the
Fe/Ti atoms in a slab at z=0 .5, while the second one is made only by the 0atoms in the slab containing the Fe/Ti atoms. Atomic arrangement in the slab isgiven in Fig. 2 , which is similar to that seen in a part of the p-H structure [2] .

•

Fe!Ti

0 0

J
Fig .1 Structure ofpsuedorhombohedral

Fig .2 Atomic arrangementin the slab at z=0.5 .

References
1
Brown , F. , Flores , M . J. R. , Kimizuka , N., Michiue, Y., Onoda , M ., Mohri ,T., Nakamura , M. and lshizawa , N. (1999) J. Solid State Chem. 144, 9199 .
2
Michiue , Y ., Onoda , M., Watanabe, M., Brown , F. and Kimizuka , N. (2001 )Acta Crystallogr. 857 , 458-465 .

162

AMoP-64
USING THE HREM TO STUDY MORPHOLOGY AND STRUCTURE
OF NANOMATERIAL Ta AND TaNxVo Vonq ," Luu tien Hung ,b Steffen Schulze ,c and Michael Hietscholdc
alaboratory of Electron Microscopy - National Centre for Natural Science andTechnology, 18 Hoangquocviet Str., Caugiay Hanoi, Vietnam ; bDepartment of
Physics, Vinh University, Vinh City , Nghean , Vietnam ; clnstitute of Physics ,Chemnitz University of Technology , D-091 07 Germany (vvemlab@ncst.ac.vn)

The grain sizes , phases , structures and morphology of Ta and TaN x thinfilms on Si and Si0 2 substrates , which belong to the most promising barriermaterials for copper in interconnect systems of semiconductor devices were
determined by using high resolution electron microscopy (HREM).
In this work , we present the sample preparation of these films for TEM
plan-view investigations. Special efforts had to be made in order to reachelectron transparency despite of the high internal stress in the thin films . In
detail , we discuss the grain sizes, phases and structures of the films and alloys
as deduced from bright-field and dark-field images and selected area electron
diffraction patterns.

163

AMoP-65
STRUCTURE-BASED DESIGN OF ANTI-INFLAMMATORY AGENTS:
CRYSTAL STRUCTURE OF A COMPLEX FORMED BETWEEN COBRAVENOM PHOSPHOLIPASE A2 AND A DESIGNED POTENT PEPTIDEINHIBITOR VAL-ALA-PHE-ARG-SER- (VAFRS) AT 1.9 A RESOLUTION.

R. K. Singh , J . Makker, P. Vikram , M. Paramsivam , T. Jabeen , S. Sharma , S.
Dey, P. Kaur, A. Srinivasan and T. P. Singh
Department of Biophysics, All India Institute of Medical Sciences , New Delhi11 0029 , India (rajendra84@hotmail.com)

Phospholipase A2 (PLA2) is a key enzyme involved in the production of
prostaglandins and other related compounds collectively known as eicosanoids .
These substances mediate inflammatory response in humans . Among several
structure-based designed peptide molecules, a pentapeptide VAFRS showed
an inhibition of PLA 2 with a binding constant of 10-11 M. In order to understandthe mechanism of binding and evaluate the interactions between PLA 2 andpeptide VAFRS , a complex between PLA2 and VAFRS was prepared . The
complex was crystallized using 35% ethanol as a precipitant. The crystals
belong to space group P4, with a = b = 42.8 A, and c = 65 .9 A. The crystals
diffracted to 1.9 A resolution . The structure was determined by molecularreplacement method and refined to an R-value of 0.182. The peptide was
located at the binding site of PLA2. It formed several hydrogen bonds and vander Waals interactions. The most notable interactions were observed with the
Arg of peptide molecule . The side chain of arginine formed multiple interactions
with Asp49 , His 48, Cys 45 , Gly 30 , Tyr 28 indicating the significance of its
substitution at polar end of the peptide. The VAF part of the peptide wasinvolved in a number of van der Waals interactions in the hydrophobic channel.
The prominent conformational differences between the native cobra PLA 2 andthe PLA2 in the complex were restricted to !?,-wing and the C- terminal regions of
the enzyme . Indeed , the structure provided an excellent model based on themethod of structure based drug design .

164

Tuesday August 12

AsCA'03/Crystal-23

ABSTRACTS
ORAL SESSIONS

165

PL-3
ULTRA-HIGH SPEED NEUTRON DIFFRACTION STUDIES: COMBUSTIONSYNTHESIS OF TiJSiC2 AND RELATED COMPOUNDSErich H. Kisi , and Daniel P. Riley
School of Engineering , The University of Newcastle , Callaghan NSW 2308 ,Australia (meehk@cc.newcastle.edu.au)
TbSiC2 is an exciting new material that combines the attractive
properties of both metals and ceramics . Combustion synthesis (or Selfpropagating High-temperature Synthesis , SHS) has received considerable
attention as a low cost alternative to synthesising materials such as Ti 3SiC2.
The process is attractive because , after an initial input of heat to initiate thereaction , the heat of formation of the product phases supplies all of theremaining energy requirement. A quantitative understanding of SHS has beenhampered by the rapid reaction rates and high temperatures involved .
In-situ neutron diffraction patterns (0-160°) at 0.9s and 0.38s time
resolution were used to capture the reaction mechanism during SHS of
Ti3SiC2 from furnace ignited stoichiometric Ti/SiC/C, Ti/Si/C and Ti/AI4CJIC
mixtures . As shown in Fig 1, the diffraction patterns are rich in detail. They
indicate five stages: (i) pre-heating of reactants , (ii) hcp -'l bcc phasetransformation in Ti , (iii) pre-ignition reactions , (iv) formation of a single solidintermediate phase in -0 .5s and (v) rapid precipitation of TbSiC 2 after a shortincubation period. The intermediate phase is believed to be a solid solution of
Si in TiC which preserves the overall stoichiometry, (3Ti :1Si:2C) . The results
are quite general , applying to all of the reactants studied and independent(apart from the ignition temperature) of the physical state of the reactant
powders .
Lattice parameters and known thermal expansion data were used toestimate the ignition and combustion temperatures eg , in the system
3Ti+SiC+C , these were 923(10) °C and 2320(50) °C respectively. An anomaly
in the cooling curve measured in this way was used to propose a diffractionbased thermal analysis technique capable of supplying estimates of phasetransition enthalpies .

Fig. 1 Three dimensional plot of a portion of the diffraction pattern s during SHS of Ti 3SiC2.
Time is on the y-a xis, two theta on the x-axis and diffracted intensity on th e z-axis .
The labels refer to pea ks from (a) a-Ti , (b) a-Ti (decreasing) and B-Ti (increasing), (c) SiC, (d)the intermediate phase and (e) Ti 3SiC2 .

166

PL-4
ELECTRON MICROSCOPY TECHNIQUES- MICROSCOPY, DIFFRACTION
AND SPECTROSCOPY

Michiyoshi Tanaka
Institute of Multidisciplinary Research for Advanced Materials, Tohoku
University
Katahira 2-1 -1 Aoba-ku , Sendai Japan (tanakam@tagen.tohoku.ac.jp)
The electron microscope has three functions for the characterization ofmaterials, 1) microscopy, 2) diffraction and 3) spectroscopy.
1) The spatial resolution of the standard electron microscope has been alittle less than 0.2 nm. Recently, owing to the development of the correction
techniques of the spherical aberration of the objective lens, the resolution isreaching 0.1nm . It is , however, noted that the resolution is far from thewavelength of the electrons , namely 0.0025nm at 200kV, because theconvergence angle of the electron beam allowed is only about 1o-2 rad .
Further development of electron optics is strongly expected for the
improvement of the spatial resolution .
2) Electron diffraction is divided into two techniques . The first is selectedarea diffraction (SAD) , which has been long time used as the standard
technique. The second is convergent beam electron diffraction (CBED), whichuses a convergent beam instead of a parallel beam used in SAD. CBED candetermine all the 32 crystal point groups using dynamical diffraction effect ,while X-ray diffraction can determine 11 Laue groups. Dynamical extinctions
allow us to distinguish between mirror planes and glide planes , and rotation
axes and screw axes . As a result, CBED can determine most space groups
using the dynamical extinctions. A nanometer-scale crystal structurerefinement can be performed by fitting the reflection intensities of CBED
patterns with simulation patterns, where the phase problem does not appear
because the reflected intensities contain phase information due to multiple
reflections in the materials . The defocus technique or the large angle
technique (LACBED) , by which both the information from the real andreciprocal spaces can be obtained , can determine unambiguously thequantitative feature of c rystal defects, while the traditional electron
microscope method uses only limited information from the defects.
3) Electron spectroscopy is increasing its importance , because it canobtain spectra from nanometer-scale areas and can cover a very wide energy
range , namely from 1 to 1OOOeV. Electron energy loss spectroscopy (EELS)
and wave dispersive spectroscopy (WDS) with an about 0.2eV energy
resolution are very effective for the analysis of electronic structures ofmaterials. CBED is the major subject to be reported in this talk.

167

ATu1A-1
CATALYSIS AND ALLOSTERIC REGULATION IN PHOSPHORIBOSYLDIPHOSPHATE SYNTHASE; THE ROLE OF TWO MAGNESIUM IONS

Sine Larsen , and Frank B. Nygaard
Centre for Crystallographic Studies , University of Copenhagen ,Universitetsparken 5, 2100 Copenhagen , Denmark (sine@ccs.ki.ku.dk}
5-Phospho-D-ribosyl "-1-diphosphate (PRPP) provides exclusively theribose moiety present in all purine, pyrimidine and pyridine nucleotides. The
essential metabolite PRPP is prepared in a reaction between ATP and ribose5 phosphate , catalysed by enzyme PRPP synthase (PRPPase) . The key
position of PPRP in the metabolism of the cell explains why the activity of
PRPPase is highly regulated . Most PRPPases are regulated in an allostericmanner, in which purine nucleotides especially ADP acts as the most potent
inhibitor. Inorganic phosphate (Pi) is an activator of bacterial and mammal
PRPPases . MgATP is the true substrate for PRPPases , but in addition the
enzyme requires a free Mg 2 + ion as an activator. The structure of the
PRPPase from Bacillus subtilis has been determined complexed with sulfate(mimicking Pi), ADP and Cd 2+ . All structures reveal the same hexamericarrangement of the PRPPase subunits in which crystallographic threefold
symmetry relates two independent subunits related by non-crystallographic
twofold symmetry. Furthermore the structures made it possible to identify thebinding sites for substrates, activators , allosteric inhibitors and divalent metal
ions [1 ,2]. However it could not be ascertained which state of the enzyme thedifferent complexes represented , as neither of them contained structural
information about the supposedly active site loop rich in conserved residues.
The structures have been determined for six additional complexes of the
PRPPase from B. subtiiis determined from crystals grown under different
experimental conditions making use of the kinetic data for the enzyme [3]. It
was possible to trace the active site loop in the structure , which had thetransition state analogue AIF3 bound . The complex with the allosteric inhibitor
GOP gave similar information about the allosteric regulation. The new
structural results have enabled us to propose detailed reaction models forboth catalytic function and allosteric regulation of the enzyme , that can explain
the abundant kinetic data available for the enzyme. The two Mg 2 + ion play a
crucial role in catalysis , and the allosteric regulation can be rationalized interms of domain movements in the subunits and subunit movements within
the hexamer, that can explain why single point mutations in the prs genecauses severe illness.
References
I
Eriksen , T. A. , Bentsen , A. -K., Kadziola , A. , Harlow, K. W. and Larsen ,S. (2000) Nature Struc. Bioi. 7, 303-308.
2
Eriksen, T. A. , Kadziola , A. and Larsen . S. (2000) Protein Science 11,271-279.
3
Willemoes , M, Hove-Jensen , B. and Larsen , S (2000) J. Bioi. Chern.
275, 35409-35412.

168

ATu1A-2
ENZYMES OF RIBOSE METABOLISM: STRUCTURE AND MECHANISM

Sherry L. Mowbray,8 C. Evalena Andersson ,b Annette Roos ,b Torsten Unge b
and T. Alwyn Jonesb
8
Department of Molecular Biosciences , Division of Structural Biology , Swedish
University of Agricultural Sciences, BMC, Box 590 , SE-751 24 Uppsala,Sweden; bDepartment of Cell and Molecular Biology, Uppsala University,
BMC , Box 596 , S-751 24 Uppsala, Sweden (mowbray@xray .bmc.uu .se)
Although it is well established that ribose is a crucial sugar, its metabolism
has only recently been investigated from a structural and mechanistic point ofview. Our studies have explored the ribokinase and ribose-5-phosphate
isomerases essential for using (and re-cycling) ribose, as well as in its
interconversion with other sugars.
Ribokinase was the first example of a new fold since found in related
enzymes such as adenosine kinase. Conformational changes associated withribose binding also are typical of the family[1]. Ribokinase 's activation by amonovalent cation was linked to the formation an anion hole in the active site,
the first documented case of allosteric activation of a carbohydrate kinase by anion[2] Site-directed mutagenesis successfully created an ion-independent versionof ribokinase[3].
Ribose-5-phosphate isomerase interconverts ribose-5-phosphate andribulose-5-phosphate, and is thus an essential enzyme in the pentose phosphatepathway and the Calvin cycle of plants. Two types of unrelated enzyme exist,
often within the same organism . The structure of RpiA from E. coli was studied
together with the groups of Savchenko (Toronto) , Edwards (Toronto) and
Joachimiak (Argonne)[4] . This was again a new fold; the structure showed how
the ribose ring could be opened to provide the linear form necessary forisomerizaton, as well as identifying the groups needed for binding and catalysis.
A second , unrelated type of ribose-5-phosphate isomerase from E. coli (RpiB)
was found to have a completely different fold and catalytic mechanism[5] . The
enzyme from Mycobacterium tuberculosis has a structure closely related to RpiB,
but with a different catalytic mechanism[6]. The three Rpis thus presentinteresting examples of convergent and divergent evolution.
References

1

2
3
4

5

6

Sigrell , J.A. , Cameron , A.D. , Jones, T.A. & Mowbray, S.L. (1998) Structure
6, 183-193; Sigrell , J.A. , Cameron , A.D. and Mowbray, S.L. (1999) J. Mol.
Bioi. 290 , 1009-1018.
Andersson , C.E. and Mowbray, S.L. (2002) J. Mol. Bioi. 315, 409-19.
Andersson , C. E. , Roos, A. Unge, T. and Mowbray, S.L. (2003) in
preparation.
Zhang , R. , Andersson, C. E., Savchenko, A. , Skarina , T., Evdokimova, E. ,Beasley, S. , Arrowsmith , C. H., Edwards, A.M. , Joachimiak, A. andMowbray, S.L. (2003) Structure 11 , 31-42.
Zhang , R.-g., Andersson, C.E., Skarina , T. , Evdokimova, E. , Edwards, A.M .,Joachimiak, A., Savchenko, A. & Mowbray, S. L. (2003) J. Mol. Bioi.
submitted .
Roos, A. , Andersson , C.E., Joachimiak, A., Unge, T. , Jones, T.A, andMowbray, S.L. (2003) in preparation.

169

ATu1A-3
CRYSTAL STRUCTURE OF TWO KNOTTED PROTEINS:ACETOHYDROXY ACID ISOMEROREDUCTASE ANDtRNA(m 1 G37)METHYLTRANSFERASE

Se Won Suh , Hyung Jun Ahn , Jin Kuk Yang , Byung II Lee , and Hye-Jin Yoon
Department of Chemistry, Seoul National University, Seoul 151-742, Korea(sewonsuh@snu.ac.kr)

Acetohydroxy acid isomeroreductase (AHIR) is a key enzyme inbiosynthesis of branched chain amino acids . We have determined the first
crystal structure of a class I AHIR from Pseudomonas aeruginosa. Its
dodecameric architecture of 23 point group symmetry is assembled of si x
dimeric units and dimerization is essential for the formation of the active site .
The dimeric unit of P. aeruginosa AHIR partially superimposes with a threedomain monomer of spinach AHIR, a class II enzyme , thus demonstrating that(i) the so-called 'plant-specific' insert in the middle of spinach AHIR is
structurally and functionally equivalent to the C-terminal a-helical domain of P.
aeruginosa AHIR , and (ii) the C-terminal a -helical domain was duplicatedduring evolution from the shorter, class I AHIRs to the longer, class II AHIRs.
The dimeric unit of P. aeruginosa AHIR possesses a deep figure-of-eight knot,
essentially identical to that in the spinach AHIR monomer.
tRNA(m 1G37)methyltransferase (TrmD) catalyzes the transfer of amethyl group from S-adenosyi-L-methionine (AdoMet) to G 37 within a subset ofbacterial tRNA species, which have a residue G at 361h position . The modified
guanosine is adjacent to and 3' of the anticodon and is essential for the
maintenance of the correct reading frame during translation. We havedetermined the first crystal structure of TrmD from Haemophilus influenzae , asa binary complex with either AdoMet or S-adenosyi-L-homocysteine (AdoHcy) ,as a ternary complex with AdoHcy/phosphate , and as an apo form. The
structure indicates that TrmD functions as a dimer. It also suggests the binding
mode of G36 G 37 in the active site of TrmD and catalytic mechanism. The Nterminal domain has a trefoil knot, in which AdoMet or AdoHcy is bound in anovel , bent conformation.
ReferencesI
2

Ahn , H. J. , Eom , S. J. , Yoon , H. J., Lee , B. I. and Suh , S. W. (2003) J.
Mol. Bioi. 329, 000-000 . (in press)
Ahn , H. J., Kim, H. W., Yoon , H. J., Lee , B. 1. , Suh , S. W. and Yang , J.
K. (2003) EMBO J. 22 , 000-000 . (submitted)

170

ATu1A-4

SUPEROXIDE DISMUTASES FROM HYPERTHERMOPHILES
Geoffrey B. Jameson ," Julian J. Adams ,8 Paul D. Hempstead ,8 Irene
Morgenstern-Badarau ,b James W. Whittaker,c Edward N. Baker,d and Bryan
F. Anderson 8
8Centre for Structural Biology, Institutes of Fundamental Sciences andMolecular BioSciences , Massey University, Palmerston North , New Zealand ;blnstitut de Chimie Moleculaire d'Orsay, Bat. 420 Universite Paris-Sud XI,
91405 Orsay, France; cSchool of Biological Sciences , University of Auckland ,Auckland, New Zealand, dDepartment of Biochemistry and Molecular Biology ,Oregon Graduate Institute School of Science and Engineering , Beaverton ,Oregon 97006 , USA (G.B .Jameson@massey.ac.nz)

The structures of the apo, Fe and Mn forms of the manganese-preferring
superoxide dismutase from the hyperthermophilic microaerobic archaean
Pyrobaculum aerophilum (Pa-SOD) have been determined at 2.0 , 2.2 and 1.9
A, respectively, and the structure of the Fe-specific superoxide dismutase
from the thermophilic methanogenic anerobic archaean Methanobacterium
thermoautotrophicum (Mt-FeSOD) has been determined at 2.6 A.
Corresponding values for R (Rtree) are, presently, 0.16 (0.20) , 0.19 (0 .24),
0.17 (0.20) , and 0.22 (0.24) ; the asymmetric unit is a dimer for Pa-SODs anda tetramer and half-tetramer for Mt-FeSOD.
The extreme thermal stability of Pa-SOD , which survives the autoclaving
necessary to insert metal ions into the E. coli-expressed apo-protein, appears
to arise from a combination of previously identified structural determinants forthermal stability. In particular, both the Pa-SODs and the Mt-FeSOD form
extremely compact tetramers.
In common with all other structurally characterised Mn- and FeSODs ,the central metal ions of Pa-FeSOD, Pa-MnSOD and Mt-FeSOD have an
identical primary coordination sphere . Three histidines , a monodentate
aspartate and a solvent-derived ligand (OH- in oxidised M 111 forms) coordinate
in a trigonal bipyramidal manner, in which the solvent-derived ligand and ahistidine ligand are trans to each other. No differences exist in the second
coordination sphere -for both species a histidine C-H moiety hydrogen bonds
to the solvent-derived ligand , although in many other SODs this aprotic C-H
moiety is substituted by a glutamine NH2 moiety . It is only in the third
coordination sphere, involving the hydrogen-bonding network to the amine
moiety of the coordinated axial histidine that significant differences can befound not only for these SODs but also for other SODs that have been wellcharacterised both structurally and functionally. A methionine thioether moiety
appears to direct a different hydrogen-bonding network to the axial histidine
for Mn-specific SODs, in contrast to Fe-specific SODs where an aliphatic
residue is found at this location , position n on the helix supporting the axial
histidine at position n+3.

171

ATu1A-5
X-RAY ANALYSES OF FAMILY 8 CHITOSANASE FROM BACILLUS SP.
K17
Wataru Adachi , Shinji Shimizu , Tomoko Sunami , Tesuya Fukazawa , Mamie
Suzuki, Rie Yatsunami , Satoshi Nakamura, and Akio Takenaka
Graduate School of Bioscience and Biotechnology, Tokyo Institute ofTechnology, Nagatsuta , Midori-ku , Yokohama 226-8501 , Japan(wadachi@bio. titech .ac.j p)
Glycosylases are classified into 86 families according to the characteristicsof their amino acid sequences. Chitosanase from Bacillus sp. K-17 (C-K17)
belongs to the family 8 and differs from other chitosanases in cleavage site
specificity. The family 8 also includes cellulase, xylanase and lichenase.
Sequence comparison was difficult to distinguish the difference of their catalytic
site. The active site of C-K17 must, however, have some difference in theirthree-dimensional structures. To understand the structural evolution of the
enzymes in the family 8, X-ray analyses of C-K17 have been performed at
different pH .
The two structures of the active (pH 6.4) andinactive (pH3.7) forms are almost the same except the
Glu74 residue that have two conformations at pH3.7,
suggesting its inactiveness. The architecture of the
enzyme is composed of a double-a6-barrel structure,
the protruded loops from the P-sheets making a large
cleft for binding the substrate.
A structural comparison between cellulase from
Clostridium thermocellum (CeiA) and C-K17 shows Fig. 1. Th e double- a 6that their overall structures are similar, but different in ba rrel structure of C-K1 7.
the cleft regions with insertions of additional P-sheets
and loops. The Asp residue , whi ch acts as a proton acceptor in CeiA, ischanged to Asn271 in C-K17 . Instead, the inserted Glu261 residue is locatedclose the catalytic site as aproton acceptor.
Sequence alignment basedon the above structural featureshows that proteins in the family
8 are classified into the threesubfamilies (A, B and C)
according to the proton acceptor,
chitosanases and lichenases
being in the subfamily A,
whereascellulases
andxylanases in the subfamily B. It
Fig. 2. The acti ve sites superimposed between
C-K17 (CPK co lor in gray scale) and Ce iA(gray) .
is thus concluded that the
The in serted loop is circled.
common ancestor of proteins in
the family 8 is diverged into threesubfamilies by inserting a loop to change the specificity of catalytic reactions.

172

ATu1B-1
EXPERIMENTAL SYSTEM FOR X-RAY MAGNETIC DIFFRACTION UNDEREXTREME CONDITIONS
Etsuo Arakawa ," Masahisa lto ,b Naoki lshimatsu ,c Motohiro Suzuki ,d Naomi
Kawamura ,d Hiroshi Sakurai ,b Fumitake ltoh ,b Yoshiya Honma ,e Akira Ochiai ,1Yuichi Akahama ,9 Kazuyuki Matsuda ,9 Yoh Kohori ,h Shunji Kishimoto / Keiichi
Hirano / Hiroshi Maruyama,c Kazumichi Namikawa, 8 and Osamu Shimomurai
80epartment of Physics, Tokyo Gakugei University, Koganei , Tokyo , 1848501 , Japan; bGunma University, Japan; cHiroshima University, Japan;dJASRI/SPring-8, Japan; 8 lnst. of Metal Res., Tohoku University, Japan;
1
Tohoku University, Japan; 9 Himeji lnst. of Tech ., Japan; hChiba University,
Japan; ;PF/KEK, Japan ; jJAERI/SPring-8, Japan (arakawae@u-gakugei.ac.jp)

Experimental system of an x-ray magnetic diffraction with a phase plate
under extreme conditions at BL39XU/SPring-8 is reported. The main parts ofthis system are a superconducting magnet and a diamond anvil cell (DAC) .
This experimental system is made to study magnetic phenomena underconditions of low temperature (5 K) , high magnetic field (6 T) and highpressure (20 GPa).
A method of switching the magnetic field direction has been used so far
to measure magnetic signals in the measurement. It is however not suitable
for measuring magnetic signals with a superconducting magnet. On thecontrary, polarization modulation method which reverses the helicity of theelliptical polarization has been developed to observe magnetic signals in
XMCD[1] and resonant x-ray magnetic scattering experiment[2] . The
polarization modulation method is suitable for measuring the magnetic signals
with a superconducting magnet. Principally, both methods give samemagnetic signals.
The experimental system contains four parts ; (1) a phase plate of
diamond crystal, (2) the superconducting magnet of 6 T , (3) two axis
manipulator for adjusting sample orientation in a DAC , (4) five axis
goniometer for the magnet. Small single crystal of UTe (0 .3 mm x 0.2 mm x
0.1 mm) was mounted in the DAC. Incident x-ray beam of small size (0.1 mm
x 0.1 mm) was irradiated on the sample , and the diffracted x-rays weredetected at sample temperature of 5 K. Instrumental details of the present
system are to be presented.
References
I
Suzuki, M., Kawamura, N. , Mizumaki, M. , Urata , A., Maruyama, H. ,Goto , S. and Ishikawa, T. (1999) J. Synchrotron Radiation 6, 190-192.
2
Hashizume, H. , lshimatsu , N. , Sakata , 0. and Hosoito, N. , eta/. , (1997)
Jpn. J. Appl. Phys. 36, 4252.

173

ATu1B-2
ELECTRONIC DIPOLE-MOMENT OF HYDROGEN ATOM IN A
HYDROGEN-BOND STUDIED BY X-RAY AND NEUTRON

Yukio Noda ,8 Ryoji Kiyanagi ,8 Masashi Watanabe," Hiroyuki Kimura, aAkiko Kojima ,b Tomoyuki Mochida ,c and Tadashi Sugawarad
8

lnstitute of Multidisciplinary Research for Advanced Materials, Tohoku
University, 2-1-1 Katahira , Aoba-ku , Sendai 980-8577 , Japan; bGraduate
School of Science and Technology, Faculty of Science , Chiba University,
Yayoi , Chiba 263-8522, Japan; coepartment of Chemistry, Faculty of Science ,Toho University, Miyama , Funabashi-shi , Chiba 274-8510, Japan;
dDepartment of Basic Sciences, Graduate School of Arts and Sciences, The
University of Tokyo , Komaba , Meguro-ku , Tokyo 153-8902, Japan(ynoda@tagen .tohoku .ac.jp) .
We have performed detailed structure analyses of an isolated hydrogenbond material MeHPLN (C ,40 2H14, 5-methyl-9hydroxy-phenalenone)[1] by Xray and neutron scattering experiments. Since neutrons look nuclei and Xrays look electron cloud, we can get slightly different information from eachtechnique. For neutron experiments , we used a newly developed four-circle
diffractometer FONDER installed at JRR3M Tokai[2]. Maximum Entropy
method[3] is used to get image of distribution of nuclei and electron cloud .
Both structure analyses gave reasonably good R-factors , and essentiallythe positional parameters of skeleton atoms are identical. By comparing the
distribution of electrons and nuclei of hydrogen atoms participating in thehydrogen bond , we have found peculiar difference of the center of mass ofelectrons and nuclei. Such displacement of electrons introduces a local dipole
moment, which may play an important role in the phase transition of thishydrogen-bonded material. The magnitude of the local dipole moment isabout the one seen in the ordinal ferroelectric materials. We also investigated
the temperature dependence of the structure down to 8K through the phasetransition temperature 34K. Ordering of hydrogen atoms in the hydrogen-bondand methyl-molecule as well as the rotational ordering of molecules wererevealed. The transition scheme became clear on this structure analysis . The
complimentary usage of neutron and X-ray will open the field of the structural
physics .
References
Mochida, T., lzuoka , A. , Sugawara , T., Moritomo, Y. and Tokura , Y.
I
(1994) J. Chern Phys. 101 , 7491 .
Noda, Y. , Kimura, H., Kiyanagi , R. , Kojima , A., Morii , Y., Minakawa , N.
2
and Takesue, N. (2001) J. Phys. Soc. Jpn. 70, S456 .
Sakata , M. and Takata , M. (1990) Acta Cryst. A46, 263 .
3

174

ATu1B-3
THREE-BEAM DIFFRACTION ANOMALOUS FINE STRUCTURE OFGALLIUM ARSENIDE

Shih-Lin Chang ," Yen-Ru Lee," Yu . P. Stetsko ,b Sen-Yuan Cheng ," Guin-Gi
Lin ,a Shih-Chang Wonga and Wen-Shien Suna
80epartment of Physics , National Tsing Hua University; bNational Synchrotron
Radiation Research Center, Hsinchu , Taiwan , 300, R.O.C.
(slchang@phys.nthu.edu.tw).

The coherent interaction in three-beam diffraction provides information
about crystallographic phase [1] and resonance phase shift due to electronictransition [2] . This phase information may be useful in understanding theatomic and electronic structures of the constituent atoms of a crystal.
Following this idea a three-beam diffraction anomalous fine structure (OAFS)
technique is developed , where three-beam diffraction intensity as a function of
x-ray photon energy in the vicinity of an absorption edge is measured.
A [111] cut GaAs single crystal is used as a sample crystal. The
diffracted intensity of the three-beam (222/113) case, as well as fluorescence
yield are measured for the photon energies covering the GaK and AsK edges.
The phase information is used to link the real and imaginary parts of theatomic scattering factors considered . Analysis based on the dynamicaldiffraction theory and XAFS gives fine structures of OAFS spectra. The details
about the experimental aspects and the analysis procedures this techniquewill be presented and discussed.
References
1
Chang, S.-L., King, H. E., Huang , M.-T., and Gao , Y. (1991) Phys. Rev.
Lett. 67 , 3113-3116.
2
Stetsko, Yu. P ., Lin , Huang, Y.-S ., Chao , C.-H ., and Chang , S.-L. (2001)
Phys. Rev. Lett. 86 , 2026-2029.

175

ATu1B-4
THE NEW QUASI-LAUE DIFFRACTOMETER AT THE REPLACEMENTRESEARCH REACTOR

Wim T. Klooster
Bragg Institute, ANSTO , PMB 1, Menai , NSW 2234 , Australia(wim@ansto.gov.au)

The new single-crystal diffractometer for the Replacement Research
Reactor will be a quasi-Laue diffractometer, similar to VIVALDI at ILL, France .
It will be competitive with the best instruments currently available . Data
collection times for a normal structure determination will be less than a day, aconsiderable improvement on current data collection times , typically a few
weeks at HIFAR. Also , the crystal size needed for an experiment can as small
3
as about 0.1 mm , opening up new research areas where it has proved3
difficult to grow crystals sufficiently big (several mm ) which are currently
needed . Another area of research opening up will be multiple temperature
and/or pressure measurements.
This new instrument will be a useful tool to obtain structural information
in a timely fashion , where x-rays do not provide enough detail.
The instrument will be on the end of a thermal supermirror guide, and weare exploring the possibility of enhancing the flux further by using a
converging guide section immediately before the instrument itself.
More detailed information on the instrument will be presented.

176

ATu18-5
VALENCE AND STRUCTURAL PHASE TRANSITIONS IN THE SERIESBa2PrRu1-xlrx06
Brendan J . Kennedy. a Leqing Li ,a Christopher J . Howardb and Brett A . Hunte~aThe School of Chemistry , the University of Sydney , Sydney, NSW 2006,
Australia; bANSTO , PMB1 Menai NSW 2234 , Australia;(b.kennedy@chem.usyd.edu.au)

There is considerable interest in the magnetic and electronic propertiesof the 4d and 5d oxides . The double perovskites Ba 2PrRu0 6 and Ba2Prlr0 6
both exhibit rocksalt ordering of the B-type cations (Pr and Ru(lr)). Previous
studies have demonstrated that in the Ru compound the oxidation states are
Pr(lll) and Ru(V) whereas in the lr compound they are Pr(IV) and lr(IV). The
series of oxides Ba 2PrRu 1.xlrx0 6 might therefore be expected to showinteresting properties and structures .
High-resolution powder synchrotron diffraction studies of 15 members inthe series Ba 2PrRu1-xlrx0 6 have been undertaken at the ANBF . These studies
have confirmed that the structure of Ba2PrRu06 is best described in the
monoclinic space group P2 1/n , however we find that Ba 2Prlr0 6 is in fact
tetragonal and can be adequately described in P4 /mnc. The transition
between these two structural types is related to the relative size of the Bcations involved and occurs near x = 0.3. That is the Pr exists in the +3
oxidation state in the Ru rich compounds and this stabilizes a a•b·b- tilt
patterns so that the structure is monoclinic. In the lr rich compounds the Pr ispresent in the +4 oxidation state and the reduction in size of the Pr cation
alters the tilt system is a 0a0 c•. Interestingly although a continuous P4/mnc to
P2 1/n transition is allowed, in the present compounds this is observed to be
first order and there is a two-phase region between x =0.4 and 0.5.
The temperature dependence of the P21/n to P4/mnc transition in two
members of this series have been also investigated using both synchrotron
and powder neutron diffraction methods . These measurements confirm thefirst order nature of the monoclinic to tetragonal transition. In both cases thevolume of the tetragonal structure is noticeably smaller than the monoclinic
structure as a consequence of the change in the Pr valency.

177

ATu2A-1
STRUCTURE OF THE PUTATIVE ANTITERMINATOR PROTEIN Rv1626
FROM MYCOBACTERIUM TUBERCULOSIS
J.P. Marth •v. Feng ,b L. J. Perry,b and P. A. Tucker""EMBL c/o DESY Hamburg Outstation , D-22603 Hamburg , Germany ;bMolecular Biology Institute , UCLA, CA 90095 , USA (premo@emblhamburg .de)

The project is a part of the Mycobacterium tuberculosis structural
genomics project. Rv1626 was initially identified by sequence comparison asa response regulator of a two component system without an apparent
histidine kinase associated with it. Just recently a new domain type wasdiscovered by sequence comparison , the domain was found in (A)miR and(N)asR (T)ranscription (A)ntitermination (R)egulators (ANTAR) [1] . Rv1626
contain a C-terminal ANTAR domain in addition to the N-terminal receiverdomain , common to response regulators .
The untagged Rv1626 was purified from an E. coli expression strain ,and crystallised using the microbatch method . Heavy atom derivitation was
done by a quick soak using sodium iodide . The structure was solved by single
anomalous scattering (SAS) from the anomoluos signal of iodide. The
structure shows high structural similarity to an antiterminator protein AmiR ,except for a kink region in the linker helix between the N- and C- terminal
domains of Rv1626 , which breaks up the proposed coiled coil found present
in the AmiR dimer.

References
1
Shu , C . J. and Zhulin , I. B. (2002) TRENDS in Biochemical Science 27 ,
3-5 .

178

ATu2A-2
STRUCTURAL STUDIES OF LATEXIN, A NOVEL CARBOXYPEPTIDASEINHIBITOR

Anna Aaqaard ,8 Pawel Listwan ,b Nathan Cowieson ,a Thomas Huber,cChristine Wells ,8 Timothy Ravasi ,8 Bostjan Kobe,a,b David Hume, 8 andJennifer Martina
8
lnstitute for Molecular Bioscience , The University of Queensland , Brisbane ,OLD 4072, Australia ; bDepartment of Biochemistry and Molecular Biology,
The University of Queensland , Brisbane , OLD 4072 , Australia ; cAdvanced
Computational Modelling Centre , The University of Queensland , Brisbane ,OLD 4072 , Au stralia (a.aagaard@imb .uq.edu.au)

Latexin is a 222 amino acid protein possessing inhibitory activity against
carboxypeptidase A1 (CPA1) and CPA2 as well as mast-cell CPA[1]. It is
unusual in the sense that it is by far the largest proteina ce ou s
carboxypeptidase inhibitor so far reported[2]and it shows no sequencesimilarity to any of the other known carboxypeptida se inhibitors. Furthermore ,it is the only known CPA protein inhibitor of mammalian origin[1] . Studies on
rat and human latexin showed that it is expressed in many different tissues
including heart, prostate, ovary and kidney[3] .
We found that latexin is also expressed at high levels in mouse
macrophages and is further inducible in these cells by lipopolysaccharide.
Based on these results , latexin was selected as a target for structural studies
as part of a focused high throughput crystallography project at The Universityof Queensland . The gene was cloned and the protein expressed in E. coli. We
used an autoinduction method to produce tens of milligrams of native andselenomethionine labelled protein from 500 ml cultures. Crystals of both thenative and labelled protein were obtained by means of hanging-drop vapour
diffusion using a 96-well fo rmat crystallisation tray. Conditions for freezing
crystals have been identified and frozen crystals diffract to 2.2 A on our inhouse X-ray equipment. Beamtime has been allocated for both MAD andnative data collection at the Advanced Light Source in Berkeley early in 2003.
We expect that the structure of the protein will be solved from the MAD data.
Results from these experiments will be presented at the conference.
References
Normant, E., et al. , Proceedings of the National Academy of Sciences of1
the United States of America, 1995. 92(26) : p. 12225-12229.
Vendrell , J., E. Querol , and F.X. Aviles.Biochimica Et Biophysica Acta2
Protein Structure and Molecular Enzymology, 2000. 1477(1-2): p. 284298 .
Liu, Q., et al. Molecular Biology Reports , 2000 . 27(4): p. 241-246.
3

179

ATu2A-3
CRYSTAL STRUCTURE OF AN ANCIENT CONSERVED DOMAIN

J. Shaun Lott, 8 Mark J. Banfield ,b Jill Sigrell ,c and Edward N. Baker"
8

Laboratory of Structural Biology, School of Biological Sciences, University of
Auckland , Private Bag 92-019 , Auckland 1020, New Zealand ; bDepartment ofBiochemistry , University of Bristol , University Walk, Bristol , BS8 1TD, UK;
cAmersham Pharmacia Biotech , Research and Development, Bjorkgatan 30,
Uppsala Se-751 84 , Sweden (s.lott@auckland.ac.nz)
As a pilot exercise in structural genomics , we selected a small set ofopen reading frames (ORFs) from the hyperthermophilic archaean
Pyrobaculum aerophilum [1], which were annotated as unknowns and forwhich no functional or structural predictions could be made based on aminoacid sequence. We set out to determine the three-dimensional structures ofthe proteins encoded by these ORFs in order to establish if they indeed
represent new protein folds, and to attempt to identify their functions.
Here we report the structure of one of these functionally uncharacterised
proteins , PAE2307 , which is a representative of a conserved family of proteinsfound in both archaeal and bacterial species. As such , it represents an'ancient conserved domain' , which presumably has an evolutionarily distantorigin , prior to the divergence of the bacteria and the archaea .
PAE2307 was expressed in E. coli and purified by immobilised metal
affinity and size exclusion chromatography. It crystallised readily in two crystal
forms . The prevalent form appeared twinned and diffracted to 3 A, but therarer form diffracted to 1.45 A resolution . The non-twinned crystals proved
difficult to reproduce , so screening of potential heavy atom derivatives bynative polyacrylamide gel electrophoresis was used to establish suitable
derivatization conditions. The structure was solved by SAD using datacollected from a single crystal soaked in K 2Pt(N0 2 )4.
PAE2307 exists as a tightly associated hexamer. The monomer iscomposed of two domains. The main domain consists of a five-stranded antiparallel ~-sheet with two a-helices packed against one face and a third helix
packed against the other. The second domain domain consists of a threestranded ~-sheet and a C-terminal helix , which makes extensive contacts withan adjacent subunit in the hexamer. A histidine residue at the start of the ~5strand is modified , possibly by phosphorylation , indicating a putative activesite. The fold of the protein is similar but not identical to a number of otherproteins , the most similar being a thermostable DNA polymerase .
The structure of PAE2307 and the information that it gives towards afunctional assignment for this protein family will be discussed.
ReferencesI
Fitz-Gibbon , S. T. , Ladner, H., Kim , U. J., Stetter, K. 0 ., Simon , M. 1. ,and Miller, J. H. (2002) "Genome sequence of the hyperthermophilic
crenarchaeon Pyrobaculum aerophilum." PNAS (2002) 99, 984-989.

180

ATu2A-4
RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
Shigeyuki Yokoyama
RIKEN Genomic Sciences Center, RIKEN Harima Institute at SPring-S , andDepartment of Biophysics and Biochemistry, Graduate School of Science ,The University of Tokyo (yokohama@biochem.s .u-tokyo.ac.jp)

The RIKEN Institute has started the Structural Genomics/Proteomics
Initiative (RSGI) (http://www.rsgi.riken.go.jp) at the Genomic Sciences Center(GSC) and the Harima Institute at SPring-S . RSGI is now integrated into theJapanese national project , National Project on Protein Structural andFunctional Analyses , which studies both structures and functions of proteinsin selected biological systems. We have been determining the threedimensional structures of proteins of sequence families and analyzing
molecular and cellular functions of these proteins in order to establish thestructure-function relationships.
RSGI has two main components. One is genome-driven structural
genomics to analyze the structures and functions of proteins encoded by the
genome of an organism. The other is to study structures and functions of
medically/biologically important proteins from higher eukaryotes incollaboration with pharmaceutical and chemical companies. For the genomedriven structural genomics , a eubacterial extreme thermophile , Thermus
thermophi/us HB8, and an archaeal hyperthermophile , Pyrococcus horikoshii
OT3 have been selected as the target organisms. The other component oftargets are higher enkaryotes , human , mouse , and Arabidopsis thaliana.
Mouse and Arabidopsis full-length eDNA clones have been collected andanalyzed by H. Hayashizaki and K. Shinozaki , respectively. Human cDNAs
collected by the Kazusa DNA Institute and others are also used . The target
proteins are selected by bioinformatics of both sequence clustering withrespect to domains and functional (interaction) proteomes of biological andmedical interest. Protein-protein interactions are analyzed mainly by mass
spectrometry, while natural and non-natural ligands are screened in silica andexamined by wet experiments . For protein sample preparation, the cell-freeprotein synthesis method is routinely used in addition to authentic
recombinant methods. After the screening step of solubility , structural
stability, feasibility of large-scale expression and crystallizability , large-scale
sample preparation is conducted. Selenomethionine substituted proteins for
X-ray crystallography are prepared by cell-free method . Robotic techniques
are introduced and large protein preparation facilities are established .
We use both X-ray crystallography and NMR spectroscopy to the same
extent. For X-ray crystallography , in addition to other structural biology
beamlines, two beamlines at SPring-8 in Harima, dedicated to structural
genomics are in use. The NMR methods can be applied for proteins that do
not crystallize.

181

ATu2B-1
DETERMINATION AND REFINEMENT OF A DISORDERED HOST-GUEST
CRYSTAL STRUCTURE USING AN EVOLUTIONARY ALGORITHM INCOMBINATION WITH MONTE CARLO METHODS
H.-B. BUrqi. 8 and T. Weberb
8

Laboratory of Crystallography, University of Berne, Freiestr. 3, CH-3012
Bern ; blaboratory of Crystallography, ETH Zentrum , CH-8092 Zurich ,Switzerland (hans-beat. buergi@krist. unibe.ch)

The complex diffraction pattern of a heavily disordered host-guest
compound [perhydro-triphenylene with 1-( 4-nitrophenyl)piperazine(5C1 sH3o·C10H13N30 z)l has been investigated with synchrotron radiation andan area detector. A complete , three-dimensional data set collected at 120 K
revealed a rich variety of features including one- , two- and three-dimensional
diffuse scattering , as well as incommensurate satellites. Most of the scattering
could be assigned to R /S occupational disorder of the chiral host molecules ,to positional disorder of the guest molecules or to loca l distortions of theaverage structure. Assignments are based on the disorder deduced from theaverage structure and the molecular form factors of host and guest molecules
both of which show characteristic patterns in reciproca l space. Two smaller,
orthorhombic twin fragments and an additional phase with hexagonal
symmetry have also been found [1].
An evolutionary algorithm called ·differential evolution' is combined with
Monte Carlo simulation to determine and optimise models of the disordered
crystal structure . Requirements for successfully finding the parametersdescribing disorder from diffuse scattering data are discussed . The algorithm
is applied to resolving the racemic and associated displacive disorder of theperhydrotriphenylene host substructure. Refinement results in a very goodvisual agreement between observed and calculated intensities and in a
relatively low value of R ctiffuse = 0.148(3). Initially the computations fordetermining and refining the structure took 29 d with five to ten workstations
running in parallel. Improved computing power and more efficient programs
have reduced this time to 3-4 days. Analysis of the progress of the structure
determination shows that the essential information ca n be obtained within a
few hours. Limits of the technique and strategies to further optimise theprocedure are discussed. Nearest neighbour correlations are -0.15 along x,-0 .28 along y and 0.86 along z [2] .
References Weber, Th. , Estermann , M. A. and BUrgi , H. -B. (2001) Acta
Cryst. 857, 579-590.
2
Weber, Th . and BUrgi , H. -B. (2002) Acta Cryst. A58 , 526-540.

182

ATu2B-2
THE IMPORTANCE OF MULTISITE CORRELATIONS IN DISORDERED
STRUCTURES
T.R. Welberry and R.L. Withers
Research School of Chemistry, Australian National University, Canberra , ACT0200 , Australia (welberry@rsc.anu.edu .au)
Conventional crystal structure determination using Bragg reflections reveals
only single-site properties of a structure (average atomic positions mean-squareatomic displacement amplitudes, site occupancies). Diffuse scattering, on theother hand , being the Fourier transform of the pair correlation function contains
information about two-site properties and gives direct information about themutual behaviour of (neighbouring) pairs of atoms. Since many theories of how
atoms and molecules interact involve pair interactions (e.g. Lennard Jones
potential , Buckingham potential etc.) it might be supposed that there will be adirect correspondence between the observed diffuse scattering and the pairinteractions that may be considered to be the fundamental parameters of thesystem . It should be noted , however, that without any direct phase information
the diffraction experiment does not contain any information about multi-sitecorrelations.
If a system has properties which stem from multi-site interactions then ,although diffuse scattering effects may be observed , these arise only from theindirectly generated pair correlations. In such circumstances there is no direct
link between the observed pair correlations and the fundamental inter-atomic
interactions and little purpose is served by trying to interpret the scattering interms of a model formulated in terms of pair-interactions. In this paper we
describe examples of real systems in which complex diffraction patterns can be
explained by extremely simple models involving multi-site atomic interactions.
The first of these examples involves 0/F ordering and associated Mo ion
shifts in the system K3Mo0 3F3 . Monte Carlo modelling is used to show how thelatter, when coupled with an appropriate local crystal chemical constraint (a multisite interaction) , can give rise to the observed highly structured diffuse scattering
patterns. Examples of different sections of the calculated diffraction pattern are
shown in Fig .1.

~~ ~ ~ ggg.g~ ' .'~ ~62~6~~~~
0<2,
0 ~'
·r

0 0 0 0 r -, 0 0 0 0o·o ·o· c · · ·')·o·o·o

r

::J

c.

~ g~}~ ~ i}g? ~ ~~~o~ 2~b·r .~,oooooor, ·o ·o·o ·o ·r

.
.,

o
.:..

.

Fig. 1. Three example reciprocal sections (1 00, 113, 331) of the K3Mo03F3
system, calculated from a Monte Carlo model based on a simple chemical constraint.

A second example involves Bi/Zn cation ordering in the cubic pyrochlore(Bi, 5Zn 0.5)(Zno.5Nbt5)0?. Here too a multi-site interaction based on a simple
chemical constraint is required to explain the observed diffraction patterns.

183

ATu2B-3
STRUCTURE SOLUTION AND REFINEMENT OF KNbOB20sA COMMENSURATE MODULATED STRUCTURE
Siegbert Schmid
School of Chemistry, The University of Sydney, NSW 2006 , Australia(siegbert@chem.usyd.edu.au)
Non-centrosymmetric oxo pyroborates, AMOB 20 5 (A = K, Rb , Cs, Tl; M =Nb, Ta) [1-5), 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 Pmn2 1 setting of
CsNbOB20 5 [4]). Despite the availability of single crystals for all compounds ,single-crystal structure refinements have only been reported for TINbOB 20 5 [1),RbNbOB 20 5 [3], CsNbOB 20 5 [4-5] and CsTaOB 20 5 [5]. The Cs compounds arereported without superstructure, i.e. to be of the basic structure type, while the Tl
compound displays a two-fold superstructure and the Rb compound a five-foldsuperstructure, however, the structure wasn't truly refined as a superstructure.
An electron diffraction and single-crystal X-ray diffraction investigation of
RbNbOB 20 5 verified the existence of an exact five-fold superlattice along b [6] . A
characteristic hierarchical intensity distribution among the satellite reflections wasstrongly suggestive of a modulated structure in that the Gp ± 2J5bp* (p for parent)
satellite reflections were clearly much stronger than the Gp ± 1J5 bp * satellite
reflections). For KNbOB 20 5 the single-crystal X-ray diffraction patterns were very
similar to the patterns for RbNbOB 20 5 . The superlattice along b was exactly
eight-fold, with the Gp ± 3J8bp* (p for parent) satellite reflections clearly thestrongest satellite reflections. While the Rb compound was best refined as anincommensurate modulated structure, solution and refinement of KNbOB20 5
showed , that this structure was best described as a commensurate modulated
structure .
In both refined structures apparent valence calculations show, that rubidium
and potassium , respectively, are satisfactorily bonded . While caesium, thelargest A ion in this family realises an unmodulated structure, the modulation in
the other compounds provides the A ions with an adequate bonding
environment. If Rb, Tl and K were to form the same structure as Cs, they would
be significantly underbonded. A calculation of bond valence sums after simply
substituting these cations for Cs gives values of 0.59, 0.46 and 0.42 ,respectively.
References
I
Gasperin, M. (1974), Acta Crysta. 830, 1181- 1183.
2
Bau cher, A. and Gasperin, M. (1975), Mat. Res. Bull. 10, 469-472.
3
Baucher, A. , Gasperin , M. and Cervelle, B. (1976), Acta Crysta. 832, 2211 - 22 15.
4
Becker, P., Bohaty, L. and Frohlich, R. (1995), Acta Crysta. C51 , 1721- 1723.
5
Akella , A. and Keszler, D. A. (1995), J. Solid State Chem. 120, 74- 79.
6
Schmid, S. , Withers, R. L. , Corker, D. and Baules, P. (2000), Acta Crysta. 854,
558-564.

184

ATu2B-4
APPLICATION OF A SIX-DIMENSIONAL TWIN REFINEMENT TECHNIQUETO MULTIPLE-TWINNED CRYSTALS OF Cu2SnS3, CugGeS5 andAg7TaS5
M. Onoda , H. Wada , X. -a . Chen , A. Sato, and M. Ishii
Advanced Materials Laboratory, National Institute for Material Science ,Namiki 1-1 , Tsukuba , lbaraki , 305-0044 , Japan (ONODA.Mitsuko@nims.go.jp)
The twinned structure could be described by a six-dimensional formalism
and refined using the multi-dimensional refinement program FMLSM [1,2]. Whenthe reflections can be indexed based on two sets of basic vectors , a, b, c and a',b ', c', each reflection is expressed by q=ha*+kb*+lc*+h'a'*+ k'b'*+fc'*.
Symmetry operations are also expressed in the (3+3)-dimensional formalism [2] .
Those for the major domains (a, b, c) are given by the scheme g=(( R 0 I 0 R) I
(vlv)) , where R and v are the matrix and the vector of the corresponding threedimensional symmetry operations. The symmetry operations for the minor
domains (a', b', c') are obtained by multiplying the six-dimensional twinning
operation t={ T I 0} into the major domain symmetry operations g where T is thematrix (000100 I 000010 I 000001 1100000 I 010000 I 001000) [2].
The X-ray diffraction data of low-symmetry Cu 2SnS 3 were obtained from atwinned monoclinic crystal (a=6.653 , b=11 .537 , c=6.665 A ~=1 09.39!) [3] . The
reflections were indexed on the basis of a, b, c and a', b', c', where a'*=-a*,b'*=b*, c'*=-(2/3)a*+c*. The reflections are of three groups, the first is assignedby both of hk/000 and OOOh 'k'l' and considered to be common to two twin
domains, while the second (hk/000) comes from the major domain and the third(OOOh 'k'/) comes from the minor domain. The structure was described based ona, b, and c with space group Cc. Refinement was performed using all reflections
through FMLSM . The agreement was satisfactory with 52 structural parameters
Observed reflections ofand 2 scale factors; RF=0.036 and wRF=0.038.
Cu 8GeS 6 [4] seemed to be from a twinned rhombohedral crystal (a- 9.9 A anda- 90 !), the major ones based on a, b, c and minor ones based on a'=-a, b'=-b,c'=-c. The model proposed using powder data was that with A=7 .0445 ,8=6.9661 , C=9.8699A and Pmn2 1. After selecting new bases a=A+B, b=B-A,
c=C, the lattice constants were a=b= 9.9073, c=9.8703A, a=~=90! , r-90.642!.
Symmetry operations were also converted into the formula based on C-lattice:generator sets are 1/2+x,1/2+y, z; y,x,z; 3/4-y,1/4-x,1/2+z. The major groupreflections and six major domains with the twin operations x,y,z, y,z,x, z,x,y, x,-y,z, -y,-z, x, and -z,x,-y were considered . Then the minor group reflections and six
minor domains were added. Besides structural parameters, 12 scale factors
were considered as parameters in refinement. The agreement was satisfactoryfor 1804 reflections; RF=0.083 and wRF=0.091 .
In a similar manner, the structure of the monoclinic low-temperature phaseof Ag1TaS 6 was examined on the basis of X-ray diffraction data from a 24-foldtwinned crystal with 12 major domains and 12 minor domains.
References
Kato, K. (1994) Acta Cryst. A50 , 351-357 .
1
Kato, K. (1997) Z. Kristallogr. 212 , 423-427 .
2Onoda, M., Chen X.-a., Sato, A. and Wada, H., (2000) Mat. Res. Bull. 35, 1563-1570.
3
Onoda, M., Chen X.-a., Kato, K., Sato, A. and Wada , H., (1999) Acta Cryst. 855,4
721-5.

185

186

Tuesday August 12

AsCA'03/Crystal-23

ABSTRACTS
POSTER SESSIONS

187

ATuP-01
ELECTRON MOMENTUM DENSITY STUDY OF ICOSAHEDRAL Cd 84 Yb 16

Y. Sakurai ," J . T. Okada ,b Y. Watanabe ,b S. Nanao ,b R. Tamura ,< S.
Takeuchi ,<Y. Yokoyama, d N. Hiraoka,e and M. ltou•"Japan Synchrotron Radiation Research Institute ~JASRI} , SPring-8 , 1-1-1
Kouto, Mikazuki , Sayo , Hyogo 679-5198 , Japan ; Institute of Industrial
Science , University of Tokyo, 4-6-1 Komaba, Meguro , Tokyo 153-8505,
Japan; <science University of Tokyo , Nod a, Chiba 278-8510 , Japan ; dHinejiInstitute of Technology, 2167 Himeji, Hyogo 671-2201 , Japan; eEuropean
Synchrotron Radiation Facility (ESRF) , BP 220 , F-38043 Grenoble Cedex,
France (sakurai@spring8.or.jp)
Quasicrystal is a new form of solids that differs from crystalline andamorphous materials since it possesses quasi-periodicity and non-crystallographic
rotational orders. The presence of a pseudogap is one of the characteristics inquasicrystals and is of great importance to understanding the cohesion
mechanism of the unconventional compounds. The pseudogap opens in thedensity of states across the Fermi level, possibly by two scenarios; one is thequasi-Brillouin zone- Fermi surface interaction (called Hume-Rothery mechanism)and the other is the sp-d hybridization.
Icosahedral Cd84 Yb, 6 is a stable binary quasicrystal that has been recently
discovered by Tsai et a/.[1] . A pseudogap signature has been observed in thehigh-resolution photoemission spectra [2] . Theoretically, Ishii and Fujiwara havecarried out computations on the 1/1 cubic approximant Cd 6Yb and concluded thatthe hybridization of the d states of Yb with a wide sp band plays a major role in thepseudogap formation while the Hume-Rothery mechanism is minor [3].
In this conference, we present the electron momentum density distribution(Compton profile) of icosahedral Cd 84 Yb 16 obtained using the high-resolution
Compton scattering spectrometer [4] at SPring-8. The energy of the incident x rays
was 116 keV and the scattering angle was 165 degrees. The overall momentum
resolution was 0.16 atomic units.
The experimental valence-electron Compton profile is decomposed into twopartial profiles: an inverted parabola-like profile and a broad Gaussian-like profile. It
is found that the Fermi sphere, whose radius is estimated from the number ofelectrons under the inverted parabola-like profile, is just inscribed in the quasiBrillouin zones defined by the strong (211111) and (221 001) diffraction planes.
The broad Gaussian-like profile is accounted for by the Yb-5d states which are
lowered below the Fermi level by hybridization with the sp bands. These results
show that the Hume-Rothery mechanism and the sp-d hybridization effects work
cooperatively for forming the deep pseudogap and thus stabilizing the icosahedralphase of Cd84 Yb,6.
References
1
Tsai, A. , P., Guo, J., Q., Abe , E., Takakura , H. and Sato, T. , J. (2000) Nature(London) 408, 537.
2
Tamura , R. , Murao, Y. , Takeuchi, S., Kiss , T., Yokoya , T. and Shin, S. (2002) Phys.
Rev. 8 65, 224207.
3
Ishii , Y. and Fujiwara, T. (2001) Phys. Rev. Lett. 87, 206408.
4
Hiraoka, N., ltou , M. , Ohata, T. , Mizumaki, M., Sakurai, Y. and Sakai, N. (2001) J.
Synchrotron Rad. 8, 26-32.

188

ATuP-02
CHARGE DENSITY STUDIES OF Z' = 2 MOLECULES. POSSIBILITIESAND LIMITATIONS
Dai Hibbs , Mark P. Waller and Jacob Overgaard
School of Chemistry, University of Sydney , NSW 2006, Australia(hibbs_d@chem.usyd.edu.au)
Experimental X-ray charge density (CD) studies of molecules with morethan one molecule in the asymmetric unit are relatively rare [1]. On the contrary ,such occurrences are abundant in structural chemistry, evidenced by the 22015
hits of Z''c/2. in CCDC , corresponding to 8% of all published structures [2]. Thus, it
is apparent that such compounds have been avoided by the CD community. Thi s
is due to several factors . Firstly, the increase in the number of parameters is asignificant drawback, since a successful multipole model in most cases requires
more than 300 reflection s per non-hydrogen atom . Secondly , one of themolecules often experiences a rather weak crystal field; hence the thermal
motion of this molecule can be severe and the molecule may even bedisordered . Thirdly, there can exist significant correlations between multipole
parameters from different molecu les. All in all , CD studies of this type of crystal
structures offer a range of problems that need to be addressed .
Th ere are, however, large potential benefits of studying the CD in suchmolecules . In the case of rigid molecules, it allows the determination of multipole
parameters of identical atoms in slightly different environments without thepresence of systematic errors intrinsic in a comparison of different experiments.
Hence, it is important in the evaluation of transferability of atomic multipole
parameters [3] .
This presentation will outline the details of experimental and theoreticalcha rg e density studies of three organic molecules all having two molecules in theasymmetri c unit (see Figure) . Besides a discussion of the prospects of giving an
independent description of the two molecules in the same study, each of thethree systems represents interesting chemical and theoretical issues that will be
addressed .

FLAVONEFLUORENOL

TFIPN

ReferencesI

2
3

Gatti , C., May, E., Destro, R. and Cargnoni, F. (2002) J. Phys. Chem. A. 106, 2707;
van Reeuwijk, S. J., van Beek, K. G. and Feil , D. (2000) J. Phys. Chem. A. 104,10901 .
eeoc search 13/3/03 gave 22015 hits equalling Z'V2 out of 272066.
Pic hon-Pesme, V ., Lecomte , C. and Lachekar, H. (1995) J. Phys. Chem. 99, 6242 .

189

ATuP-03
CRYSTAL EXPLORER: A GRAPHICAL USER INTERFACE FORDISPLAYING AND MANIPULATING HIRSHFELD SURFACES AND
FINGERPRINTS FOR CRYSTAL ENGINEERING APPLICATIONS

Dylan Jayatilaka, Daniel Grimwood , and Stephen Wolff
Department of Chemistry, University of Western Australia , Crawley, WA 6009,
Australia (dylan@theochem.uwa .edu .au)

The Hirshfeld surface is a region enclosing a moeity in a crystal , within
which more than 50% of the electron density comes from that moeity. The
surface can be coloured in a number of ways , to highlight local packing
interactions in the crystal. In addition, a fingerprint of the surface can be madewhich quickly displays in a 2D format inter-moeity interactions - thus making
comparison of crystalline interactions in different crystal structures
stra ig htforwa rd [ 1].
Crystal Explorer is a graphical user interface (GUI) for manipulating
Hirshfeld surfaces [2] . Examples of the GUI and its uses will be presented .
ReferencesI
See, e.g ., McKinnon, J. J. , Mitchell, A. S. , and Spackman , M. A. (1998)
Chem. Eur. J. 4 , 2136-2141 .
2
Crystal Explorer: A GUI for manipulating Hirshfeld Surfaces,
www.theochem .uwa.edu.au/hirshview.

190

ATuP-04
CRYSTALLIZATION OF SECRETED PROTEIN BY COMPLEXATION WITH
AN ANTIBODY FRAGMENT

Taro Tamada ,8 Keiko Kurosawa ,8 Uichi Nishiyama,b Tomoaki Kuwaki ,b andRyota Kuroki 8
8Pharmaceutical Research Laboratories, Pharmaceutical Division, Kirin
Brewery Co. , Ltd. , 1-13-5 Fukuura, Kanazawa-ku, Yokohama , Kanagawa
236-0004, Japan; bPharmaceutical Development Laboratory, Pharmaceutical
Division, Kirin Brewery Co., Ltd., 3 Miyahara-cho, Taka saki 370-1295, Japan(ttamada@kirin.co.jp)

It is known that secreted glycoproteins , such as cytokines, are hard to
crystallize in spite of their industrial importance .
Our approach for
crystallization of these proteins is the use of antibody fragment (Fab). The
first example was the crystallization of thrombopoietin (TPO). TPO is acytokine which primarily stimulates megakaryocytopoiesis andthrombopoiesis. TPO was crys tallized by comp lexation with Fab derived
from a neutralizing monoclonal antibody [1) . The tertiary structure of TPO
was also successfully determined only by molecular replacement techniqueusing the known coordinates of Fab as a search model. It was confirmed thatthe use of Fab was effective not only for protein crystallization , but also forphase determination.
The second example is the crystallization of soluble receptors.
The
extracellular domain of receptors is the entrance of signals induced by ligand
binding . The interaction of the receptors with several drug candidates iswidely investigated . To elucidate activation mechanism of TPO receptor by
ligand binding , we aim to determine the complex structure of TPO and its
receptor by complexation with Fab. The extracellular region of human TPOR
expressed using by the animal cell was used for crystallization. Several Fabfragments derived from a monoclonal antibody that recognize the extracellulardomain of TPOR were used for the search of crystallization condition . Aftervarious screening for crystallization condition , TPO/TPOR/Fab complex , andTPOR/Fab complex, were successfully obtained with the use of one of theFab fragments. Although further optimization of crystallization condition isneeded , the use of Fab was effective approach for TPOR crystallization . The
structure information of TPOR will give the useful information forpharmaceutical development of TPO .
References
1 Kuroki , R., Hirose, M., Kato , Y., Feese , M. D., Tamada , T., Shigematsu , H. ,Watarai , H. , Maeda , Y. , Tahara , T., Kato , T. , & Miyazaki , H. (2002) Acta
Cryst. D58 , 856-858.

191

ATuP-05
CRYSTALLIZATION OF ALPHA-AMYLASE AS A MODEL PROTEIN FOR
DEMONSTRATING THE EFFICACY OF THE COUNTER-DIFFUSIONTECHNIQUE UNDER MICROGRAVITY CONDITIONS

Masaru Sato,a Hiroaki Tanaka ,"·b Koji lnaka ,c Sachiko Takahashi ,b Satoshi
Sano ,a Susumu Yoshitomi ,a and Hiroshi Komatsud
8
Space Utilization Research Center, National Space Development Agency ofJapan (NASDA). lbaraki 305-8505 , Japan; b Japan Space Utilization
Promotion Center, Tokyo 169-8624, Japan ; cMaruwa Food Industries, Inc.,
Nara 639-1123 , Japan; dlwate Prefectural University, lwate 020-0193 , Japan(PXW0167 4@nifty.ne.jp)
It is necessary to work for a well characterized model protein for
demonstrating the efficacy of the new protein crystallization method . Therefore
we chose alpha-Amylase as a representative of many significant proteins for its
molecular weight and biochemical characteristics. Alpha-Amylase is a
glycoprotein derived from Aspergillus oryzae , which catalyze the hydrolysis of thealpha-1 ,4 glycosidic linkage in starch . The major problems of the crystallization ofalpha-Amylase on the ground using PEG as precipitant are the incorporation of
isozyme and the highly clustered morphology, which cause difficulties to obtain
monocrystal on the ground experiment. We expect that the microgravity effects
can provide the optimal diffusive environment to overcome these problems.
Crystallization of alpha-Amylase was carried out by counter-diffusion
method using Granada Crystallization Box (GCB)[1] with the condition of 90
mg/ml protein, 40%(w/v) PEG 8000, 2mM CaCI2, and 50mM Tris-HCI pH 7.5 at
20C under microgravity for 10 weeks in Odissea mission in 2002. On the ground,crystals were appeared within 10 days as highly clustered crystals at theacupunctured-end of the capillary . Each crystal belonged to the orthorhombic
space group P2,2,2, with unit cell dimensions a=50.2 b=65.7 c=130.8, anddiffracted beyond 1.6 A resolution . In space, however, crystals were obtained asa single crystal. They belonged to the tetragonal space group P4 3212 with unit
cell dimensions a=b=67.4, c=268.0 A, which had the same space group asreported previously [2] . Preliminary diffraction experiments at ambient
temperature at SPring-8, BL 12b2 indicated that diffraction pattern extends
beyond 1.6 A resolution . Three crystals were grown only in one capillary. There
were no crystal observed in other five capillaries, however, the clusteredorthorhombic crystals had started to grow within 24 hours after landing.
These results suggest that the mechanism of nucleation and/or growth ofprotein crystal under microgravity is quite different from those under gravity.
Characterization of crystals obtained with and without gravity will be reported indetail.
Acknowledgements: The flight opportunity of Odissea mission was donated byfavour of ESA and Dr. Garcia-Ruiz in University of Granada , Spain .
References
I
Garcia-Ruiz, J.M. and Moreno, A. (2002) Acta Cryst. D58, 1638-1642.
2
Ninomiya, K., Yamamoto, T ., Oheda , T ., Sato, K., Sazaki , G. andMatsuura , Y. (2001) J. Crystal Growth 222, 311-316 .

192

ATuP-06
INVESTIGATION OF CRYOPROTECTANT CONDITION FOR PROTEINSTRUCTURE ANALYSIS USING CRYOPROTECTANT DATABASE

Sachiko Takahashi ,8 Takashi Yoshimine,8 Masaru Sato ,b Hiroaki Tanaka ,a,b
Kensaku Hamada,c and Susumu Yoshitomib
aJapan Space Utilization Promotion Center, Tokyo 169-8624, Japan ; bSpace
Utilization Research Center, National Space Development Agency of Japan(NASDA) , lbaraki 305-8505 , Japan; cShimane University, Shimane 690-8504 ,Japan (PXW01674@nifty.ne.jp)
To perform X-ray diffraction experiment properly and obtain the complete
data sets, it is essential to protect protein crystals from the serious damages
caused by synchrotron X-ray beam . It is well known that freezing crystals
reduces radiation-induced damages on crystals, however, inadequate
cryoprotectants and operational techniques frequently deteriorate valuable
crystals. Therefore it is very important to decide appropriate conditions forfreezing each protein crystal. Since NASDA has promoted protein crystallization
experiments in space twice a year since 2003, it is necessary to improve thecryoprotective technique for crystals grown in space, which is the main purpose
to construct this database.
We picked up 279 cryo-data mainly from articles in Acta Crystallographica
0 2000 and 2002. The information we extracted were the name of the protein ,origin , PDB reference , precipitant, crystallization method , cryoprotectant, freezing
method and freezing temperature. The database is available free in the following
address: http://idb.exst.nasda.go.jp/. We will continue to update (200 more data
this year) and analyze these data sequentially.
According to the investigation from the database, 54% of the crystals were
flash-frozen and glycerol was most commonly used as cryoprotectant in 48% of
the flash-frozen crystals. In case of flash-frozen crystals, the relationshipbetween PEG 4K % and glycerol % in cryoprotectant is shown in Fig. 1. This
figure indicates that composition of glycerol as cryoprotectant for flash-freezing
can be preliminary optimized according to the concentration of PEG used as
precipitant. We will also show the relationships between glycerol % and otherprecipitants in detail.
The crystallization occurs in capillaries using counter-diffusion technique for
NASDA"s experiment in space. Taking advantage of it, we came up with the ideaof the simple method
RelationshPbetween PEG 4K% end Glycerol%thesoakingforcrystals in glycerol as
30,.-------------------,
cryoprot-ectant mildly
25 f---~'"'"~-....::::-~~-----------l
within the capillaries.
We will report this.......--..:....
method in detail. We
these
apply
will
lO f - - - - - - - - - - - - - - - - - - + --lfortechniques
freezing the crystalsoL--~-~-~~-~-~-~~-~-~
which will return from
40
35
30
25
15
10
0
PEG4K~
InternationaltheSpace Station in May
2003 .

w r-----------------~--=-----------~

15 ~-------------------~~ ;::-r-~

193

ATuP-07
CRYSTAL STRUCTURE OF NONADECANE-1,19-DITHIOL
H. Shimizu ," K. Uno," Y. Ogawa ,b and N. Nakamura 8
Materiai-Energy Science and Engineering Major, Graduate School of
Science and Engineering , Ritsumeikan University, 1-1-1 , Nojihigashi ,Kusatsu , Shiga 525-8577 , Japan; bDepartment of Chemistry, Faculty of
Science , Kumamoto University, 2-39-1 , Kurokami , Kumamoto 860-8555,
Japan (rc005999@se.ritsumei.ac.jp)

8

It has been well known that long-chain aliphatic compounds with a terminal
mercapto group form a self-assembled monolayer on a surface of gold[1]. In thisstudy, the crystal structure of nonadecane-1 ,19-dithiol, HS- (CH 2 ) 1g-SH , wasanalyzed.
The single crystal of the title compound was obtained from a solution with amixed solvent of ethyl acetate and ethanol (2 :1) by the slow evaporation method.
All measurements were made on a Rigaku AFC-5R diffractometer with graphite
monochromatized Cu-Ka radiation . The crystal structure was a triclinic system(a=4 .7628(6)A, b=5.5741 (7)A, c=40.927(5)A, a=92.51 (1) , j3=92 .02(1) ,y=102 .57(1) , Z=2) with a space group P-1 . All calculations were performed
using the Crysta!Structure crystallographic software package . The structure wassolved by direct methods with S/R92. The non-H atoms were refined
anisotropically. The methylene H atoms were52
located at idealized positions, and were allowed
Cl9
to ride on the parent C atoms (C-H=0.95A).
The isotropic displacement parameters were c J ~set at 1.2Ueq of the parent atom. However, the mposition of mercapto H atoms could not be
determined from a difference Fourier map. The c"
final refinement was made by full-matrix leastsquares based on 3809 observed reflections c 12
(F2>-3a(F2 )) . The refinement was concluded
with final reliability factors R(F2>2a(F2 ))=0.060, ctowR(F2 )=0 .135.
As is shown in Fig.1 , the hydrocarbon c'skeleton included both terminal mercapto
groups had an all-trans conformation . In the c•crystal structure, the long axis of the molecule
is inclined to the ab plane.
In this study, a feature of the crystal Cl
structure of nonadecane-1 ,19-dithiol will be
discussed with those of other alkane-a ,wdithiols[2-4].
sl

Cl7

C ll

C l3

CIO

C9

C7

C5

C)

Cl

+a

References
Fig.1 The molecular and crystal
1
Drawhorn, R.A. and Abbott. N.L. (1995) J.
structure of nonadecane- 1,19-dithiol.
Phys. Chem. , 99, 16511 .
Thalladi, V.R. , Boese, R. and Weiss, H.C. (2000) J. Am. Chem. Soc. , 122, 11 86.
2
3
Nakamura, N., Uno, K. and Ogawa, Y. (2001) Acta Cryst., E57, o508.
4
Nakamura, N., Uno, K. and Ogawa, Y. (2001) Acta Cryst., E57, o505.

194

ATuP-08
A STRUCTURAL STUDY ON THE MONOSUBSTITUTED FERROCENEDERIVATIVES

Y. Kawamura , Y. Okada , K. Uno and N. Nakamura
Material-Energy Science and Engineering Major, Graduate School of Scienceand Engineering , Ritsumeikan University, 1-1-1, Nojih igashi , Kusatsu , Shiga
525-8577 , Japan (rc004983@se.ritsumei.ac.jp)
The crystal structures of o-nitrophenylferrocene , m-nitrophenylferrocene
and p-nitrophenylferrocene were already analyzed by other workers[1] . In thisstudy , the crystal structures of o -a cetylphenylferrocene and p acetylphenylferrocene were determined by the X-ray diffraction method inorder to discuss an influence of the substituent over the crystal structures . All
measurements were made on a Rigaku AFC-5R diffractometer with graphite
monochromatized Cu K a radiation . All calculations were performed using
Crysta!Structure[2] crystal structure analysis package. The single crystals ofo-acetylphenylferrocene and p-acetylphenylferrocene were obtained from asolution with a mixed solvent of benzene : ethanol (1 :3) and ethyl acetate :ethanol (1:4) by the slow evaporation method , respectively.
The crystal structure of o-acetylphenylferrocene was a orthorhombic
system (a=7 .552(2)A, b=31.114(2)A, c=5.901 (3)A, Z=4) with a space groupP2 12 1 2 1 . The structure was solved by direct methods with S/R92[3) andexpanded using the Fourier Technique. All non-H atoms were refined
anisotropically. The H atoms were located from a difference Fourier map, andwere allowed to ride on the parent C atoms to which they are attached . The
H-atom isotropic displacement parameters were set at 1.2Ueq of the parent
atom. The final refinement was made bj, full-matrix least-squares based on
221560 observed reflections (F2>-3a (F )). The R(F > 2 a (F )) value wasconverged to 0.034 by the final refinement.
The crystal structure of p-acetylphenylferrocene was a orthorhombic
system (a=10 .544(5)A, b=33.998(4)A, c=7.725(5)A, Z=8) with a space groupPb ca . The structure was solved by direct methods with S/R92[3] andexpanded using the Fourier Technique. All non-H atoms were refined
anisotropically. The H atoms were introduced at their theoretical positions andallowed to ride on the C atoms to whi ch they are attached . The H-atom
isotropic displacement parameters were set at 1.2Ueq of the parent atom . The
final refinement was made by full-matri x least-squares based on 2532
22
observed reflections (F2>-3a (F2 )) . The R(F >2a (F )) value was converged to
0.096 by the final refinement.
References
1. Roberts, R.M.G., Silver, J., Yamin , S.M., Drew, M.G.B. and Eberhardt, U.
(1988) J. Chern . Soc., Dalton Trans ., 6, 1549.
2. Rigaku/MSC and Rigaku Corporation . (2001) Crystal Structure Version
3. 10. , Rigaku/MSC, 9009 New Trails Drive , The Woodlands , TX 7738 1,
USA. Rigaku , 3-9-12 Akishima , Tokyo 196-8666, Japan .
3. Altomare, A., Cascarano, G., Giacovazzo, C. , Guagliardi , A., Burla , M. ,Polidori , G. and Camalli , M. (1994) J. Appl. Cryst. , 27 , 435.

195

ATuP-09
CRYSTAL STRUCTURE of Teo.4Seo.s

Yuji Soejima ,8 Akie Hoshiko," Hirotoshi Hayashida ," Yoshinori Ohmasa,bHirohisa Endo, c and Masaru Kawaminami d•oepartment of Physics, Kyushu Univ., Hakozaki 6-10-1 , Fukuoka 812-8581 ,Japan ; bDepartment of Physics , Kyoto Univ. , Sakyo-ku , Kyoto 606-8502 ,Japan ; cFaculty of Engineering , Fukui Univ. of Technology, Gakuen 3-6-1 ,Fukui 910-8505, Japan ; dDepartment of physics , Kagoshima University, 8900065 Kagoshima, Japan ; (oko6scp@mbox.nc.kyushu-u.ac.jp)
At the atmospheric pressure , the most stable form of tellurium andselenium is trigonal. Under pressure , they show several structural transitions andsemiconductor-to-metal transition. It has been well known that Te-Se mixture
also shows interesting electronic properties under high pressure, and recently, it
was found that the crystal structure of TexSe,_x is quenched to the atmosphericcircumstance only in the case of x = 0.4 [1]. In the present work we have carriedout the structure determination of Te 04 Se 0.6 , with short wave length ofsynchrotron radiation .
The X-ray diffraction measurements were made on BL -1 OA at Photon
Factory, KEK. The incident X-ray was tuned at 0.4 A by 311 diffraction with silicon
flat-plate monochromator. One specimen crystal was chosen for intensity
measurement after being examined , in particular, in connection with crystalline
quality by rotational photography. The size of the specimen was 230x130x150
J.!m 3 The linear absorption coefficient J.1 =15. 76 mm-1 thus absorption collection is
not required for the present case . The orientation matrix was determined using
thirteen strong reflections within 8= 15°. The lattice constants were determined
a=8.164, b=27.856, c=13 .852 A and ~=10 8", and the space group Cc was
assigned . Th e intensities of the higher harmonics of the monochromated beam
were very weak, but further reduced by a discriminator of the detector circuit. The
intensity data of the unique region of the reciprocal space were collected in therange sin8//c ! 0.5 by assuming no extinction rule : to collect additional reflections
which have non-integer indices due to longer periodicity of the real lattice;namely ax9bx2c , the lattice parameter were defined as a=8 .1 64, b=250.70 ,c=27 .704 A. 1630 unique diffractions were measured and the integrated intensity
was determined by summing up the intensity measured stepwise in the w--scanand by subtracting background. After correction for incident of synchrotron beam ,a set of structure factor was obtained .
At first , the least-square refinement (SHELX-97 coded by G. M. Sheldric)was carried out assuming monotonic occupancy of 0.4 Te and 0.6 Se atoms at
all atomic site. After reaching a minimal R factor of 0.124, the refinement wascontinued introducing occupation parameter r of Te fraction at 27 unique sites.
Finally we obtained the structure with R=0 .098 using isotropic temperaturefactors. The results indicate that the discrepancy of two facts that Te and Se
atoms tend to align alternatively and that the composition of Te and Se is 0.4:0 .6
leads to the ax9bx2c structure.
References
I
Ohmasa , Y., et al. (1995) J. Phy. Soc. Jpn, 64, 4766.

196

ATuP-10
CRYSTAL STRUCTURES OF A BISAZOMETHINE DYE FORMING
J-AGGREGATES
Shinya Matsumoto, a Kazuko Shirai ," Kimiko Kobayashi,b Tatsuo Wada ,c andMotoo Shiroa
8
Faculty of Education and Human Sciences, Yokohama National University,
Yokohama 240-8501 Japan ; bMolecular Characterization Division ; andcsupramolecular Science Laboratory , RIKEN (The Institute of Physical andChemical Research) , Saitama 351-0198 Japan; dX-ray Research Laboratory,
Rigaku Corporation , Tokyo 196-8666 Japan (smatsu@edhs.ynu .ac.jp)
The title dye 1 synthesized from ;:s, - - - - - - - - - -- -- ---,
diaminomaleonitrile together with 4- ·odiethylaminobenzaldehyde
has - ~
attracted attention as a material for ~ goorganic electroluminescent devices
because of its red fluorescence insolution as well as in the solid state[1 ,2]. This dye was also found to form
J-agg regates in a vacuum deposited
Wave length I nm
film as shown in Fig . 1. X-ray structure
Fig . 1 Absorption spectra of dye 1 (a) inanalysis of 1 was carried out to CHCI and (b) in a deposited film (1500 A).
3elucidate the solid state structure . The
result indicates that the molecules are arranged in a characteristic stacking
fashion that reminds us of molecular arrangement in J-aggregates, as depicted
in Fig . 2. The J-aggregates films were characterized by the almost same phaseas that of the single crystals: Crystal
data (298 K) , a = 9.225 (2), b = 11.290(3), c = 18.182 (6) A, a = 79 .94 (3) , f3 =76.09 (2), y = 89.69 (2) 0 , triclinic, P-1(Z=3). Bond lengths of the terminal
amino moieties were found to beunusual. Then several attempts weremade to separate disordered groups.
The phase in which there are six
molecules in the unit cell was found ataround 93 K: Crystal data (93 K), a =11 .040 (1) , b = 18.097 (1) , c = 18.255(1) A, a = 103.76 (1) , [3= 90 .33 (1) , y =100.32 (1) 0 , triclinic , P-1 (Z=6) .
Fig. 2 Molecular packing of 1 at 298K.
However, the ethyl groups are still
partially disordered . Theoretical investigation of the electronic states of theaggregates on the basis of the present crystal structure will also be discussed .
References
I
Shirai , K. et al. (2000) Dyes Pigm. 47 , 107-115.
2
Yu , J. et al. (2001) Jpn. J. Appl. Phys. 40, 3201-3205 .

197

ATuP-11
STRUCTURAL STUDY OF STRESS-INDUCED LUMINESCENT PARTICLE
SrAb04:Eu

Hiroshi Yamada ," Hajime Kusaba ," Weng-Shen Shi ,b Keiko Nishikubo ,band Chao-Nan Xub
aPRESTO , Japan Science and Technology Corporation (JST) , Honcho,
Kawaguchi , Saitama 332-0012 , Japan; bNational Institute of Ad vanced
Industrial Science and Technology (AIST) , Shuku , Tosu , Saga 841-0052 , Japan(cn-xu@aist.go.jp)
SrAb0 4 doped with Eu 2 • shows an intense green luminescence inducedby mechanical stress so-called the mechanoluminescence. A lot of interest has
been paid in the relation to the crystal structure and the luminescent mechanism
because the atomic configurations around Eu 2• strongly affect the luminescent
properties .
The crystal structure of SrAb0 4 is a family of the stuffed tridymite stru cture
and possesses polymorphism of a - and ,13-phase as shown in figure , where
SrAI 2 0 4 usually transforms to ,13-phase above 650°C. Recently we successfully
synthesized spherical fine particles with pure a-phase , pure ,13-phase, and themix phase by the spray pyrolysis method but only the particle with pure ,13-phaseshows no photoluminescence [1 , 2]. In this work , we have investigated therelation to the stabilization of ,13-phase and the disappearance of theluminescence . The structural characterization of th ese samples have been
carried out by the Rietveld analysis with high-resolved powder X-ray diffraction
data , which were measured by using a synchrotron radiation with wavelength
0.775 A. Furthermore , in order to determine the distribution of doped Eu ion , theelectron density distribution is derived by the maximum entropy method ,demonstrating that the Eu ions partially occupy the Sr ion sites. We will discuss
the additional structural features at the conferen ce.

a: - phasej]-phase

ReferencesI
Shi , W. S., Yamada , H., Nishikubo, K. , Kusaba , H. , and Xu, C. N. Chem .
Mater. (submitted) .
2
Yamada , H., Kusaba , H., Shi , W. S. , Nishikubo , K. and Xu , C. N. (2003) J.
Electrochem. Soc. 150 (4) (to be published) .

198

ATuP-12
POSITIONS OF La AND Ba OF BaLa4Ti401s HOMOLOGOUS COMPOUND
H. Ohsato," Y. Tohdo ," K. Kakimoto,a T. Okawa ,b and H. Okabeb

aDepartment of Materials Science and Engineering , Nagoya Institute ofTechnology, Gokiso-cho, Showa-ku , Nagoya 466-8555 , Japan; bDaiken
Chemical Co ., Ltd. , Japan, 2-7-9 Hanaten-Nishi , Joto-ku, Osaka 536-0011 ,Japan; (ohsato .hitoshi@nitech .ac.jp)

Homologous compound BanLa4Ti 3+n0 12+3n (n=1, 2, and 4) series are one ofcandidate materials for base station of mobile telecommunications. The
compound with n=1 has good microwave dielectric properties: £, =46 , Q ·f =46 ,000 GHz and Tr = -11 [1] . Moreover, temperature coefficient of resonant
frequency was improved to near zero: 1.3 ppm( C with high £, of 44 and Q· f of
47 ,000 GHz[1] .
These homologous compounds were reported by Saltykova et a/. [2] ,which have three kinds of compound on the La 4Ti 30 12 -BaTi0 3 tie line near thetungsten bronze-type like Bas.3xRa+2xTi ,aOs4 ( R = rare earth ) solid solutions in
the Ba0-La 20 3-Ti0 2 ternary system. The homologous compounds
BanLa 4Ti3+n01 2+3n with n=O , 1, 2, and 4, have been composed by means ofadding n-times of BaTi0 3 on La 4Ti 30 12 as following:
La4Ti301 2+ n(BaTi03) ~ BanLa4Tb+n01 2+3n·
These crystal structures are presented by Harri[3], which have a layer
perovskite structure so called hexagonal perovskite . The crystal data are as
follows: trigonal system , P-3c1 , a=5 .571 (1 ), c=22 .488(2) A, Z=2 , Ox=6 .178g/cm 3.
In this study, we determined the positions of Ba and La (denoted as A ion)of homologous compound BaLa4Ti401 s based on the radius of Ba and La ions ,which have never been reported up to now to our knowledge because of theinherent difficulty due to similarity of the atomic scatter factors. These A ions:
2Ba and 8 La in one unit-cell are considered to locate in the A 1:4d, A2 :4d andA3:2a sites with 12 coordination numbers in the close packing layer of oxygen
and A ions. Here, 4d and 2d are multiplicity and Wyckoff letter of positions. The
Ba occupation was finally confirmed by X-ray single crystal structuralrefinements with the least square method with constraint of site occupancies.
A 1 sites locate near the empty cation octahedra , but other A2 and A3 sites
locate near the Ti0 6 octahedra. A 1 sites are displaced upward on the packing
layer toward the empty octahedra side .
ReferencesI
2
3

Okawa , T., Kiuchi , K., Okabe , H. and Ohsato , H. (2001) Jpn. J. Appl.
Phys . 40, 5779-5782 .
Saltykova, V. A., Mel'nikova , 0. V. , Leonova , N. V. and Fedorov, N. F.
(1985) Russ. J. lnorg. Chern ., 30, 105-107.
Harre, N. , Mercurio, D., Trolliard , G. and Frit, B. (1998) Material Research
Bulletin, 33[1 0], 1537-1548.

199

ATuP-13

RELATIONSHIPS BETWEEN RUTILE STRUCTURES
Christopher J. Howard ,"·b Zhaoming Zhang ," and Brendan J. Kennedyc
8Australian Nuclear Science and Technology Organisation , PMB 1Menai , NSW
2234 , Australia ; bSchool of Physics, The University of Sydney, Sydney, NSW
2006, Australia ; cSchool of Chemistry, The University of Sydney, Sydney, NSW
2006 , Au stralia (B .Kennedy@chem.usyd .edu.au)

The structu re of rutile , Ti0 2 , can best be viewed as an edge sharing andcorner sharing arrangement of nearly regular Ti0 6 octahedra. Specifically the
structure consists of chains of edge-sharing octahedra corner linked toneighboring chains.
The tetragonal rutile structure permits some flexibility in the octahedral coordination , through variation of the an ion position parameter along with thelattice parameters a and c. A greater flexibility , and the ability to accommodatea wider range of cations is achieved in distorted variants. In this work , wereview these structures using group theory as implemented in the computer
program ISOTROPY.
Typical distortions are (i) the distortion of the AX 6 octahedron for example
due to Jahn-Tellar effects; (ii) off-centre displacements of the cations (several
different displacement patterns are possible) (iii) tilting relative to one another ofthe corner-linked chains. Each of these distortions can be associated with
irreducible representations of the parent space group P4 2/mnm, andISOTROPY details structures produced by the se different distortions acting
separately or in combination. We have included a consideration of cation
ordering in double rutiles ABX4 and trirutiles A 2 BX 6 . Structures from theliterature have been checked against the structures we have derived.

200

ATuP-14
STRUCTURAL STUDIES ON JACALIN- CARBOHYDRATE COMPLEXES
K. Sekar.a A. A . Jeyaprakash ,b P. G. Rani ,b S. Katiyar,b A. Surolia ,b and M.
VijayanbaBioinformatics Centre and Supercomputer Education and Research Centre ;bMolecular Biophysics Unit, Indian Institute of Science , Bangalore 560 012 ,India (sekar@physics.iisc.ernet.in)

Jacalin is a 66kDa tetrameric lectin from the seeds of jackfruit (Artocarpus
integrifolia). Each subunit consists of two chains , a long a chain and a short ~chain , produced by post-translational proteolysis. The structure of the lectinbound to Me-a -galactose was earlier solved in this laboratory. The structure
revealed a novel lectin fold and the use of post-translational modification as a
strategy for generating specificity for galactose at the primary binding site. At
the disaccharide level, it is specific to tumour-related Gai ~ 1-3GaiNAc , known as
T-antigen. We have now prepared and solved the structures of the complexesof the lectin with Gal , Me-a-GaiNAc, T -antigen , Me-a-T -antigen and GaiNAc ~ 1 3Gai-O-Me. In the complexes with T-antigen and Me-a -T-antigen , the primarysite is occupied by the GaiNac residue . The interactions of the Gal residue
with the protein are confined to water bridges . The methyl group in Me-a-Tantigen has favourable interaction with an aromatic residue, accounting for its
increased affinity to the lectin. In the complex with GaiNAc~1-3Gai-O-Me ,however, the primary site is occupied by the Gal residue presumably on
account of the favourable interaction of the methyl group with the residue . The
structures of the complexes provide a reasonable explanation for the available
thermodynamic data of jacalin-carbohydrate interactions. The details will bepresented.

201

ATuP-15
PRESENT STATUS OF PHARMACEUTICAL INDUSTRY BEAMLINE AT
SPRING-S

Shintaro Misaki ." Kenji Suzuki ,b Yoshio Katsuya ,c Kazumi Nishijima ,d and
Yukiteru Katsubec,e"Shionogi & Co ., Ltd ., Sagisu 5-chome, Fukushima-ku , Osaka , 553-0002 ,Japan; bDainippon Pharmaceutical Co. , Ltd ., Enoki , Suita , Osaka , 564-0053,
Japan; cPharmaceutical Consortium for Protein Structure Analysis , Kouto,
Mikazuki , Sayo , Hyogo, 679-5198 , Japan; dMochida Pharmaceutical Co. , Ltd .,Yotsuya 1-chome, Shinjuku-ku , Tokyo, 160-0004, Japan; eRIKEN Harima
Institute, Kouto , Mikazuki , Sayo , Hyogo, 679-5148 , Japan(shintaro .misaki@shionogi.co.jp)
The Pharmaceutical Consortium for Protein Structure Analysis (PCProt)
was established in April 2001. This consortium is composed of 22
pharmaceutical companies affiliating with the Japan Pharmaceutical
Manufacturers Association (JPMA) . The Pharmaceutical Industry Beamline isconstructed at SPring-8 for exclusive use by members of PCProt. The full-time
operation of this beam line was started last September.
The specification of the Pharmaceutical Industry Beam line is almost sameas that of RIKEN Structural Genomics Beamline I & II . The PharmaceuticalIndustry Beamline is technically supported by RIKEN and the Japan
Synchrotron Radiation Research Institute (JASRI). It is expected that thebeamline will contribute to both pharmaceutical protein crystallography for drug
design and structural genomics carried out in RIKEN .
The Pharmaceutical Industry Beamline has the SPring-8 standardtransport channel and optics for bending magnet. Energy of monochromatic Xrays is tuneable from 7 to 17 keV using a double crystal monochromator and is
focused at sample using a bent cylindrical mirror. The authors will report on
MAD experiments and some others carried out in the beamline.

202

ATuP-16
REFINEMENT OF THE CRYSTALLIZATION CONDITIONS OF CONGER EELGALECTIN, CONGERIN I AND II

Takashi Yamane," Atsuo Suzuki,a Yumiko Miyabe,8 Clara Shionyu-Mitsuyama ,8Yuusuke Niwa,8 Tomohisa Ogawa ,b Koji Muramoto,b and Mitsuo Atakac
8
Graduate School of Engineering , Nagoya University, Nagoya 464-8603, Japan;
bGraduate School of Agricultural Science , Tohoku University, Sendai 981-8555,
Japan; cNationallnstitute of Advanced Industrial Science and Technology (AIST),
Ikeda 563-8577 , Japan (yamane@hix.nagoya-u.ac.jp)
The skin of conger eel (Conger myriaster) secrets mucus containing the
galectin family proteins, congerin I and II. To understand the carbohydrate
recognition mechanism of congerins, the crystal structure of congerin I wasdetermined at 1.5 A resolution[1] . Recently the crystal structure of congerin II withlactose and 2-(N-morphorino)ethansulfonic acid (Mes) was determined at 1.45 A
resolution[2] . In order to obtain further insights into the structure-function relation
between congerins, the refinement of the crystallization conditions has been
carried out as a part of the efforts to conduct microgravity experiments using HighDensity Protein Crystal Growth (HDPCG) cell[3] .
Congerin 1: original conditions; A 5 Jll of protein solution (2.0% (w/v) protein
in 0.01 M Tris-HCI buffer (pH 7.0)) was mixed with 5 Jll reservoir solution (25%(w/v) PEG6000 in 0.1 M Tris-HCI buffer (pH 9 . 0) ~ . Crystals were grown within one
month to max. dimensions of 0.5 x 0.4 x 0.2 mm ; refined conditions; 40 111 dropletof protein solution (1.75-2.0% (w/v) protein in 0.1 M Tris-HCI buffer (pH 8.5) with
17.5-20% (w/v) PEG6000) and 560 111 reservoir solution (35% (w/v) PEG6000 in
0.1 M Tris-HCI buffer (pH 8.5)). Crystals were grown within two weeks to max.
3
dimensions of 0.2 x 0 .2 x 0.2 mm . Congerin II: original conditions; 8Jll droplet ofprotein solution (1 % (w/v) protein in 0.5 M Mes buffer (pH 6.5) with 1 mM lactose
and 0.8 M MgS04) and 1 ml reservoir solution (1.6 M MgS04 in 1.0 M Mes buffer(pH 6.5)) . Crystals were grown in one month to max. dimensions of 0.5 x 0.5 x 0.5
mm 3 ; refined conditions; 40 Jll droplet of protein solution (1.0-1 .75% (w/v) protein in
0.1 M Mes buffer (pH 6.5) with 1.2-1.3 M MgS04) and 560 111 reservoir solution(1 .6-1 .75 M MgS04 in 0.1 M Mes buffer (pH 6.5)) . Crystals were grown within two
weeks to max. dimensions of 0.4 x 0.4 x 0.2 mm 3 .
The synchrotron radiation experiments were performed at SPring-8 (Proposal
No. J03A12B2-0500N). For congerin I, 1.3 A resolution data were collected fromnew crystals. It is interesting that two morphologically different crystals weregrown. One belongs to orthorhombic system , with a=40.7, b=93 .7 and c=113 A.
The other is isomorphous to that of congerin II. On the other hand , both new andoriginal crystals of congerin II are isomorphous, and the new crystals diffracted to
1.0 A resolution . Structure determination of congerin I and II using these data iscurrently under way.
This study is funded in part by "Science Research Program Experiment
Themes for Protein Crystal Growth Experiment in Space using STS-1 07 " by
NASDA and Japan Space Forum.
References
I
Shirai , T . eta/., (1999) Structure 7, 1223-1233.
2
Shirai, T. eta/. (2002) J. Mol. Bioi., 321 , 879-889 .
De Lucas, L. J. eta/ (2002) J. Crystal Growth 237-239,1646-1650.
3

203

ATuP-17

NEUTRON PROTEIN CRYSTALLOGRAPHY OF CUBIC INSULIN
M. Maeda ," T. Chatake ," I. Tanaka ," A. Ostermann ,"·b and N. Niimuraa
aAdvanced Science Research Center, Japan Atomic Energy Research Institute(JAERI} , 2-4 Sirakata Shirane, Tokai-mura , Naka-Gun , lbaraki , 319-1195 ,Japan ; bPhysik-Department E 17 der TUM , James Frank Str., 85747 Garching,
Germany (mmaeda@neutrons.tokai.jaeri.go.jp)

Hydrogen atoms and water molecules surrounding protein play importantroles in many physiological functions . However, it is difficult to determinehydrogen atoms in protein molecules in X-ray protein crystallography. On theother hand , neutron protein crystallography has become a powerful method forlocating position of hydrogen (deuterium) atoms bound waters of proteins [1] . In
order to elucidate hydration structure in cubic insulin crystals , large single
crystals of cubic insulin for neutron protein crystallography have been grown in
0 2 0 by a dialysis method. The size of the grown largest crystal of cubic insulin
is 4.0 x 4.0 x 1.25 mm 3 in volume.
The neutron diffraction experiment has been carried out with single crystal
diffractometer BIX-3 installed of JRR-3M reactor in JAERI. The structure
analysis has been investigated , and important information has been extracted
from the structural result.
This study is supported by a grant from the Organized Research
Combination System (ORCS) .
References
I
Niimura, N. , Minezaki , Y. , Nonaka , T. , Castanga , J-C. , Cipriani , F. , Hoghoj.
P. , Lehmann. , M.S. , & Wilkinson. C. (1997). Nat. Struct. Bioi. 4 , 909-914 .

204

ATuP-18
PREPARATION, CHALACTERIZATION AND CRYSTALLIZATION OF THE
COMPLEX COMPOSED OF GRANULOCYTO COLONY-STIMULATINGFACTOR AND ITS RECEPTOR
Eijiro Honjo,8 Shouhei Mine ,8 Takumi Koshiba ,b Tomoyuki Okamoto,8 Taro
Tamada ,8 Yoshitake Maeda ,8 Yasuko Matsukura ,8 Akane Horie,8 Matsujiro
lshibashi ,c Miharu Sato,8 Mizue Azuma ,8 Masao Tokunaga ,c Katsutoshi Nitta ,band Ryota Kuroki 8
8Protein Engineering Group, Pharmaceutical Research Laboratories, Kirin
Brewery Co. Ltd. , 1-13-5 Fukuura , Kanazawa-ku , Yokohama 236-0004 , Japan;bDivision of Biological Sciences, Graduate School of Science , Hokkaido
University, Kita-ku , Sapporo 060-0810 , Japan ; claboratory of Applied
Microbiology, Faculty of Agriculture , Kagoshima University, 1-21-24 Korimoto ,Kagoshima 890-0065 , Japan (Eijirou_Honjo@beer.kirin .co .jp)
Granulocyte colony-stimulating factor (G-CSF) is a cytokine that regulates
the proliferation and differentiation of neutrophils. These responses are initiatedby interaction with a specific receptor (G-CSFR) . G-CSFR has a composite
structure consisting of an immunoglobulin (lg)-like domain , a cytokine receptor
homologous (CRH) domain and three fibronectin type Ill domains in theextracellular region. G-CSF forms a tetrameric comple x with G-CSFR ,comprising two G-CSF and two receptor molecules. The tetrameric structure of
the complex is unknown , but it is indicated that the lg domain and the CRH
domain of G-CSFR are involved in G-CSF binding .
To attempt to determine the tertiary structure of G-CSF/G-CSFR complex
by X-ray crystallography, we first prepared G-CSFR (lg-CRH) insect cell culture ,in which G-CSFR was expressed as fusion protein with Fe region of mouse lgG.
After digestion of G-CSFR-Fc by thrombin to remove Fe region , the G-CSFR
was prepared by gel filtration . The isothermal titration of G-CSFR with G-CSF
showed that the ligand-receptor affinity was -10 8 M-1. The light scatteringexperiment equipped with gel filtration column showed that the averagemolecular weight of G-CSF/G-CSFR complex was 132000 daltons indicating a
2:2 ligand-receptor complex. The G-CSF/G-CSFR complex thus characterized
was used for crystallization screening . The complex was crystallized to a spacegroup P41212 with unit cell dimensions of a = b = 11 0.1A, c = 331 .8 A at acondition containing 0.1 M Na formate and 1.0 M Na acetate (pH 4 .6) . The
preliminary diffraction experiment indicated that the crystal diffracts only upto 4
A resolution . We are now attempting to obtain the different form of G-CSF/GCSFR complex by removing the N-linked sugar chains located in G-CSFR using
several glycosidases.

205

ATuP-19
CRYSTAL STRUCTURE OF DSBG A DISULFIDE BOND ISOMERASEFROM ESCHERICHIA COLI

Begofia Heras." Melissa A. Edeling ," Jennifer L. Martin ," and Salish Rainab"Institute for Molecular Bioscience. University of Queensland , Brisbane OLD
4072 Australia ; bCentre Medical Universitaire, Departement de Biochimie
Medicale, 1 Rue Michel-Serve!, 1211 Geneve 4, Switzerland(b .heras@imb .uq.edu .au)
The correct formation of disulfide bonds is important for the folding andfunction of many secretory and membrane proteins . In bacteria , disulfide bondformation occurs in the periplasmic space and is catalysed by the Dsb (gi.§.ulfide
Q.ond formation) family of proteins (DsbA, DsbB , DsbC , DsbD , DsbE , andDsbG) [1]. These proteins form two distinct pathways for disulfide formation andrearrangement. The DsbA-DsbB pathway [2] rapidly introduces disulfide bonds
into target proteins , sometimes resulting in the formation of nonnative disulfide
bonds , the DsbC/DsbG-DsbD pathway [3] catalyzes the rearrangement ofincorrect disulfide bonds, allowing proteins to fold correctly.
Crystal structures of three Dsb proteins have been determined , DsbA ,DsbC and DsbE [4-6] . Here we present the crystal structure of the last soluble
member of the Dsb family , DsbG , a disulfide bond isomerase from E. coli that
also functions as a molecular chaperone [7] . DsbG crystal structure
determination required dehydration of crystals prior to data collection . This postgrowth treatment dramatically improved the diffraction resolution of DsbG
crystals from 10 to 2 A (1. 7 A at a synchrotron source) [8] . The crystal structureof DsbG was determined by multiwavelength anomalous diffraction (MAD)methods and refined to an R free of 20.5% (R factor 18.8%) at 1.7 A.
The overall structure of DsbG resembles that of DsbC [5] . Both are Vshaped homodimers in which each monomer incorporates an N-terminal
dimerisation domain and a thioredoxin like catalytic domain separated by alinker a-helix . However, a striking difference between the two is the length of thelinker helix located between the dimerisation and catalytic domain in eachmonomer, wh ich is 2.5 turns longer in DsbG .
References
1. Kadokura, H., Katzen, F. and Beckwith, J. (2003) Annu. Rev. Biochem. 72 ,111-135.
2. Bardwell , J . C., Lee , J . 0 ., Jander, G. , Martin , N., Belin , D. and Beckwith , J .
(1993) Proc. Nat/. Acad. Sci. USA 90 , 1038-1042.
3. Rietsch , A ., Belin , D. Martin , N. and Beckwith, J. (1996) Proc. Nat/. Acad.
Sci. USA 93, 13048-13053.
4 . Martin, J. L., Bardwell , J . C. and Kuriyan , J. (1993) Nature 365, 464-468.
5. McCarthy, A. A., Haebel , P. W. , Torronen, A., Rybin , V., Baker, E. N. andMetcalf, P . (2000) Nature Struct. Bioi. 7, 196-199.
6. Edeling, M.A., Guddat, L. W ., Fabianek , R. A. , Thi.iny-Meyer, L. and Martin ,J . L. (2002) Structure 10, 973-979.
7. Shao, F., Bader, M. W. , Jakob , U. and Bardwell , J. C. (2000) J. Bioi. Chern.
275, 13349-13352.
8. Heras, B., Edeling , M.A. , Byriel , K. A. , Jones, A., Raina , S. and Martin, J. L.
(2003) Structure 11 , 139-145.

206

ATuP-20
PROTEIN MODEL BUILDING USING IMAGE PROCESSING TECHNIQUE
AND OPTIMIZATION ALGORITHMS

Osamu Takahashi,a,b and Shigenobu Kobayashib
aNEDO Fellow, New Energy and Industrial Technology Development
Organization; bDepartment of Computational Intelligence and Systems Science ,Tokyo Institute of Technology, 4259 Nagatsuta Midoriku Yokohama 226-8502
Japan (osamu@fe .dis.titech.ac.jp).
To reveal protein structures becomes important more and more at theperiod of post sequence genomics. X-ray crystallography is one of effective
methods to do that , but it often requires much time and effort at someprocesses that include tracing and building model from an electron density map .
And , an automated iterative model building method was proposed by Perrakis
et al. [1] .
We presented a new basic concept using three-dimensional image
processing te ch nique to obtain rough protein molecular model at the last
ICCBM9 [2] . We extended thinning technique , which is one of normal image
processing techniques for two-dimensional images , to for three-dimensional
images like electron density maps . Thinned electron density map shows its
skeletal structure . Trunk of the skeleton corresponds to main chain of theprotein, and branches correspond to the side chains. And the branching points
on it roughly correspond with C-alpha atoms.
Here, we present the latest work after the image processing . Referring torough positions of branching points, we refine C-alpha atom positions using real
number optimization algorithm with peptide bond template . To form thetemplate, we use Gaussian density distribution as a pseudo electron density
distribution from an atom in real space . After the process , incremental atom
position optimizing search forms tables of amino residue fitting value into eachside chain positions . At the last we can build a molecule model from the value
table and given amino acid sequence. Using the image processing techniqueand the optimization algorithm , we can robustly build protein molecule modelfrom X-ray crystallography data.

Fig 1. Obtained Skeleton in a Dens ity Map

Fig 2. Branching Points in the Skeleton

References
I
Perraki s, A. , Morris, R. J. and Lamzi n, V. S. (1999) Nature Structural Biology 6,

458-463.
2

Takahashi , 0 . and Kobayashi , S. (2002) 9th International Conference on the
Crystallization of Biological Macromolecules O-A5.5(0ral Presentation) .

207

ATuP-21
CRYSTAL STRUCTURE OF TBP-INTERACTING PROTEIN (TK-TIP26)
FROM HYPERTHERMOPHILIC ARCHAEON THERMOCOCCUS
KODAKARAENSIS STRAIN KOD1

T. Yamamoto,• T. Matsuda ,b H. Matsumura,• T. Inoue,• M. Morikawa ,b S.
Kanaya,b and Y. Kai"
"Department of Materials Chemistry, Graduate School of Engineering , Osaka
University, 2-1 Yamada-oka, Suita , Osaka 565-0871 , Japan ; bDepartment ofMaterial and Life Science, Graduate School of Engineering , Osaka University,
2-1 Yamada-oka , Suita , Osaka 565-0871 , Japan (taka@chem.eng .osakau.ac.jp)

The 26 kD TBP-interacting protein from hyperthermophilic archaeon
Thermococcus kodakaraensis KOD1 (Tk-TIP26) is a possible transcriptional
regulatory protein in Thermo cocca les. It was isolated from cell lysates of thisstrain by affinity chromatography with TBP-aga rose . Cloning of the geneencoding this protein showed that Tk-TIP26 is composed of 224 amino acidresidues (molecular weight of 25 ,558) and exists in a dimeric form . The
recombinant Tk-TIP26 and Tk-TBP interact with each other with an equilibrium
dissociation constant, Ko of 1.24-1.46 ~ M . In the presence of Tk-TFB , Tk-TIP26
does not inhibit the formation of TFB/TBP/DNA ternary complex , but interact
with this complex to form TIP26/TFB/TBP/DNA quaternary complex. On theother hand , in the absence of Tk-TFB , Tk-TIP26 prevents Tk-TBP from binding
to TATA-DNA. These results suggest that TIP26 plays an important role intranscriptional regulation in Thermoco cca /es. We have determined 3'd_dimensional structure of T k- Tl P26 by the multiwavelength anomalous
dispersion method at 2.3 A. The monomer structure had the shape of a 'foot' ,containing two domains (N-terminal domain, and C-terminal domain). N-terminal
domain formed B-sandwich structure comprising 4 a -helixes and 6 B-strands ,and its topology resembled Holiday junction resolvase (Hjc) from Pyrococcus
furiosus. The dimer structure of Tk-TIP26 was composed of two monomers
related by the crystallographic 2-fold axis. Dimeric Tk-TIP26 had a few clefts
that might accommodate TBP. The minute discussion on the interaction
between Tk-TIP26 and Tk-TBP is in progress .

208

ATuP-22
TOWARDS A MORE USABLE PROTEIN STRUCTURE DATABASE

W. Bret Church ,a.b Hong Wing Lee,b William M. Shui ,c Stephen C. Graham ,bLawrence K. Lee,b and Raymond K. Wong c•Molecular Biotechnology Program ; bSchool of Molecular and Microbial
Biosciences GOB , University of Sydney, NSW 2006 , Australia ; cSchool ofComputer Science and Engineering , University of New South Wales , NSW
2052 , Australia (b.church@biotech .usyd .edu.au)

In recent years several structural genomics initiatives have been started
with the aim of determining the structures of a large number of proteins , and it
has been suggested that the PDB may hold 35 ,000 entries by the end of 2005.
We are using a database management system to provide a consistentXML database interface for data storage and retrieval of PDB data. This system
employs the Semi-structured Object Database (SODA) [1] . A SODA specifictranslation language is responsible for mapping external , non-XML data sources
to XML so that they can be queried by SODA. The entire contents of PDB files
can be made available. While the ATOM (and HETATM) records are critical to aprotein structure database, significant additional annotation records such as
CAVEAT and SITE records could also be made available to query.
Data derived from the PDB entries , such as accessible surface
calculations , can easily be housed within the database. Based on the given andderived meta-data , whenever the source data layer is changed a trigger system
invokes modules to recalculate and update the meta-data layer. SODA gives
users the choice of triggers at either the source data layer or the meta-datalayer. The latter option makes for a rate limiting initial step but it uses fewer
resources overall. An extended form of the XML query language XQueryproviding support for updates is available in SODA [1] .
The wider context of this work allows for integration of existing repositoriesof data and information created with tools for biological analysis. Populating andquerying these databases can be conducted according to the whims of theresearcher.
We will report our progress on the installation and use of this database.
References
Wong , R.K ., In Proceedings of the ACM Symposium on Document
I
Engineering, Eds . Ethan Munson, Atlanta USA, 9-10 Nov. 2001 , ACM ,USA, pp95-104. http://www.sodatech.com

209

ATuP-23
DATA BASE OF HYDROGEN AND HYDRATION IN PROTEINS

N. Niimura
Advan ced Science Research Center, Japan Atomic Energy Research Institute,
Tokai -mura , lbaraki-ken , 319-1195 , Japan (niimura@kotai3 .tokai.jaeri.go .jp)

Neutron diffraction provides an experimental method of directly locatinghydrogen atoms in proteins , and the development of the neutron imaging plate(NIP} became a breakthrough event in neutron protein crystallography. Several
high resolution neutron diffractometers dedicated to biological macromolecules(BIX-2 , BIX-3 and BIX-4) with the NIP have been constructed at the Japan
Atomic Energy Research Institute and these have enabled high resolution (suchas from 1.5A to 2.0A) structural analyses of several proteins to have beenca rried out. The crystal structures of myoglobin , rubredoxin (wild & mutant), hen
egg-white lysozyme (at pH4 .9 and 7.0) and , human lysozyme, cubic insulin ,DsrD and oligomer DNA have been determined using BIX. From these studies ,all the hydrogen and hydration in these proteins have been summarized as database , and by using them , very interesting topics relevant to hydrogen andhydration in proteins, such as hydrogen bonds , H/D exchange , acidic hydrogen
atom , the role of hydrogen atoms in enzymology , the identification of methylhydrogen atoms and dynamical behaviors of hydration structures includinghydrogen have been extracted from the structural results.

210

ATuP-24
E. COLI DIHYDROOROTASE: STRUCTURE OF THE ENZYMECRYSTALLISED IN THE PRESENCE OF DIHYDROOROTATE. THE
POSSIBILITY OF COOPERATIVITY BETWEEN SUBUNITS?

Mihwa Lee, J. Mitchell Guss, Richard I. Christopherson , and Megan J. Maher
School of Molecular and Microbial Biosciences , University of Sydney, NSW
2006 , Australia (m.lee@mmb .usyd.edu.au)
Dihydroorotase (DHOase) is a zinc metalloenzyme that ca talyses thereversible cyclisation of N-carbamyi-L-aspartate (CA-asp) to dihydroorotate(DHO) in the third step of the de novo pyrimidine biosynthetic pathway. In
prokaryotes DHOase is a homodimeric and monofunctional enzyme of
approximate molecular weight 40 kDa [1]. In higher eukaryotes, DHOase
activity is associated with a trifun ctional enzyme (CAD) which catalyses the first
three steps of the pathway [2] .
The first structure of a DHOase (from E. co/1) has been reported to a
resolution of 1.7 A with one homodimer per asymmetric unit [3] . In agreementwith sequence-based predictions , the overall architecture of the enzyme
resembles that of urease. The protein folds into a TIM-barrel motif, with eightstrands of parallel ~-sheet flanked on the outer surface by a-helices. The active
site was shown to contain a binuclear Zn site with bridging water/hydroxide andcarboxylated lysine ligands. The crystals of DHOase were grown in thepresence of the substrate CA-asp and interestingly the structure showed DHO
bound at the active site of one subunit (molecule A) with CA-asp at the active
site of the other subunit (molecule B) . Importantly, a loop flanking the active
site of molecule B (CA-asp-bound) including residues 109- 112 was notobserved in the published structure.
We have been working on crystallizing hamster DHOase for some timewith limited success [4] . Since the ultimate aim of the work is that of inhibitor
design, we decided to direct our attention to the structure of inhibitor complexesof E. coli DHOase. As a preliminary study, we have collected data from crystalsof the enzyme grown in the presence of DHO (rather than CA-asp as in theoriginal report [3]) and refined the structure to 1.9 A resolution. Again , we findthe product DHO bound in the active site of one subunit and CA-asp in theactive site of the other subunit. Importantly, we have been able to resolve theconformations of the formerly missing residues 109-112. These residues
comprise a loop which takes on very different orientations in the two subunits ,depending on whether DHO orCA-asp is present in the active site . This raises
the possibility of cooperation/communication between the subunits and may
have important implications for both mechanism and inhibitor design.
References
Washabaugh , M . W. and Collins , K. D. (1984) J. Bioi. Chern . 259, 3293.
I
Coleman, P. F. , Suttle, D. P. and Starck, G. R. (1977) J. Bioi. Chern. 252 ,2
6379.
Thaden , J. B., Phillips, G. N. J., Neal, T. M., Raushel , F. M. and Holden H.
3
M. (2001) Biochemistry 40, 6989.
Maher, M. J., Huang, D. T. C., Guss , J. M. , Collyer, C. A. and4
Christopherson , R. I. (2003) Acta Cryst. 059 , 381.

211

ATuP-25
THE CRYSTAL STRUCTURE OF RUBREDOXIN FROM DESULFOVIBRIOGIGAS AT ULTRA-HIGH 0.68 A RESOLUTION
Chun-Ju ng Chen ,"·c Yi-Ting Chen ," Ming-Yih Liu ,b and Jean Le Gallb"X-ray Structural Biology Group, National Synchrotron Radiati on ResearchCenter, Hsinchu 30077 , Taiwan; bDepartment of Biochemistry & Molecu lar
Biology , University of Georgia , Athens , GA 15260, U. S. A. ; cDepartment of
Ph ysics , National Tsing-Hua University, Hsinchu 30077 , Taiwan(cjchen@srrc.gov.tw)More and more examples of phasing macromolecular crystal structures
based on sing le-wavelength anomalous dispersion (SAD) show that this method
is more powerfu l and may have more genera l application in structural biology.
Advanced data-collection facilities and cryogen ic techniques , coupled withpowerful programs for data processing , phasi ng, density modification andautomatic model building , have made the SAD app roach gain wider use
because of its simplici ty and faster data collection and phasing than the multiwavelength (MAD) method or other methods . It can be performed at any
wavelength where anoma lous scatteri ng can be observed in synchrotron . For
those proteins co ntaining metal ions , metal clu sters or heav ier atoms with
sufficie ntl y la rg e Of', such as Fe, Ni , Cu and S, the SAD expe rim ent can be
carried out directly on th e native crysta ls without the need of selena-derivatives .
The SAD method combines the use of SAD data and so lvent flattening toreso lve phase ambigui ty.
We have recently determined the ab initio structure of rub redoxin at ultrahigh resolution , 0.68 A, using the single-waveleng th iron anomalous dispersion
signal at SPring-8 BL 12B2 and NSRRC BL 17B2 Taiwan beamline. Rubredoxinfrom anaerob ic sulfide reducing bacteria Desulfovibrio gigas is a sma ll redox
protein composed of 52 amino acids. It contains with sing le iron atom bound ina tetrahedral coordination by the su lfu r atoms of four cysteinyl residues . The
protein is often pu rified from anae robic bacte ri a where it is thought to be
involved in electron tran sfer or exchange processes. Th e crystal belongs to thespace group P21 with unit ce ll of a = 19.44 A, b = 41.24 A, c = 24 .10 A, and ~ =108.46°. The electron density at 0 .68 A ultra-high resolution ca n help
determining very accu rate atom ic position, especial ly for the coord ination of [Fe4S] cluster, which re vea ls deta iled inform ation of biological fun ction. In thisstudy, we wil l demonstrate the power of Fe-SAD combin ing solvent flattening as
the demanding phasing method for metal or su lfu r- containing proteins , andreport the ultra-high resolution crysta l stru ctures.

212

ATuP-26
TUMOUR PEPTIDE PRESENTATION BY MHC CLASS I
Michelle A. Dunstone ,a Andrew Z. Webb ,b Anthony W. Purcell ,b and Jamie
Rossjohna
aThe Protein Crystallography Unit, Department of Biochemistry and Molecular
Biology, Monash University, Clayton , VIC 3800 , Australia ; bDepartment ofMicrobiology and Immunology, University of Melbourne , VIC 3010 , Australia(michelle.dunstone@med.monash.edu.au)

The role of Class I Major Histocompatibility Complex (MHC) is to capture ,transport and present intracellular peptides to the cell surface. These peptides
are derived by the proteolytic processing of both endogenous host cell proteinsand viral proteins . Discrimination of whether these peptides are foreign isperformed by circulating T lymphocytes , where recognition of a foreign peptide
results in activation of an immune response .
Tumourogenesis can result in expression of proteins that are silent innormal cell types resulting in peptides presented specifically by tumour cells .
These peptides have also been found to be immunogenic opening up theprospect of stimulating the immune system to target tumours using peptide
vaccination . One such candidate is the region 155-167 of NY-ESO , called NYES0-1 (sequence SLLMWITQCFL). Peptides of this region have been found to
be presented by the HLA-A2 MHC in melanoma , breast, lung and bladdercancers.
Research into development of a vaccine to this region so far has identified
a need to improve the resistance to peptidases and to modification of thecysteine and methionine residues without compromising immunogenicity of thepeptide. The aim of this research is to develop a peptide analogue which
addresses these aspects. The structure NY -ES0-1 151-1 65 (SLLMWITQC) , incomplex with the HLA-A2 molecule , has been solved to a resolution of 2.1 A
and is presented here . Effects on the structure by the substitution with peptide
analogues are analysed together with the results of functional assays of these
peptide analogues.

213

ATuP-27
THE CRYSTAL STRUCTURE OF A CORAL POCILLOPORIN

Pascal G. Wilmann ,a,b Travis Beddoe ,a.b Mark Prescott,b Michael Ling ,b Aaron J.
Oakley ,c Sophie Dove ,d Ove Hoegh-Guldberg ,d Rodney J. Devenish ,b andJamie Rossjohn a.b~he Protein Crystallography Unit; bDepartment of Biochemistry and Molecular
Biology, School of Biomedical Sciences , Monash University, Clayton , Victoria
3800 , Australia ; cDepartment of Pharmacology/ Crystallography Centre ,University of Western Australia , Crawley, Western Australia 6009 , Australia;
dCentre for Marine Studies , University of Queensland , St. Lucia , Queensland
4072, Australia (pascal.wilmann@med.monash.edu.au)
Reef building corals contain fluorescent pigments, termed pocilloporins thatfunction by regulating the light environment of coral. These act as photoprotectants
to the excessive sunlight that is related to the photo bleaching phenomenon incorals. Rtms5 is a blue non fluorescen t pocilloporin from the reef-build ing coralMontipora efflorescens which has strong sequence and structural homology toboth green fluorescent protein from Aqueorea victoria (GFP) and a red fluorescentprotein from Discosoma coral (OsRed).
To date no pocilloporin structure has been published , however the
information gained from elucidating the structure of a pocilloporin would provide
detailed insights into the mechanism of coral photoprotection. Rtms5 has beencloned , expressed , purified and crystallized resulting in intensely blue crystals (0.3
x 0.2 x 0.3 mm) with an octahedral appearance [1] . Directed mutagenesis ofresidues surrounding the chromophore have been performed resulting in afluorescent variant termed Rtms5His 146 Ser. Fluorescence analysis has revealed
Rtms5His 146Ser is currently the most red-shifted fluorescent mutant, with anemission maximum of 636nm . Rtms5His 146Ser has also been purified andcrystallized. The structures of both Rtms5 and Rtms5His 146Ser have been
determined through molecular replacement using OsRed as the probe [2] .
Structural analysis of Rtms5 showed the chromophore to be in a unique transcon figuration and it was believed that Rtms5His 146 Ser structure should have a cis
chromphore conformation due to its fluorescent nature. However the transconformation was also observed in Rtms5His 146Ser. Subsequently it ishypothesized that only a small population of Rtms5His 146 Ser molecules adopt thecis chromophore conformation and it is these molecules that are responsible forthe observed fluorescence . Under some conditions the fluorescence intensity of
Rtms5His 146 Ser is markedly increased. It is proposed that the increase influorescence is due to an increased proportion of the molecule in the cis
conformation. This observation may be related to a documented "kindlingphenomenon" [3] of another pocilloporin . Efforts are being made to determine thestructures of Rtms5 under the conditions that increase fluorescence .
ReferencesI
Beddoe , T., Ling , M., Dove, S., Hoegh-Guldberg, 0 ., Devenish , R. , Prescott,M. and Rossjohn , J. (2003) Acta Cryst 059 , 597-599.
2
Prescott, M., Ling, M. , Beddoe, T., Oakley, A. , Dove, S., Hoegh-Guldberg, 0.,
Devenish , R. and Rossjohn , J. (2003) Structure 11 :(3), 275-284 .
3Chudakov, D. , Belousov, V., Zaraisky, A., Novoselov, V., Staroverov, D.,
Zorov, D. , Lukyanov, S. and Lukyanov, K. (2003) Nat Biotechno/21 :(2) , 191194.

214

ATuP-28
STRUCTURAL CHARACTRISATION OF MITOCHONDRIAL IMPORTRECEPTORS

Travis Beddoe .a,b Pascal Wilmann, a.b Simon Bushell ,a.b Judy Scoble,c Diana
Macasev,c Trevor Lithgow,c and Jamie Rossjohn a.b~he Protein Crystallography Unit; bDepartment of Biochemistry and Molecular

Biology School of Biomedical Sciences Monash University Clayton, Victoria ,3168, Australia; cDepartment of Biochemistry and Molecular Biology, Universityof Melbourne, Victoria , 3010, Australia (travis.beddoe@med.monash.edu .au)
Nuclear genes encode the majority of mitochondrial proteins therefore theproteins are synthesised by cytosolic ribosomes and are then imported by the
mitochondria. Preproteins are targeted to the mitochondria by specificsequences , either at their N-terminus, C-terminus or internal sequences. They
are recognised at the surface of the mitochondria by the TOM (translocase of
the outer membrane) complex. In yeast , the receptor subunits of the TOM
complex are Tom70-Tom37 and Tom20-Tom22 , and are involved in initialbinding of all precursors. The Tom70 receptor is especially important in binding
precursors with internal targeting sequences , whereas the Tom20-Tom22
receptor complex binds N- and C-terminal targeting sequences. Once a
precursor has bound to the Tom70 receptor it is passed to the Tom20-Tom22
complex via an interaction between Tom70 and Tom20. After binding to Tom20Tom22 , the precursor proteins are transferred to the translocation pore ,consisting of Tom40 and its associated subunits Tom5 , Tom6 and Tom? . Oncethrough the Tom40 pore , the precursor is sorted into the correct
submitochondrial compartment , often with a requirement for membranepotential , where it will be folded and assembled by the TIM (!ranslocase of thejnner membrane) complex.
To determine how this complex recognises preproteins and imports them ,several of the individual proteins have been expressed and purified from E. coli.
Data will be presented on the progress towards their structural determination.

215

ATuP-29
MHC CLASS I PEPTIDE PRESENTATION -A STRUCTURAL INSIGHT
L. K. Ely," W. A. MacDonald ,b L. Kjer-Nielsen ,b C. S. Clements ," A. G. Brooks,bA. Purcell ,b J. McCiuskey,b and J. Rossjohna"The Protein Crystallography Unit, Department of Biochemistry and Molecular
Biology, Monash University, Clayton , VIC 3800 , Australia; bDepartment ofMicrobiology and Immunology, The University of Melbourne, Parkville, VIC
3052, Australia (lauren .ely@med .monash.edu .au)

The ability for T lymphocytes to selectively recognise peptide-MHC
complexes is critical for cell-mediated immunity . Antigen presenting cells digest
both endogenous and viral antigenic protein to produce peptide fragments ;these peptides are transported to the plasma membrane by MHC molecules .
Passing T lymphocytes recognise specific peptide-MHC complexes throughtheir T cell antigen receptors (TCRs) and selectively kill virally infected cells .
The ability for self-TCRs to recognise foreign MHC complexes is termed
allorecognition . This cross reactivity has significant clini cal implications as it is
the basis forT cell mediated transplant rejection.
To understand the structural basis ofT-cell allorecognition we are studying
the immune response to Epstien Barr Virus (EBV) . EBV is a ubiquitous humanpathogen that infects approximately 90% of the population . In individuals that
express the MHC allele HLA B8 , TCRs are produced to specifically recognise
the EBV peptide in complex with the B8 allele . Previous work in ourlaboratories has resolved the crystal structure of the HLA B8 with the EBV
peptide in complex with this TCR [1]. These TCRs are alloreactive binding an
endogenous peptide in complex with the MHC alleles HLA B4402 and B4405
however not with the closely related HLA B4403 . Historically , transplants
between HLA B4402 and B4403 patients have been associated with organ
rejection and thus considered taboo. These two alleles are extremely
abundant, making up 10-15% of Caucasian HLA B alleles, and thus thismismatch represents a significant transplant barrier.
The endogenous peptide or "allopeptide" that is recognised by this TCR in
the cleft of the HLA B44 alleles is unknown . Little is understood about how thepeptide sequence influences the presentation in the MHC cleft and the effectthis has on TCR recognition . To address this question I have solved a series ofhigh-resolution HLA B44 structures with varying peptide ligands . Here I will
present a structural analysis of this alloreactive system .

ReferencesI
Kjer-Neilsen, L. , Clements, C. S., Purcell , A. W., Brooks , A. G. , Whisstock,
J. C. , Burrows, S. R. , McCluskey, J. and Rossjohn, J. (2003) Immunity 18,
53-64 .

216

ATuP-30
THE CRYSTALLIZATION AND X-RAY DIFFRACTION OF THE HALOACIDDEHALOGENASE DEHIVA FROM THE SOIL BORNE BACTERIUM
BURKHOLDARIA CEPACIA MBA4
Jason W. Schmidberqer, Matthew C. J. Wilce , Aaron J. Oakley, and Colin A.
Thompson"Stru ctural Biology Group , Department of Pharmacology, University of Western
Australia , Nedlands, WA 6009 Uwschm idberger@yahoo.com.au).

DehiVa is a dehalogenase enzyme with a hydrolytic activity found in
Burkholdaria cepacia MBA4. It belongs to a group of deha logenating enzymes
that degrade halogenated aliphatic acids and exhibit a broad range of substratespecificities . Although a sign ificant amount of biochemica l inform ation about
DehiVa is already known , its tert iary structure is not. Fu rthe rm ore, only two
related enzymes from thi s group have had their structures solved . This study
aimed at solving the tertiary structure of DehiVa . Protei n was pu rifi ed to -98%
through a series of mostly chromatographic methods , and then screened
against JB Screens 2 and 3. Bipyramidal crysta ls with largely hexagonal shapewere successfu lly grown in less than 24 hours in JB Screen 3, conditions A6 ,81 and 84 . A succession of screens around these growing conditions (15%
PEG 4000 , 0.2M ammonium su lfate , and 0.1M sodium acetate buffer pH 4.4)
produced larger crystal s, which were found to diffract to 3.4 angstroms . Five
crystal forms have since been identified growing in a variety of cond itions .

217

ATuP-31
TRYPTOPHAN BIOSYNTHESIS IN MYCOBACTERIUM TUBERCULOSIS

J. Shaun Lott, 8 Anthony J. Harrison ,8 Emily Parker,b Rochelle J. Ramsay,8and Edward N. Bake ~8

Laboratory of Structural Biology , School of Biological Sciences , University of
Auckland , Private Bag 92-019 , Auckland , New Zealand ; blnstitute ofFundamental Sciences , Massey University, Private Bag 11-222, Palmerston
North , New Zealand (s .lott@auckland.ac.nz)

Mycobacterium tuberculosis is the most successful pathogen of mankind.
More people are killed by M. tuberculosis infection than by infection with anyother bacterium . Recent estimates of the worldwide problem indicate that morethan 1000 new cases of tuberculosis (TB) occur every hour, resulting in thedeath of more than 7000 people per day. Although TB is readily treated with
antibiotic therapy , the treatment is slow (6-9 months) and incomplete therapy
has given rise to TB strains which are resistant to one or all of the preferredantibiotics [1 ,2]. The rise of multiple drug resistant (MDR) TB strains has
contributed to the increase in the incidence of TB in the major industrialised
nations throughout the 1990s, reversing the steady decline of previous decades[3] and has precipitated the search for new therapies and antibiotics.
Tryptophan biosynthesis makes an attractive target for the design of new
anti-TB drugs , as auxotrophic mutants of M. tuberculosis are essentiallyavirulent [4] and the biosynthetic pathway is not present in humans . The firststep in tryptophan biosynthesis is carried out by the anthranilate synthase (AS)complex , made up of two polypeptides , trpE and trpG. There are two candidates
trpE ORFs in M. tuberculosis (Rv1609 and Rv2386c) but no clear candidate for
trpG. The second step in tryptophan biosynthesis is carried out by anthranilate
phosphoribosyltransferase, trpD (Rv2192c).
We have expressed in E. coli and purified trpD , trpE and trpE2 fromM. tuberculosis as either GST fusion proteins or histidine-tagged proteins. TrpD
has been crystallised and data has been collected from these crystals to a
resolution of 2. 3A . TrpE2 has also been crystallised and these crystals diffract
to a resolution of -3 .5A. We are currently working to improve the quality ofthese crystals and to prepare selenomethionine-substituted protein for MAD
phasing.
References
I
Rattan , A. , Kalia , A. and Ahmad, N. (1998) "Multidrug-resistant
Mycobacterium tuberculosis: Molecular Perspectives ." Emerging Infectious
Diseases 4 , 195-209.
2
World Health Organisation (2000) Drug-resistant strains of TB increasing
worldwide.
3
Stokstad , E. (2000) "Drug-Resistant TB on The Rise ." Science , 287, 2391.
4
Smith, D.A. , Parish, T. , Stoker, N.G. and Bancroft, G.J . (2001)"Characterization of auxotrophic mutants of Mycobacterium tuberculosis
and their potential as vaccine candidates." Infection & Immunity 69, 11421150.

218

ATuP-32
UNDERSTANDING THE FUNCTIONING OF THE COPPER BINDING
DOMAIN OF THE AMYLOID PRECURSOR PROTEIN

G. K. W. Kong ."·b W. J. McKinstry," J. J. Adams ." G. Polekhina ." N. A.
Williamson ,6 D. Cappai ,b K. J. Barn ham , b R. Cappai ,b and M. W. Parker aaBiota Structural Biology Laboratory, St. Vincent's Institute of Medical Research ,Fitzroy, Victoria 3065 , Australia ; bDepartment of Pathology, The University of
Melbourne , Victoria 3010 , Australia (g .kong1 @pgrad .unimelb.edu.au)
Redox active metal ions , like copper (Cu) , are abundant in human brains
and may contribute to the pathogenesis of various neurodegenerative diseases[1] . In Alzheimer's Disease (AD) , the amyloid plaques , the pathological hallmarkof the disease formed by the over-production and aggregation of peptides called
A~ . bind and thus concentrate Cu ions in the vicinity of brain neurones . As
Cu(ll) ions are highly oxidising and can react with oxygen to produce reactive
oxygen species , they can inflict oxidative damage to the neurones [1] . The
clearance of metal ions from A~ and/or plaques thus represents an importantmeans of intervention in AD .
The A~ peptide is derived from the cleavage of the amyloid precursor
protein (APP) , a single transmembrane protein found on the surface of brainneurones , by enzymes called secretases. The APP contains , near the Nterminus , a copper binding domain (CuBD) which binds Cu(ll) with high affinity[2]. The binding of Cu(ll) to APP helps to clear the ion from the extracellularenvironment [3] and influences APP metabolism so as to lower A~ secretion [4].
Cu(ll)-binding also causes changes to the structure of the CuBD and may
subsequently modulate APP-APP interactions [5] . Structural studies of the
CuBD will help to understand the Cu(ll)-binding process and may enable thedevelopment of CuBD agonists that disfavour the production of A~.
Well -diffracting crystal forms of the CuBD have been grown in a few
conditions and attempts to solve the phase problem involved using an existing
NMR model for molecular replacement (MR) [6] . With a large number ofmolecules per asymmetric unit in the initial crystal forms (between 6 to 12), MR
was further complicated by errors in the NMR model. Eventually a crystal form
was found containing only one molecule in the asymmetric unit and a 2 A
resolution data set collected . After trying various MR programs , a solution was
obtained by AMoRe [7] . The current, preliminary crystal structure is free of any
metal ions , and like the NMR model , the fold is based on a helix packed against
a ~ sheet of 3 strands. The focus is now on defining the Cu binding site throughobtaining a Cu-bound structure of the CuBD.
References
I
Bush , A.l. (2000) Curr. Opin. Chem. Bioi. 4, 184-191.
2
Multhaup, G. et at. (1997) Biochem. Pharmacal. 54, 533-539.
3White et al (1999) Brain Res. 84, 439-444 .
4Borchadt, T. eta/. (1999) Biochem. J. 344, 461-467.
5
Beher, D. eta/. (1996) J. Bioi. Chem. 271 , 1613-1620.
6
Barnham , K.J. et at. (2002) , submitted.
7
Navaza , J. (1994) Acta Cryst. A 50, 157-163.

219

ATuP-33
CRYSTALLOGRAPHIC STUDIES OF THE MITOCHONDRIAL FISSIONPROTEIN FIS1

Michael A. Gorman, 8 Diana Stojanovski, b Michael T.Ryan ,b and Jacqueline M.
Gulbis a8

Department of Structural Biology , The Walter and Eliza Hall Institute, 1G Royal
Parade , Parkville , Victoria, 3050 , Australia; bDepartment of Biochemistry, La
Trobe University, Victoria , 3086 , Australia (gorman@wehi.edu .au)

The vital role of mitochondria for ATP production , Ca2+ homeostasis andinitiation of apoptosis has been apparent for some time. Mitochondria are notsingu lar organel les but are dynamic structures that divide and fuse continua lly
throughout the life of the cel l. Since mitochondria are not created de novo, theymust proliferate and segregate into daughter cel ls during ce ll division so thateach one maintains a full complement. Most of the work has been done in themodel system of S. cerevisiae in which two conserved GTPases regulate
mitochondrial shape . Fzo1 p[1] mediate mitochondrial fusion and Dnm1 p[2]regulates mitochondrial fission. Loss of Dnm1p function impairs fission resulting
in the formation of highly connected networks due to the accumulation of
unopposed fusion events . In yeast , two additional proteins Mdv1p and Fis1p are
essential components of the fission machinery[3]. Fi s1 p is an integral
mitochondrial outer membrane protein recruiting Dnm1 p and Mdv1 p to thesurface of the outer membrane . In vivo stud ies indicate the intact C-terminal
structu re of Fis1 p is essential for localisation whereas the N-terminal region ofFis1 p is necessary for mitochondrial fission. In mammalian cells, the dynaminlike homologue to Dnm1 p, Drp1 p, is also required for mitochondrial fission. It is
distributed predominantly in the cytoso l and is transiently associated withmitochondria. The human homologue hFis1 shares 25 % sequence identity and
61 % sequence similarity with the yeast counterpart. The structures of hFis1 andhFis1 /Drp1 p comp lex will help identify the molecular interaction and how
specificity is achieved . To this aim, the cytosolic domain of hFis1 has been
expressed as a GST-fusion protein and the progress towards the determinationof hFis 1p X-ray crystal structure will be discussed.
References
1
Rapaport, D., Brunner, M., Neupert, W. and Westermann (1998) J. Cell.
Bioi. 273 , 20150-20155 .
2
Otsuga , D. eta/ (1998) J. Cell. Bioi. 143, 333-349.
3
Mozdy , A. D., McCaffery, J. M. and Shaw, J. M. (2000) J. Cell. Bioi. 151 ,
376-379 .

220

ATuP-34
THE CRYSTAL STRUCTURE OF T84.66FAB AT 2.2 A RESOLUTION AND
MODELLING THE BINDING OF ANTI-CEA ANTIBODY CONSTRUCTS TO
THE CEA ANTIGEN
Jennifer A. Carmichael ."·b Barbara Power."·b Albert van Donkelaar." Mark
Sherman, c Paul Yazaki ,c Anna M. Wu ,d and Peter J. Hudsona.b
CSIRO Health Science and Nutrition 343 Royal Parade, Parkville 3052 ,Victoria , Australia ; bCRC for Diagnostic Technologies , 343 Royal Parade ,Parkville 3052 , Victoria , Australia ; cDepartment of Molecular Biology , Beckman
Research Institute of the City of Hope, Duarte , CA 91010 , USA; dUCLA school of
medicine , Los Angeles , CA 90095, USA (Jenny.Carmichael@csiro .au)a

The crystal structure of the Fab arm of the T84.66 anti-carcinoembryoni cantibody (T84.66Fab) was solved to 2.2A and compared to the previously
solved structure of an engineered T84.66 anti-CEA scFv diabody (T84.66Di)
previously solved in this laboratory [1]. The CDR loop structure seen in the
T84 .66Fab supports the novel loop structures observed in the T84.66Di L 1 andH3 loops. The same loop structure has now been seen in all three Fv structures(T84.66Fab , T84 .66DiAB , T84 .66DiBA) determined and indicates that this isunlikely to be the result of crystal packing, a possibility raised when the
T84 .66Di structure was first solved. The T84 .66Fab T84 .66Di comparison also
revealed flexibility in one of the Fv C domain interface loops that could be afactor in the design of future scFv constructs for immunodiagnostics ortherapeutics.
These structures (T84.66Fab , T84 .66DiAB , T84 .66DiBA) and anotherengineered anti-CEA scFv , MFE-23 [2]. PDB ace., 1QOK , were then used indocking studies with a model of the CEA antigen based on the crystal structureof CEACAM1 [3] PDB ace. , 1L6Z. This resulted in models of the potential
binding sites of these antibody variants to the CEA antigen. A model of thedocked T84.66 structure(s) is presented. The docking of the MFE-23 is alsopresented and discussed in reference to a previously constructed MFE-23-CEA
model [4].
References
I
Carmichael , J. A. , Power, B. E. , Garrett, T. P. , Yazaki , P. J., Shively, J. E. ,Raubischek, A. A. , Wu , A.M. and Hudson , P. J. (2003) J Mol Bioi. 326 ,
341-351.
2
Boehm , M. K. , Carper, A. L. , Wan , T. , Sohi , M. K. , Sutton , B. J. , Thornton ,J. D., Keep , P. A., Chester, K. A., Begent, R. H. and Perkins , S. J. (2000)
Biochem. J. 346, 519-528.
3
Tan , K. , Zelus, B. D. , Meijers , R., Liu , J. H., Bergelson , J. M. , Duke , N.,
Zhang , R. , Joachimiak, A., Holmes, K. V. and Wang , J. H. (2002) EMBO J.
21 ' 2076-2086.
4
Boehm , M. K. and Perkins , S. J. (2000) FEBS Lett. 475 , 11-16.

221

ATuP-35
STRUCTURAL STUDIES OF CP PROTEIN AND ITS FRAGMENTS WITH
ANDROGEN RECEPTOR-mRNA
Mah jooba Sidiqi ,8 Julian Vivian ," Jackie Wilce ,b and Matthew Wilce••oepartment of Pharmacology, QEII Medical Centre, Perth, W.A 6009,
Australia ; bDepartment of Biochemistry, 35 Stirling Hwy, Ned lands, Perth, W.A
6009, Australia (treasures40@yahoo.com)

For some proteins regulation of gene express ion can occur posttranscriptionally, at the level of mRNA stability and translation al efficiency . Thishas been shown to differ from one mRNA to another and can be regulated byprotein-RNA interactions. mRNA stability can be determ ined by elements often
located at the 3' untranslated region (UTR) of the mRNA. A Va ri ety of proteins
have been identified which bind such elements in leading to the stabi lization of
the mRNA. CP protein specifica lly binds poly (C) rich regions at the 3' UTR of
the and rogen receptor mRNA and is thought to lead to its stabi lsation andincreased androgen receptor express ion which plays a critica l role in the
proliferation of prostate cancer cells. Its characterization may provide importantin sig ht into the regu lati on of androgen receptor expression and potentially assist
in the development of drugs aimed to reduce androgen expression in prostatecancer.
CP and CP fragments (containing KH domains representing RNA binding
motifs in the sequence) were successfu lly cloned in bacterial overexpress ion
systems. Milligram quantities of pure protein was successfu lly prepared andpurified for some of the fragments. Prelim inary stru ctu ral studies showed thatCP KH domain three is suitable for NMR studi es. Small crysta ls of this fragment
were also obta ined and we present the structure was determined at a resolutionof 1.9A. In th e future crysta llization experiments will be co nducted in thepresence of androgen receptor mRNA which wi ll hopefully shed some light on
the stabi lisation of androgen re ceptor mRNA and thus the mechanism of
proliferation in prostate cancer cells.

222

ATuP-36
THE SIGNIFICANCE OF INTERACTION BETWEEN 06 HYDROXYLGROUPS OF GLUCOSE RESIDUES OF MAL TOORIGOSACCHARIDE AND
p-AMYLASE FROM BACILLUS CEREUS VER. MYCOIDES

Hideo Miyake ,"·b Genji Kurisu ," Masami Kusunoki ," Sigenori Nishimura ,b andYasunori Nittab"Institute for Protein Research , Osaka University, Suita , Osaka 565-0871 ,Japan; bGraduate School of Agriculture and Biological sciences Osaka
Prefecture University, Sakai , Osaka 599-8531 , Japan (miyake@protein.osakau.ac.jp)(:\-Amylase (EC. 3.2.1.2) hydrolyzes the a -1 ,4-glucosidic linkage of a -1 ,4o-glucans such as starch , thereby liberating (:\ -maltose from the non-reducing
end of substrate. In the previous study, the X-ray crystal structure of a catalytic
site mutant, E172A (Giu172_Aia) , in complex with substrate maltopentaose
was determined , and maltopentaose was observed at subsites -2 to +3 [1) .
Hydrogen bonds between 06 hydroxyl groups of glucose residues located at
subsites -2 to +1 and the side chains of Asp49 , Arg397 , Glu367 and Arg174
were formed .
Three mutants [D49A (Asp49_Aia) , R397L (Arg397 _Leu) , E367 A(Giu367 _Ala) , R174L (Arg174_Leu)) which can not form a hydrogen bondwith an 06 hydroxyl group of one of the glucose residues were created , andtheir crystal structures complexed with maltoorigosaccharide (maltose andmaltotriose) were determined at 1.8 to 2.5 A resolution , respectively by X-ray
crystallography. In the case of the crystal structure of the wild-type enzyme
complexed with maltose , two maltose molecules bound at subsites -2 to +2 intandem [1) . In the case of the crystal structure of all mutants complexed withmaltose , however, maltoorigosaccharide was not observed at the place ofmutation . Also , in the case of D49A complexed with maltotriose ,maltoorigosaccharide was not observed at subsites -2 and -1 even thoughmaltotriose is substrate for this enzyme .
On the other hands , the crystal structure of the native enzyme complexedwith a substrate analog [(1 -4)-0 - a-o-glucopyranosyl-(1-4)-0-a-oglucopyranosyl-o-xylopyranose (GGX)) was also determined . It ,which bound to
subsites +1 to +3, however, could not bind to subsites - 2 to +1 . Therefore , weconclude that this enzyme strictly recognize the 06 hydroxyl groups of glucose
residues and the interactions of 06 hydroxyl group of glucose residues locatedat subsites - 2 to +1 are significant.
Reference1
Hideo Miyake, Genji Kurisu , Masami Kusunoki , Sigenori Nishimura ,Shinichi Kitamura and Yasunori Nitta (2003) Biochemistry. in press .

223

ATuP-37

TOWARDS A CATALYTIC MECHANISM OF AMINOPEPTIDASE P
S C Graham.a M H Lee ,a M J Maher,8 W H Simmons ,b H C Freeman 8 and J M
Guss 88School of Molecular and Microbial Biosciences, University of Sydney, Australia;
bDepartment of Molecular and Cellular Biochemistry , Loyola University Chicago,USA(stepheng@usyd.edu .au)

Aminopeptidase P (AMPP) is a proline-specific peptidase that cleaves the
N-terminal amino acid residue from a polypeptide cha in where the second
residue is proline. AMPP is a ubiquitous enzyme that plays an important role ina wide va riety of bio logica l processes . Examp les include the recycling ofcellular proline and , in mammals , the regulation of peptide hormones. Human
membrane-bound AMPP is the target of a potential drug , apstatin , which has
been shown to re gu late blood pressure when used in conjunction with
angiotensin-converting enzyme inhibitors. Our previous work on E. coli AMPP
has shown that it is a member of the family of pita-bread fold enzymes with adinuclear metal centre in its acti ve site. Other members of this family include
methionine aminopeptidase and prolidase . Structures have now been refined in
the presence of inhibitors and in severa l crysta l forms at different pH va lues.
While these previous studies provided a putative mechanism of action for
AMPP , they left open a number of questions including the basis of specificity for
the N-terminus of the peptide and for proline as the second residue. We haveundertaken further structural studies , including determination of the structures ofmutant and inhibitor-bound forms of E. coli AMPP , in order to elucidate its
mechanism of cata lysis . We have shown that , while AMPP and methionine
aminopeptidase have similar structu re s, the chemistry of the secondary amidebond cleaved by AMPP and the nature of the am ino acid residues su rrounding
the active site of AMPP require differences in their mechanisms of catalysis.
We have also made a model of the human membrane-bound form of AMPP.
Thi s model has permitted us to draw some conclusions about differences inbinding affinity of subs trates and inhibitors between the E. coli and humanmembrane-bound forms of the enzyme.

224

ATuP-38
CRYSTALSTRUCTUREOFTHERMOSTABLEASPARTASEANDSTRUCTURE-BASED EXPLORATION OF FUNCTIONAL SITES IN THE
ASPARTASE FAMILY
Yasuo Hata ,8 Tomomi Fujii ," Hisanobu Sakai ,a and Yasushi Kawatab
8

lnstitute for Chemical Research, Kyoto University, Uji , Kyoto 611-0011,
Japan; bDepartment of Biotechnology , Faculty of Engineering, Tottori
University, Tottori 680-0945 , Japan (hata@scl.kyoto-u.ac.jp)

Aspartase (L-aspartate ammonia-lyase , EC 4.3.1.1) plays an importantrole in bacterial nitrogen metabolism by catalyzing the reversible conversion of
L-aspartate to fumarate and ammonium ion. The crystal structure of thethermostable aspartase from Bacillus sp. YM55-1 has been solved and refinedfor 2.5 A resolution data with an R-factor of 22 .1% [1]. The present enzyme isa homotetramer with subunits (M,= 51 ,627 , 468 amino acid residues)
composed of three domains : the N-terminal large domain , the central helix
domain , and the C-terminal small domain. It exhibits no allosteric effects , incontrast to the E. coli aspartase which is activated by divalent metal cation(Mg 2+) and L-aspartate , but is four-times more active than the E. coli enzyme.
The overall folding of the present enzyme subunit is similar to those of the E.
coli aspartase [2] and the E. coli fumarase C [3], both of which belong to thesame superfamily with the present enzyme . A local structural comparison ofthese three enzymes revealed seven structurally different regions . Five of theregions were located around putative functional sites, suggesting the
involvement of these regions into the functions characteristic of the enzymes .
Of these regions , the region of Gln96-Giy1 00 is proposed as a part of therecognition site of the a-amino group in L-aspartate for aspartase and thehydroxyl group in L-malate for fumarase . The region of Gln315-Giy323 is a
flexible but well sequence(-G 317-S-S-I-M-P 322-)-conserved loop that issuggested to be involved in the catalytic reaction . The region of
Lys123-Lys128 corresponds to a part of the putative activator-binding site in
the E. coli fumarase C. The region in the Bacillus aspartase , however, adopts
a main-chain conformation which prevents the activator binding . The regionsof Gly228-Giu241 and Vai265-Asp272 , which form a part of the active-sitewall , are suggested to be involved in the allosteric activation of the E. coli
aspartase by the binding of the metal ion and the activator L-aspartate .
Moreover, an increase in the numbers of intersubunit hydrogen-bonds andsalt-bridges is observed in the Bacillus aspartase relative to those of the E.
coli enzyme , implying a contribution to the thermostability of the present
aspartase .

References
Fujii, T., Sakai , H. , Kawata , Y. and Hata, Y. (2003) J. Mol. Bioi. (acceptedI
on March 3).
Shi , W ., Dunbar, J., Jayasekera, M. M. K. , Viola, R. E. and Farber, G. K.
2(1997) Biochemistry, 36, 9136-9144.
Weaver , T. and Banaszak , L. (1996) Biochemistry, 35, 13955-13965.
3

225

ATuP-39
CRYSTAL STRUCTURE OF THE CU-AMINE OXIDASE FROMARTHROBACTER GLOBIFORMIS IN COMPLEX WITH THE SUICIDEINHIBITOR 4-(2-NAPHTHYLOXY)-2-BUTYN-1-AMIN EDavid B. Langley,a Eric M. Shepard ,b Anthony P. Duff,a Hans Freeman ,a David
M. Dooley,b and J. Mitchell Gussa
aDepartment of Biochemistry, The Univeristy of Sydney, Australia; bDepartmentof Chemistry and Biochemistry , Montana State University, Bozeman , MT, USA(d.lang ley@mmb.usyd .edu.au)
Cu-containing amine oxidases (CuAOs) are a ubiquitous class of enzyme
catalysing the oxidative deamination of primary amines to their respective
aldehydes with the release of H20 2 and NH 3 . One class of CuAO contains thecofactor 2,4 ,5-trihydroxyphenyl alanine quinone (TPQ), which is a posttranslationally modified tyrosine res idue . The cata lyti c cycle can beconceptua lly split into two halves ; redu ctive and oxidative (A ). In the reductive
half, the primary amine nucleophilically attacks the TPQ to yield a Schiff-baseadduct which is subsequently hydrolysed to leave an N-substituted reduced
TPQ . The oxidative half involves oxidation of the reduced TPQ by molecularoxygen with the liberation of H20 2 and NH 3 .

8 "o'~'"·"'""""'J-oqo
TPO •dduc l

N

H

H

A

B

OH

0

c

The inhibitor 4-(2-naphthyloxy)-2-butyn-1-amine (NOBA) has been
specifically designed to inhibit CuAOs (B). While the primary amine is designed
to target the molecule to the active site and allow formation of the Schiff-base,provision of a triple bond is intended to facilitate attack by an adjacent aminoacid nucleophile to yield an adduct stuck in the active site. NOBA is
stoichiometrical ly potent against the enzyme from Arthrobacter globiformis(AGAO) , whi le less toxic to CuAOs from other species. We have so lved andrefined the structure of AGAO co-crystallised with NOBA. Interesting ly, theelectron density does revea l an adduct attached to the TPQ , but its shapeexcludes the presence of the Schiff-base adduct expected. A model has been
postulated to interpret the density (C). We believe that a Schiff-base product isfirst formed then hydrolysed , as per the usual catalytic cycle. However, thehydrophobic naphthyloxy ring of the product aldehyde prevents its diffusion fromthe active site . The alkyne moiety of the same product is then attacked by the
N-substituted reduced TPQ to yield the product shown in C, which is consistent
with the density observed. Current investigation is aimed at capturing thepostulated initial Schiff-base intermediate , and refining structures of other
CuAOs in complex with this inhibitor.

226

ATuP-40
STRUCTURAL GENOMICS OF NOVEL MACROPHAGE PROTEINSASSOCIATED WITH INFLAMMATORY DISEASE AND CANCER

Pawel Listwan ,"·c Nathan Cowieson ," Anna Aagaard ,"·c Robert Serek," Carmel
Walsh ,"· Timothy Ravasi ,"·c Christine Wells,"·c Thomas Huber,b David Hume ,"·cJenny Martin ,"·c and Bostjan Kobea,ca Department of Biochemistry and Molecular Biology, and Institute for Molecular

Bioscience , University of Queensland, St. Lucia OLD 4072, Australia ; b
Department of Mathematics, University of Queensland, St. Lucia OLD 4072;°CRC for Chronic Inflammatory Diseases (listwan@uq .edu .au)

Most of the potential pathogens that attempt to invade a mammalian cell
fail at the very first stage due to the remarkable effectiveness of innate
immunity. The presence of the potential pathogens is detected via receptors
that recognise generic non-mammalian structures including cell wallcomponents including lipopolisaccharides , peptidoglycans , lipotechoic acids
and microbial DNA [1] . The first line of defense is the macrophage , which
comprises 15-20% of the cells in the most organs, and is particularly abundantat the routes of pathogen entry such as lung , skin , gut and genitourinary tract[2] . When the potential pathogen is recognised , the macrophage engulfs andattempts to destroy the foreign organism . The knowledge of regulation ofmacrophage function will form the basis of two classes of therapeutics.
Amplification of the toxic function of macrophages to destroy foreign organisms
or tumor cells more effectively is one option , the other being the selective
suppression of some components of the macrophage activation response .
These then can be used to treat conditions like septicaemia and toxic shock ,arthritis , atherosclerosis and other chronic inflammatory diseases the other one.
To define the molecular functions of proteins with roles in macrophages ,we set out to characterise them structurally using X-ray crystallography. We
identify proteins with roles in macrophages through expression profiling using
microarray technology. We select and prioritise the proteins for structural
analysis according to a number of criteria such as anticipated insight intofunction and feasibility for structure determination . We have developed
protocols for cloning , expression and crystallography that can be adapted forhigh-throughput approach . To the best our knowledge , this project is the firststructural genomics effort in Australia , and the microarray-to-structure pipeline
is unique among the structural genomics initiatives worldwide. Our initial list of
40 proteins resulted in 7 soluble proteins , 2 targets are currently in
crystallisation trails and one is ready for MAD data measurement. Currently weare optimising this system and here we present our strategy for the selection ,prioritisation , cloning , expression and crystallisation of a number of protein
targets.
References
Hoffman , J.A. , Kafatos , F.C. , Janeway, C.A., And Ezekowitz , R.A. (1999)1
Phylogenetic perspectives in innate immunity, Science 284, 1313-1318.
Gordon , S. , and Hume, D. A. (1986) . Localization and function of tissue
2
macro-phages , Ciba FoundSymp 118, 54-67.

227

ATuP-41
A STRUCTURAL GENOMICS APPROACH TO TUBERCULOSIS
Edward N. Baker," Vickery L. Arcus, 8 Kristina Backbro ,8 Graeme L. Card ,8 Jodie
M. Johnston ,8 Moyra Komen ,8 Nayden Koon ,8 Simon Li ,8 Andrew A. McCarthy,8Rochelle J. Ramsay, 8 Miriam L. Sharpe ,8 and J. Shaun Lotta
8

School of Biological Sciences , University of Auckland , Auckland , New Zealand(ted. baker@auckland .a c. nz)

The availability of ever-increasing numbers of complete genome
sequences is revolutionising the biological sciences. A challenge now in this"genomic revolution " is to add value to the sequence data by focusing on the
structure and function of gene products . Current initiatives in structural
genomics have a number of objectives , both structural and functional , including
the discovery of new folds , determination of representative structures for all
protein families , discovery of function from structure , and the characterisation ofpotential drug targets .
We are participants in a worldwide structural genomics consortium
focused on Mycobacterium tuberculosis , the cause of TB , and one of theworld 's most devastating pathogens . Around 3 billion people die annually fromthe disease. Athough drugs exist , resistance is rising and treatment iscomplicated by the unusual nature of the organism , with its dense , waxy cellwall , and its ability to persist in a dormant state in the lung for long periods .
The TB Structural Genomics Consortium [1] has central facilities for the
benefit of all participants , but individual labs pursue their own objectives , withcoordination to try to avoid overlap . Our focus is on two types of target, (a)enzymes from key biosynthetic pathways which are potential drug design
targets , and (b) proteins of uncertain or unknown function that are implicated in
key aspects of TB biology. In the first category we have chosen enzymes
involved in the biosynthesis of essential amino acids and of menaquinone andthiamin . In the second category we focus on proteins of unknown function thatare implicated by microarray experiments either in antibiotic resistance or in the
hypoxic response (and possibly persistence).
The approaches taken in our laboratory to cloning , expression ,purification, crystallization and structure determination will be reviewed . The
major bottlenecks to date have been in obtaining soluble expression and in
crystallization , and we are reviewing our approaches in both these areas . So far
from about 100 genes cloned we have 9 protein structures , with more to come .
The solved structures include several proteins of unknown function , two others
that appear to be good drug targets , and one protein whose structure suggeststhat it is mis-annotated in this and other genomes.
References
1
TB Structural Genomics Consortium : See http://www.doe-mbi.ucla .edu/TB .

228

ATuP-42
HIGH THROUGHPUT APPROACHES FOR CRYSTALLISATION OF
BIOLOGICAL MACROMOLECULES
Christine L. Gee ," Richard D. Kidd ," Anna Aagaard ." Fiona M. McMillan ,aNiranjali U. Gamage,8 Paul R. Young,b David. A. Humeb and Jennifer L. Martina
alnstitute for Molecular Bioscience ; bSchool of Molecular and Microbial
Sciences , The University of Queensland , St Lucia , 4072 , Australia(c.gee@imb.uq.edu.au).

Structural genomics programs generate hundreds of proteins for structural
analysis. To keep pace with this , rapid and economical methods for highthroughput screening of crystallisation conditions are required. Here we present
a protocol for semi-automated 96 well format screening as a high throughput
approach for crystallisation.
We use a Packard multiPROBE II liquid handling robot to dispense
solutions into a master 96 deep-well tray. Once solutions are dispensed into 96
well format, multi-channel pipettes are used to dispense aliquots into microtitre
plates and to set up hanging drops on plastic sealing film. The plastic film isthen sealed over the rims of the individual wells . This method removes theneed for grease sealing and individual manipulation of cover slips used in thestandard 24 well crystallisation tray, thus saving time . The smaller footprint
trays are space saving , occupying almost half the space of the standard 24 welltrays. They are inexpensive and also save reagents , as they use one-tenth thereservoir volume of the old 24 well format , thus lowering costs.
The robot is also used to mix solutions for grid optimisation screens.
These are generally dispensed in 24 well format into a tissue culture plate andthe crystallisation hanging drops are again dispensed with a multi-channel
pipette onto sealing film.
Several proteins have been crystallised in our laboratory using thesetechniques and these will be described in more detail.

229

ATuP-43
THE STRUCTURE AND FUNCTION OF STREPTOLYSIN 0
Julian J. Adams ," Susanne C. Feil ,8 Rodney K. Tweten ,b and Michael W.
Parker88

Biota Structural Biology Laboratory, St Vincent's Institute of Medical Research
Fitzroy, Victoria 3065, Australia ; bDepartment of Microbiology and Immunology,
The University of Oklahoma Health Sciences center, Oklahoma City, Oklahoma
73190, USA Ujadams@medstv.unimelb.edu.au)

Streptolysin 0 (SLO) is a cholesterol dependant cytotoxin (CDC) secretedby Streptococcus pyrogenes . SLO is one of the key virulence factors in
streptococcus infections of soft tissue e.g . strep throat, impetigo and necrotisingfascitis. SLO is also a causative agent in toxigenic or immunopathologicaldisease e.g . Scarlet fever, toxic shock syndrome and rheumatic fever . SLO isthe archetype for the CDC super family of pore forming toxins [1], it however
differs from the other members of the family as it possesses a 70-75 amino acidN-terminal extension , the function of this extension is unknown. There is someevidence to suggest this difference may have a significant influence on
membrane specificity and activity. We hope to be able to shed some light on thefunction and biological relevance of the N-terminal domain. Our group solved
the first structure of the CDC super family: perfringolysin 0 [2] (PFO). This
structure revealed aspects of CDC toxin activity but much more needs to belearned. A structure of another CDC super family member will be invaluable .
The results from this project will be used for in silica compound screening andpossible development of treatments for streptococcus infections.
As SLO has approximately 58 % sequence identity with PFO it isanticipated that the structure will be amenable to solution by molecularreplacement (MR). If MR from the data recently collected in house and at the
APS fails to yield a structure , heavy atom soaks and multiple anomalous
dispersion techniques will be employed. To this end Pt and Hg derivative
crystals have being prepared and data sets collected.
References
I
Palmer, M. (2001) The family of thiol-activated , cholesterol-binding
cytolysins . Toxicon . 39 , 1681-1689.
2
Rossjohn, et al. (1997) Structure of a cholesterol-binding thiol-activatedcytolysin and a model of its membrane form. Cell. 89 , 685-692.

230

ATuP-44
HIGH RESOLUTION ANALYSIS OF THE NEW INHIBITOR PGD-042 BOUND
HUMAN HEMETOPOIETIC PROSTAGLANDIN D SYNTASE
N. Katsuyama ." T. Inoue," Y. Okano ," H. Shishitani ," N. Okazaki ," H.
Matsumura ," Y. Urade ,b and Y. Kai•
•oepartment of Materials Chemistry, Graduate School of Engineering , Osaka
University, 2-1 Yamada-oka , Suita , Osaka 565-0871, Japan; bDepartment of
Molecular Behavioral Biology Osaka Bioscience Institute, Osaka 565 , Japan(naok@chem.eng .osaka-u .ac.jp)

Prostaglandin (PG) 02 is an allergic and inflammatory mediator producedby human mast cells and Th2 cells in a variety of human tissues. PGD2 isformed from arachidonic acid by successive enzyme reactions: oxygenation ofarachidonic acid to PGH2 via PGG2 by PG endoperoxide synthase ,cyclooxygenase (COX) , followed with isomerization of PGH2 to PGD2 by PGD
synthase (PGDS) . Hematopoietic PGDS (H-PGDS) is responsible for thebiosynthesis of PGD2 by mast cells and Th2 cells. Overproduction of PGD2
exacerbates asthmatic reactions , such as enhancement of eosinophilia andaccumulation of Th2 cytokines , as shown by an ovalbumin-challenged athma
model in human L-PGDS- or H-PGDS-transgenic mice . On the other hand ,these asthmatic reactions are weakened in gene-disrupted mice for the D typeof prostanoid (DP) receptor specific for PGD2 . The DP receptor is constitutively
expressed in human basophils and eosinophils , and is induced in pulmonary
and airway epithelial cells by the allergic inflammation.
Recently, PGD2 was also identified as a ligand for an orphan receptor
CRTH2 , which is preferentially expressed in Th2 cells , eosinophils , andbasophils and mediates chemotaxis of these cells for PGD2 . Therefore, PGD2
produced by H-PGDS in human mast cells and Th2 cells is considered toaccelerate allergic and inflammatory reactions by stimulating both DP and
CRTH2 receptors in autocrine and paracrine manners . Thus , the human HPGDS is a promising target for the anti-allergic drug design.
Cibacron Blue is one of the potent inhibitor for human H-PGDS with IC50
value of 44 nM . However, one of the Cibacron blue derivatives (PGD-042) , with
only the quinone ring and the sulfonamide , shows 2-order reduction of theinhibition activity. To discuss the correlation between the complex structure andthe inhibition activity , we tried to co-crystallization with two compounds. The
crystallization with Cibacron blue and PGD-042 were performed by cocrystallization method in the presence of 1OOmM Cibacron blue or 1O~M PGD042 , respectively.
We obtained the complex crstal with inhibitor -042 with co-crystallization
method by using hanging-drop vapour diffusion method. We collected the X-ray
diffraction data under cryo-temperature using 1.0 Awavelength X-ray radiation
at station BL44XU of the SPring-S synchrotron radiation source. The crystals
diffracted beyond 2.0 A resolution at the synchrotron radiation source.

231

ATuP-45
THE ROLE OF PROLINE RESIDUES IN THE HINGE REGION OF CDC2KINASE SUBUNIT PROTEINS
Joyanne A. Kelly,"·b,c,d Elizabeth A. Williams,a,c,d and Matthew C. J. Wilcea,b8School of Pharmacology and Medicine , University of Western Australia ,Crawley 6009, W.A. , Australia ; bCrystallography Centre, School of Biomedical
and Chemical Sciences, University of Western Australia , Crawley 6009 , W.A. ,Australia ; ccentre for Applied Cancer Studies , University of Western Australia ,Crawley 6009 , W.A. , Australia ; dlions Cancer Institute Inc., Oasis LotteriesHouse, 37 Hampden Rd, Nedlands 6009 , W.A. , Australia
Uoyanne@cyllene.uwa.edu.au).C.dc2 J:Sinase §.ubunit (Cks) proteins are essential for mitosis , however
their precise function has eluded researchers for two decades . Two
conformations of Cks have been detected crystallographically , a compact
monomer with the C-terminal fourth ~-strand inserted into the core of themolecule between strands 2 and 3, and a strand-exchanged dimer in which thefourth ~-strand is inserted into the core of the dimer partner in an equivalent
position. There is an absolutely conserved "hinge" region , consisting of the motif
PEP , N-terminal to the fourth ~-strand . In the monomer this motif constitutes a~-turn while in the dimeric structure it is extended , allowing strand exchange .
The mutant protein , p13suc 1P 90AP 92 A, in which alanine residues replace both
pralines of the turn , provides an opportunity to examine the role of pralines inthis conformational plasticity. We have expressed and purified this mutant
protein. Two millimolar p13 5"c 1P90AP 92 A crystallised in 50mM Tris pH7.5 , 30 %PEG 1500K. Diffraction data were collected at room temperature on a MAR345
image plate using Cu Ka ; radiation from a Rigaku RU200 rotating-anodegenerator source. The structure was solved to 2.7A in space group P6(3); unit
cell parameters were found to be a=b=75. 1, c=34.9 , a=f3=90 , y=120 .
The three dimensional structure of this mutant suggests that the reducedhydrogen bonding capacity of proline residues is more likely to be responsible
for the propensity of Cks proteins to form strand exchanged dimers thanbackbone strain between pralines 90 and 92 [1] .
References
I
Rousseau , F. , Schymkowitz, J. W. , Wilkinson , H. R. and ltzhaki , L. S.
(2001) Proc. Nat/. Acad. Sci. USA 98 , 5596-5601 .

232

ATuP-46
SAD PHASING USING SULFUR ANOMALOUS SCATTERING WITH
CHROMIUM RADIATION
K. F. Tesh , C . Yang , J. W. Pflugrath , C. N. Stence, D. A. Courville , and J. D.
Ferra
Rigaku/MSC, Inc. 9009 New Trails Dr. , The Woodlands, TX 77381 , USA(kft@RigakuMSC.com)

Anomalous scattering with soft X-ray radiation opens new possibilities inphasing for macromolecular crystallography. Anomalous scattering from sulfur
atoms collected on an in-house chromium radiation (2.29 A) source was used tophase the X-ray diffraction data of thaumatin (22 kDa), trypsin (24 kDa) andglucose isomerase (40 kDa) crystals. The contribution to the anomalous term ,! f"=1 .14 e·, from sulfur for CrK-alpha radiation is double compared to that for
CuK-alpha radiation, ! f"=0 .56 e·. The direct methods program SHELXD
successfully found sulfur positions using data sets with the resolution limited to
3.5 A. The statistical phasing program SHARP was used to produce theelectron density maps using the sulfur anomalous signal alone at a low
resolution (-3.5 A). An interpretable electron density map for each structure
was obtained solely from these phases derived from single-wavelength
anomalous dispersion (SAD) data from CrK-alpha radiation. Much less data ,that is lower redundancy, is required for this sulfur SAD phasing procedurecompared to the highly redundant data reported in the sulfur SAD phasing
procedure with CuK-alpha radiation. CrK-alpha radiation can also improve thestrength of anomalous scattering of many other intrinsic elements inmacromolecules, like Ca 2+, Zn 2 +, and P, because of the doubled value of! f" .
Furthermore , the anomalous scattering of selenium is increased substantiallywhen CrK-alpha radiation is used, because its ! f" is increased to 2.28 e· from
1.14 e· with CuK-alpha radiation .
In order to measure small Bijvoet differences accurately , several devices weredeveloped for the experiment, including an Osmic Confocal MaxFiux optic
optimized for CrK-alpha radiation , a helium path and a beam stop. In the cases
studied here, radiation damage to the samples and reduction of anomalous
signal were observed in some long data sets. Therefore, an adequate
collection strategy to maximize the completeness in a short scan range wasused in subsequent data collections. The results show the anomalous signal of
sulfur atoms can be quickly collected . Since the absorption of solvent and theloop with CrK-alpha radiation may not be negligible any more, the orientation of
the crystal and exposure time were accounted for in order to minimize theeffects of radiation damage and absorption. This experimental study shows
using CrK-alpha radiation can provide sufficient phasing power from sulfur
anomalous signals for routinely phasing protein data in-house.

233

ATuP-47
STRUCTURAL CHARACTERIZATION OF TWO PHOSPHOLIPASE A2
PROTEINS FROM THE VENOM OF THE AUSTRALIAN BROWN SNAKE,
PSEUDONAJA AFFINIS AFFINIS
Roopwant K. Judge ,"·b Matthew C. J. Wilce 8 and Jacqueline A. Wilceb
8School of Medicine and Pharmacology; bSchool of Biomedical and Chemical
Sciences , University of Western Australia , Crawley 6009 , WA, Australia(rjudge@receptor. ph arm. uwa .edu.au)

Brown snake envenomation is one of the leading causes of snakebite
injury in Australia. In the absence of antivenom treatment, the risk of mortality ishigh. Though potent and highly lethal , the venom of the brown snake common
to the Perth region of Western Australia , Pseudonaja affinis affinis (dugite} , has
not been well characterized. The clinical feature of envenomation isdisseminated intravascular coagulopathy (DIC) , and a procoagulant protein
contributing to this effect has been isolated. The secondary features ofenvenomation include paralysis , cardiac arrhythmias/arrest and respiratory
failure . Protein species involved in these effects have thus far not beencharacterized.
Based on the current level of understanding in snake venom research , themajor classes of venom proteins are neurotoxins , PLA 2 and proteins mediating
haemostasis. Of these , the PLA2 proteins are the most likely candidates for
involvement in the secondary features of dugite envenomation. The PLA2
proteins are the predominant protein species in snake venoms , and possessmany diverse pharmacological properties in addition to their enzymatic property.
Such functional properties include neurotoxicity, myotoxicity and antiplatelet
effects .
Our initial interest in the PLA2 proteins of dugite venom was assisted by aproteomic study investigating the affinity of brown snake antivenom for venom
proteins . The study , carried out in our laboratory , revealed a curious result.
While the brown snake antivenom was found to bind to the coagulant proteins , it
did not recognize any 12-14 kDa PLA 2 proteins . Such a result may explain why
victims of brown snake envenomation require a considerably higher dose ofantivenom . This class of protein was therefore of interest as a target for further
study, with insight into the structural and functional characteristics of theproteins potentially aiding the development of a new antivenom therapeutic.
In order to structurally characterize the PLA 2 proteins from dugite venom,a novel "reverse" approach was utilised. This approach was based on setting up
crystallisation trials for all PLA2 proteins separable from the crude venom . In theevent that good quality diffraction data could be collected , LC-MS/MS analysis
or N-terminal sequencing of the original sample provided the basis for extractionof the complete amino acid sequence from venom eDNA using PCR. The data
could then be solved using molecular replacement methods and built into using
the derived sequence . This approach resulted in two PLA2 structures which arepresented.

234

ATuP-48
X-RAY ANALYSIS OF YEAST LIPOAMIDE DEHYDROGENASECOMPLEXED WITH NAD+

Wataru Ad achi ," Kaoru Suzuki ,b Masaru Tsunoda ,c Takeshi Sekiguchi ,b Lester
J. Reed ,a and Akio Takenaka""Graduate School of Bioscience and Biotechnology, Tokyo Institute ofTechnology, Nagatsuta, Midori-ku , Yokohama 226-8501 , Japan ; bDepartment ofEnvironmental Science , College of Science and Engineering , lwaki-Meisei
University, Chuodai-iino , lwaki 970-8551 , Japan; cSchool of Pharmaceutical
Sciences, Showa University, Hatanodai, Shinagawa , Tokyo 142-8555, Japan ;dDepartment of Chemistry and Biochemistry , The University of Texas at Austin ,Austin , TX78712 , USA (wadachi@bio.titech .ac.jp) .
Lipoamide dehydrogenase (E 3) is one of the components of 2-oxoacid
dehydro-genase complex.
This enzyme
catalyses the oxidization of a dihydrolipoyl
group of E2 with the help of the cofactors, NAD+and FAD.
E3 belongs to the pyridine
nucleotide-disulphide oxidoreductase family of
glutathione
reductase ,trypanothione
reductase , mercuric ion reductase , etc. We
already reported the native E3 structure from
Saccharomyces cerevisiae [1] . In this study,
we co-crystallized yeast E3 with NAD+ to
elu cidate the mechanism of substrate binding.
Diffraction data were collected at 1OOK
and processed at 2.2 A resolution . The spacegroup and cell parameters are P212121, a=66.6 ,
b=96.4 , and c=160 .0A, respectively. Initial
phases were derived by molecular replacement
using the native structure. The atomic· -''"
parameters were refined (the final R=20.3% Fig. 2. The binding site of NAo·.
nicoti namide moiety of NAD• is flipped out
and Rrree=24 .6%). The overall structure of in the solvent region. Dots represent theyeast E3-NAD+ complex is shown in Fig. 1. van der waals surface of E3.
When the structure is superimposed on thenative one , the overall root- mean-square deviation is 0.62 A, suggesting no
significant difference on NAD+ binding. The final electron density map clearly
indicates that the adenosine moiety and the pyrophosphate group of NAD+ arebound to the enzyme , but the remaining nicotinamide moiety is disordered (Fig.
2) . It is interesting to note that the binding mode of the nicotinamide moiety isdifferent from those of the related enzymes in the same family. Contrary in the
structures of those enzymes complexed with NAD(P)H (reduced form) , thenicotinamide moiety is stacked on the isoalloxazine ring of FAD for electrontransfer, and the side chain of a Tyr residue near the binding pocket is flip out.
In the present enzyme , however, the nicotinamide does not enter the bindingsite , despite that the Tyr residue is replaced with lie . It is concluded that theexact positioning of NAD+ on FAD depends on the redox state of the cofactor
rather than on the existence of the Tyr side chain.
ReferenceI
Toyoda, T., Suzuki , K., Sekiguchi , T. , Reed , L. J. and Takenaka , A. (1998) J.
Biochem. 123, 668-74.

235

ATuP-49
A NEW METHOD FOR PROTEIN CRYSTALLIZATION: SAMPLING PHASESPACE IN A MICROFLUIDIC ENVIRONMENT
Kyle Self,a Carl L. Hansen ,b James M. Berger,c Stephen R. Quake ,b Susanna
Ng ,8 Shelley Godley ,8 and Joseph Barco 8
8

Fiuidigm Corporation , 7100 Shoreline Court South San Francisco , California
USA; bDepartment of Molecular and Cell Biology, University of California ,Berkeley, California USA; cDepartment of Applied Physics , California Institute ofTechnology, California USA (kyle.self@fluidigm.com)

Protein structure studies have long been the province of theexpert crystallographer - too esoteric and expensive for routine use in
drug discovery and development. Conventional methods can exhaust many
milliliters of starting protein and may only produce a small number of hits.
Fluidigm has thus introduced a novel technology that enables a new approachto the identification of crystallization conditions with 100 times less sample.
The TopazrM Crystallizer has been designed for intensive screening of
crystallization conditions using a unique combination of techniques redefined
specifically for use within a microfluidic environment. By leveraging fluidic
properties in nanoscale geometries, we have created the optimal setting for
liquid-liquid diffusion of protein and precipitating reagents.
The keystone of the system is a disposable microfluidic chip, or'microprocessor', fabricated using a proprietary process known as Multi-layer
Soft Lithography-the MSL TM process. We call it a 'Microprocessor' because
the metering of fluids takes place within the device , automatically, by way of tiny
pneumatically actuated valves. With 432 valves, the Topaz Microprocessor
combines nanoliter quantities of a concentrated protein solution with discrete
chemical crystallization reagents in three different mixing ratios to screen 144
distinct conditions (48 reagents at 3 protein-reagent ratios) with as little as 3 1-1Lof protein sample.
With the Topaz Crystallizer, one technician can run 5760 diffusion trials
per week , with as little as 120 1-1L of starting protein . Internal and externalstudies indicate that this system matches or outperforms traditional screening
methods in terms of sample conservation , the production of novel crystal hits,
and that it can promote the formation of high quality crystals by eliminating
convection while maintaining supersaturation conditions. We will describe thecrystallization mechanism and the advantages of the Topaz system.

236

ATuP-50
MICROSTRUCTURES OF THE FeSiBNbCu SOFT MAGNETIC MATERIALSTUDIED BY HIGH RESOLUTION ELECTRON MICROSCOPY (HREM)Vo Vonq and Ng .Q.Thang
Laboratory of Electron Microscopy - National Centre for Natural Science andTechnology , 18 Hoangquocviet Str. , Caugiay Hanoi , Vietnam(vvemlab@ncst.ac. vn)

Microstructures of the magnetic material Fe16 .5.xCu1NbxSin 5 B9 ,which wasannealed at various temperatures between 500°C and 750°C in Ar-atmotphereand then melt-quenching, has been studied by high resolution electron
microscopy.
Changes of the grain sizes , phases and nanocrystalline structure of the alloys
under influences of the heat treatments have also been systematicallyinvestigated by the JEM-4000EX,which has accelerating voltage 400 kilovolt
and resolution 0,17 nanomet .
In the work we present the method for preparation of brittle materials
for TEM plan-view investigations.The wide areas , which electron beam cantransmite , were received in the work.
The new results ,as well as , the alloys were changed from an amorphousstate through a partially crystallized state at 550° C and finally to a fully
crystallized state at 750°C, will be submitted . Grains were observed when thesample was annealed at750°C, they have size from 60 to 82nm in diameter
The magnetic properties and microstructural evolution of the material havealso been investigated .
References
1
Vong , V. (2000) The structural changes of the materials under influence ofheat treatments, World Scientific Publishing , 670- 673 Edited by YeongDerYao
2
Hono, K. , Hiraga , K. , Wang, Q., Inoue, A. and Sakurai , T. (1992) The
Microstructure Evolution of A Fen 5 Sh 3 .5 B9 Nb 3 Cu1 Nanocrystalline Soft
Magnetic Material , Acta Metal!. Mater. 40(9) , 2137-2147 , 1992

237

ATuP-51
MICRO-ARRAY CHIP FOR HIGH THROUGHPUT PROTEIN
CRYSTALLOGRAPHY
N. Watanabe, • I. Tanaka ," C. Nishijima ,b H. Takeuch i,b T. Sumic and T. lsekib"Division of Biological Sciences , Graduate School of Science , Hokkaido
University, Sapporo, Japan ; bChemicals Development Laboratories , Mitsubishi
Rayon Co. , LTO. Yokohama , Japan ; cProduction Technology Center, Mitsubishi
Rayon Co. , LTO . Hiroshima , Japan (nobuhisa@sci.hokudai.ac.jp)
Since protein crystallization is influenced by a number of factors ,development of a method for high throughput protein crystallization is one of themost important steps for accomplishment of structural genomics. We have beendeveloping a unique device for high throughput screening of protein crystallization
condition with nano-volume [1] . The device is micro-array chip utilizing the fiber
type DNA chip technology.
In order to hold various precipitant conditions in arrayed hollow fibers on thechip, several kinds of gels are used. We have already fixed types andpolymerization conditions of gels for almost all precipitants and wide range of buffer
pH . It is possible to make arrayed chip for random conditions such as Crystal
Screens of Hampton Research and Wizard Screens of Emerald BioStructures. A
property of precipitants in a gel has been confirmed by comparing crystallization
results with batch method.
The prototype array has from 12 to 48 different crystallization conditions
integrated on a cover glass size chip. Each precipitant solution of 50 nl is kept in ahollow fiber of the arrayed chip separately. One should just put protein solution

Figure . An arrayed chip of 48 conditions and its magnified view .

onto the chip manually with any single auto-pipetter. Protein and the precipitantsolutions are mixed in the micro cell on the chip, and crystallization screening will
be performed. Only 50 nl for each crystallization condition , total of about 2 to 10
micro-L protein solution , including loss, is required for screening of conditions on
the chip. Using the chip, we can perform many screening conditions without any
robotic systems . Our unique screening procedure will make it possible to set up
more than 100 different crystallization conditions within a few minutes.
Reference
Watanabe, N., Akita , T., Sumi , T., Takeuchi, H. and Tanaka , I. (2002) Acta
1
Cryst. A58 , C94

238

ATuP-52
STRUCTURES AND PHASE TRANSITION IN THE LAYERED PEROVSKITE
Lao.sSro.1Ti03

Christopher J. Howard and Zhaoming Zhang
Materials and Engineering Science, Australian Nuclear Science and Technology
Organisation , Private Mail Bag 1, Menai , NSW 2234 , Australia(cjh@ansto.gov.au)

The crystal structure of the layered perovskite Lao.sSro.1Ti03 at room
temperature has been solved by synchrotron X-ray powder diffraction in
combination with group theoretica l analysis . The structure is orthorhombic in
Cmmm , on a cell with a = 7.7556(1) , b = 7.7349( 1) , c = 7.7910(1) A. It isbelieved that this is the structure also adopted by La213Ti03. Pertinent features
are the alternation of fully and partly occupied layers of La (Sr) cations , and outof-phase tilting of the Ti0 6 octahedra around an axis perpendicular to thedirection of the ca tion ordering . The compound undergoes a second ordertransition to a tetragonal structure, the transition temperature being estimatedas 360 °C.

239

ATuP-53
STRUCTURE ESTIMATION OF ORBITAL ORDERED THIN FILMS
USING SYNCHROTRON RADIATION
Y. Wakabayashi," H. Sawa ,• M. Nakamura,b M. lzumi ,c K. Miyano ,c andY.
Murakamia"Institute of Materials Structure Science , High Energy Accelerator Research
Organization , Tsukuba 305-0801 , Japan ; bDepartment of Applied Physics,
University of Tokyo, Tokyo 113-8586, Japan ; cResearch Center for Advanced
Science and Technology, University of Tokyo, Tokyo 153-8904, Japan;
dDepartment of Physics , Tohoku University, Sendai 980-8578 , Japan(yusuke .wakabayashi@kek.jp)
The series of perovskite Mn oxides RE 1-x AExMn03 (RE: rare earth , AE:
alkaline earth metals , x denotes hole concentration) attracts great interest
because of their unique physical properties. These phenomena are widely
noticed for the orbital physics . Thin film technique makes us able to control theorbital state through the lattice distortion and doping ratio. However, it is difficult
for conventional x-ray scattering measurement that the whole atomic position
determination in thin films because scattering intensity is sensitive todisplacements of rare-earth and insensitive to oxygen displacements. In thisstudy , we succeeded to obtain the atomic displacements for various orbital
states using the observation of superlattice spots and their photon energy
dependence.
We have measured the atomic position in AMn0 3 (A: LaasSroA , Pra.sSroA
Nd 06 Sro.4 and Sr, we will abbreviate them to LSMO, PSMO , NSMO and SMO ,respectively) thin films on SrTi0 3 substrate . In the figure , their orbital states
expected from their conductivity and hole concentration are summarized. To
extract the oxygen position , we examined what element produce the scattering
amplitude at superlattice spots using the anomalous dispersion of scatteringfactor of x-ray.
X-ray diffraction measurements were carried out at BL-1A and 9C , Photon
Factory , KEK , Japan . For SMO , we did not observe any displacements. For
other three films , we observed several superlattice reflections from oxygen
displacement having wave vector (1 /2 1/2 1/2) . For PSMO and NSMO, weobserved additional superlattice reflections from oxygen displacement and Asite displacement in b-direction . Finally , we obtained the atomic displacements
as listed in the table. Mn-01 /Mn-02 is the ratio of Mn-apical 0 distance to Mnin-plane 0 distance. It is same as cia when the atomic displacement is zero .

/ o1

SMO
c [AJ3.76

LSMO
NSMO PSMO 3 832
3 788
·
3.784
. .,
~

o~<> ~~w
SrTi0 3 substrate a=3 .90A

240

Mn-02

SMO

0. 964

0.964

N SMO

0.970

0.973

PSMO

0.97 1

0.977

L SMO

0.983

0.985

Table : Results
estimation.

Fig .: Schematic view of the orbital states.

Mn-01

cia

of structure

ATuP-54
THIN-FILM CRYSTAL STRUCTURE DETERMINATION OF Bi3Fes012
MEASURED WITH VCIP METHOD
K. Tanaka , K. ltatsu, N. Adachi , and T. Okuda
Department of Materials Science and Engineering , Nagoya Institute ofTechnology , Gokiso-cho , Showa-ku , Nagoya 466-8555 , Japan(kiyo@tana .mse .nitech.ac.jp)
BiJFes01 2 (BIG) is famous for its gigantic Faraday effect. High quality
single-crystal films of BIG was grown for the first time by one of the authors(T.O.) by means of liquid phase epitaxy (LPE) on the substrate of (111) plane ofseveral garnets , Gd 3(Sc,Ga)s0 12 (GSGG) in the present study. The crystal
structure of BIG is highly important and interesting to investigate the significant
property of BIG. However single crystal structure determination has not been
done for these thin films because intensities from BIG was too small comparedto those from the substrates and the separation of the peaks from BIG andsubstrates were difficult.
Vacuum Camera Imaging Plate method (VCIP) has been developed by us.
Vacuum camera is a cylinder with imaging plate on its inner wall and rotation
photograph of a crystal located at the center of the camera are taken undervacuum . It enables us to measure weak X-ray diffraction intensities because
the noise due to air-scattering of X-rays is minimum which is two-order less thanthat without evacuation [1] .
Thin film of BIG 3.4 11m thick grown on the GSGG substrate with athickness of 452 .2 11m and 2133x1 067 11m wide was glued on a glass rod .
Incident X-rays were collimated by a collimator with a diameter of 500 Jlm. In
order to avoid absorption of diffracted beams from BIG , substrate is placed
toward the incident beam and the crystals were rotated about ±45 ° with 2 °overlap of scan with the following film. The peaks of BIG at low angles were
well separated from those of substrate . At middle angles only the peaks fromGSGG are observed. Separated peaks of Mo Ka doublet of GSGG wereobserved at high angles , where scattered X-rays by the substrate produce highbackground. Intensities were read with Fuji-BAS2500 . Total number ofobserved reflections from BIG was 1588. Overlapped peaks of BIG and GSGG
were not used . Reflections were corrected for absorption due to the substrateand BIG itself. Without the correction R-factor would not reduce from 75 %.
Measured Bragg peaks were indexed with the program DENZO. Slant
incidence of X-rays on the IP was also corrected for.
All the atoms except 0 atoms were refined assuming anisotropic
temperature factors . Final R-factor was 15.9 %. Since the size of the sample islarger than that of the incident X-rays , each peak is large and the setting ofintegration box accompanies some difficulty. However the integration process
can still be improved and much better R-factor is expected to be obtained. The
present study opened the door to the thin-film single crystallography.
ReferenceI
Zhurova , E. A., Zhurov , V. V. and Tanaka , K. (1999) Acta Cryst. 855, 917922 .

241

ATuP-55
POL YTYPE POSSIBILITIES ARISING FROM PSEUDO SYMMETRIC
CRYSTAL STRUCTURES ALLOWING STACKING FAULTS
Anthony. C. Willis , A. David Rae, Tory N. Cayzer, and MichaelS. Sherburn
Research School of Chemistry, The Australian National University, Canberra ,ACT 0200 , Australia (willis@rsc.anu.edu.au)

Alternative stackings of substructures allows the possibility of polytypes
and indeed crystals containing coherent blocks of structure of different spacegroups and different orientations [1]. Two recent organic structures fromservice crystallography fit this concept and are described , viz (i) 6-ethyl-3-oxo1,3,3a,4 ,7a-hexahydro-isobenzofuran-4-carboxylic acid methyl ester and (ii) the
related 6-hydoxymethyl compound.
Each can be described as an occupancy modulation of a 1:1 disorderedparent structure of orthorhombic symmetry which is the Fourier transform of theI even reflections , Pnma for (i) and lbm2 for (ii) . Ordered layers can be formed
but not all symmetry elements of such a layer can be symmetry elements of anordered crystal structure. This allows alternative origins Sdl2 apart for eachlayer. For (i) the layers have P 21ca symmetry and the ordered structure has
P.21/c. symmetry in the cell ap, bp, 2Cp. For (ii) the layers have Pbc2 1 symmetry
and the ordered structure has C.c. symmetry in the cell ap+Cp, bp,2Cp. If every
second layer shifts by c/2 we create a different orientation of the structure
allowing a twin-disorder mechanism . The third and fourth layers can be related
to the first and second by translations that differ by Sdl2. This allows thepossibility of polytypes. For (i) there is the possibility of different orientations ofan ordered structure of A 21/d.. symmetry in the cell ap, 2bp, 2Cp, ie P. 2 1/c.
symmetry in the cell -2bp, ap, bp+Cp while for (ii) there is the possibility of different
orientations of an ordered structure of Pbc2 1symmetry in the cell ap, bp, 2Cp.
Reference
I
Rae, A. D. , and Willis , A. C. (2003) Z. Krist. 218 , 221-230.

242

ATuP-56
THE TEMPERATURE DEPENDENCE OF THE CRYSTAL STRUCTURE OF
3,5-DI-T -BUTYLPYRAZOLE
Alexandre N. Sobolev, and Allan H. White
Chemistry, University of Western Australia , Crawley WA 6009 , Australia(ans@chem.uwa.edu.au)

Recent studies [1 ,2] of the structure of the title compound have suggested
it to be temperature dependent, in respect of the impact on disorder in therotational dispositions of the !-butyl groups , and in the hydrogen-bondedhydrogens . The structure has now been redetermined at 1OK, revealing, enroute , a phase transiti on at ca. 11 OK from the high-temperature Pbca form , Z =8, to a low-temperatu re Pb21a form , Z = 16, the contents of the asymmetric unit
increasing from one molecule, with temperature dependent disorder, to fourmolecules ('A-D'), all devoid of crystal lographic symmetry. At 10K, all species inthe structure are ordered , with the molecules partitioned pairwise into 'cis' and'trans' forms (referring to the relative rotational dispositions of the methylhydrogens .)Redeterminations of the structure of 3,5-dimethylpyrazole[3], at roomtemperature and at 1OK are also discussed.

T=120 KT = 10 K

References
Aguilar-Parilla , F., Limbach , H. -H ., Foces-Foces, C. , Cano , F. H.,
I
Jagerovic, N., and Elguero, J. (1995) J. Org. Chern. , 60, 1965-1970.
Deacon, G. B., Gitlits , A. , Roesky, P., Burgstein , M. R., Lim , K. L.,
2
Skelton, B. W., and White, A. H. (2001) Chern. Eur. J. , 127-138.
(a) Baldy, A. , Elguero, J., Fawe , R. , Pierro!, M., and Vincent, E. -J . (1985)
3
J. Arner. Chern. Soc., 107, 5290-5291 .
(b) Smith, J . A . S., Wehrle, B., Aguilar-Parrilla, F., Limbach, H. -H ., FocesFoces , M. C., Cano, F. H., Elguero , J., Baldy, A ., Pierro!, M. , Khurshid, M.
M. T., Larcombe-McDouall , J. B. (1989) J. Arner. Chern . Soc. , 111 , 73047312 .

243

ATuP-57
EXPERIMENTAL AND THEORETICAL STUDIES OF THE SULFOXIMINEGROUP [R 1 -S(=O)(=N-R 2 )R 3]: DETECTION OF POSSIBLE LATTICEEFFECTS

Gerhard Raabelnstitut fuer Organische Chemie , Rh ei nisch-Westfaelische Technische
Hochschule Aa chen , Professor-Pirl et-Strasse 1, D-52074 Aachen , Germany(gerd .raa be@thc.rwth-aachen. de)
Sulfoximines of general structure R 1-S(=O)(=N-R2)R 3 play an importantrole in stereoselective synthesis . Eva luati on of the ava ilab le structural
information obta ined by X-ra y diffraction meth ods reveals that especially th eva lues of the bond angles at the su lfur atom cover relatively wide ranges. Thi srises th e question as to th e influence of th e environment in the crystal lattice on
the structure of the sulfoxim ine group. Th e easiest way to detect such latticeeffects is to perfo rm a qua ntum-chem ical calcu lation for the isola ted
unperturbed molecule and to compare its optimized structure with th e one
ob tain ed experimentally in th e solid state. Although sta te of art methods likeconventional ab initio and DFT-based methods today can handle relatively large
systems the computationa l efforts increase significantly as the molecule underconsideration becomes larger. Thu s, the much faster semiempirica l methods
which also require significa ntly less memory are still widely used to optimize thestru ctures of larger molecules . Th e reliabi lity of the structures obta ined withthese methods criti ca lly depends on their parametrizations. Determin ation of th esemiempirica l parameters , however, is never a trivial task especially not in thecase of an element like su lfur which ex ists in a va ri ety of va lence sta tes . We ,th erefore , performed sem iempiri ca l geometry optimizations for a large numberof su lfoximin es for which the so lid state structures are known from X-ray
diffraction stud ies. In these ca lcu lations we employed the most frequently used
sem iempirica l methods (MND0[1], AM1 [2], PM 3[3], MSIND0[4]) . Comparisonof the semiempirica l results with those obta ined for sample compounds on theconventional ab initio and DFT level shows which of the four meth ods is suited
to predict lattice effects in th e case of su lfoximines.
References
I
Dewa r, M. J. S. and Thi el, W. (1977) J. Am. Chern. Soc. 99 , 4899-4907.
2
Dewa r, M. J. S., Zoebisch , E. G., Healy, E. F. and Stewart, J. J.P. (1985)
J. Am. Chem . Soc. 107, 3902-3909 .
3(a)Stewart, J. J. P. (1989) J. Comput. Chern. 10 , 209-220 . (b)Stewart, J. J.
P. (1989) J. Com put. Chern. 10, 221 -264.
4(a)Ah lswede , B. and Jug , K. (1999) J. Comput. Chern. 20 , 563.
(b)Ahlswede , B. and Jug, K. (1999) J. Comput. Chern. 20 , 572 .

244

ATuP-58
THE PDF-4/FULL FILE AND PDF-4/0RGANICS DATABASES:NEW DATA MINING TOOLS FOR STRUCTURAL CRYSTALLOGRAPHY
AND MATERIALS CHARACTERISATION
Brian O'Connor.• Camden Hubbard ,b Tim Fawcett,c and John Faberc"Materials Research Greoup, Department of Applied Physics, Curtin University ofTechnology, GPO Box U1987, Perth, WA 6845, Australia; bOak Ridge National
Laboratory, Oak Ridge , TN 37831-6064, USA; clnternational Centre for Diffraction
Data , 12 Campus Boulevard , Newtown Square, PA 18073-3273, USA(B .O'Connor@curtin.edu.au)
The ICDD is a not-for-profit organisation compns1ng 340 of the world 's
leading x-ray scientists. It is dedicated to collecting , editing , publishing anddistributing powder diffraction data for the characterisation of crystalline materials.
The membership of the ICOD consists of worldwide representation from academe,
government and industry. It is our mission to continue as the world centre for
quality x-ray powder diffraction data to meet the needs of the technical community.
Through the combined efforts of the members and its staff of 40 at ICDD
Headquarters, the organisation serves the crystallography and materials science
communities (i) by producing the ICDD Powder Diffraction File (PDF) and otherdata base products for materials characterisation ; (ii) through x-ray analysis
education programs and conference management (including the Denver X-ray
Conference); and (iii) through philanthropic initiatives such as scholarship support
for postgraduate students working in the field.
The ICDD has recently released the PDF-4/Full File powder diffraction
database which gives powder diffractionists a very sophisticated tool for data
mining. PDF-4 contains over 87,000 measured patterns and approximately 49 ,000
patterns simulated from crystal structure data. Searches may be conducted formetals & alloys, pharmaceuticals, zeolites, superconductors , detergents pigments,
ceramics, corrosion products, polymers , cement materials, forensics andexplosives sub-files. Common query fields for data mining include elemental
composition , formula, common name , colour, melting point, space group , unit celldimensions, Pearson symbol , mineral classification and statistical quality of thepattern. Algorithms are provided to transform single cystal structural data into
powder patterns using 'on-the-fly' calculations which include adjustable
experimental effects such as slit configuration and crystallite broadening.
The organisation has recently released PDF-4/0rganics which contains datafor over 146,000 organic and organometallic phases of which almost 123,000
patterns are calculated from ICDD and CCDC single-crystal structural data. This
exciting new tool has awesome data mining capability through searching 30+
separate diffraction fields and physical properties which include formula , chemicalname , functional group index, drug activity, space group and unit cell dimensions.
Material-type sub-files include organics, pharmaceuticals , polymers, pigments andforensics .
Examples to be described will include:
1. Making use of isomorphous phase information in the data base for structure
solution
2. Pharmaceutical polymorph characterisation
3. Unknown identification

245

ATuP-59
HIGH TEMPERATURE LAUE METHOD WITH POLYCHROMATIC SR: ITSAPPLICATION TO QUARTZ PHASE TRANSITION

Kazumasa Ohsumi ," Yoshikazu Miyata ,b Katsuhiro Kusaka ," Takeshi
Nakagawa ," and Kenji Hagiyac"Photon Factory, lnst. Materials Structure Science , KEK , Tsukuba, 305-0801 ,Japan; bGraduate School for Advanced Studies, KEK , Tsukuba, 305-0801 ,Japan ; cFaculty of Science , Himeji Institute ofTechnology , Hyougo, 678-1297 ,Japan (kazumasa .ohsumi@kek.jp)
Th e Laue method is advantageous for obtaining diffraction data from acrystal at both low and high temperatures , because perturbative air-flow aroundthe sample is reduced due to the stationary crystal when using polychromaticSR.
Low and high temperature equipment and a control system for observation
through an optical microscope(LK-600PH ; Linkam Scientific Instruments Ltd .)was developed and installed vertically on the Laue camera at BL-4B1 of the
Photon Factory, KEK, Tsukuba . The Laue camera was originally developed for
diffraction studies especially for sub-micrometer sized specimens and /or
micrometer sized area of a larger sample[1],[2] . Taking into account thepossibility of a thermal gradient within the sample , the Laue camera is suitablefor our purpose. The low and high temperature system on the Laue camera wasapplied to the a-~ phase transition of quartz(Si0 2) , because it is well known
that a modulated structure exists in the narrow temperature range between a-~quartz[3] .
Diffraction data were obtained from a - to ~-phase through the modulated
structure region at 0.1 K steps. Satellite-reflection profiles and intensities aroundthe main spots clearly changed at each temperature , partially shown in the
figure below. Refinements of a - to ~-quartz were carried out including
substructure of the modulated structure region. The result indicates that thechanges of positional and anisotropic thermal parameters describe the behaviorof the oxygen atom through modulated structure region .

.

'Tlm+0.4'

T,m+O.S'

T1m+0.6'

Tlm+0.7'

T1m+0.8

T;m : Temperature at maximum intensities of satellite reflections
References
I
Ohsumi , K. , Hagiya, K. and Ohmasa , M. (1991) Jour.Appi.Cryst. 24, 340348.
2
Ohsumi, K., Hagiya, K., Uchida, M., Suda , N., Miyamoto, M., Kitamura , M.
and Ohmasa , M. (1995) Rev. Sci. lnstrum. 66(2) , 1448-1450.
3
van Tendeloo, G. , van Landuyt, J. and Amelinckx, S.(1976) Phys. Stat.
Sol. (a) 33 , 723-735.

246

ATuP-60
X-RAY EXTENDED-RANGE TECHNIQUE FOR PRECISION MEASUREMENT
OF THE X-RAY MASS ATTENUATION COEFFICIENT AND IM(F) FOR
MOLYBDENUM USING SYNCHROTRON RADIATION8

C. T. Chantler, 8 M. de Jonge ,8 Z. Barnea ,8 C. Q. Tran ,8 B. B. Dhal , and D. J.
Cooksonb
8
School of Physics, University of Melbourne , Parkville , Vic 3010 , Australia ;bANSTO , Private Mail Bag 1, Menai , NSW 2234 and Chem-Mat-CARS-CAT(Sector 15, Bldg 434D) , Argonne National Laboratory, 9700 S. Cass. Avenue ,Argonne , IL 6043 (chantler@ph.unimelb.edu.au)Complex X-Ray form fa ctors are used in crystallography , materialscience , medical diagnosis , refra ctive index studies and XAFS. Determinationsof the co mplex component typically differ by around 10% or 10 standard
deviations. This has long been a concern of the International Union of
Crystallography, and we have seriously undertaken to determine sources ofsystematic error in these measurements. We apply the X-Ray Extended-Range
Technique [1 ,2] for accurate measurements of the mass attenuation coefficientand the imaginary component of the atomic form factor . We present our latest
experimental results for Molybdenum featuring an absolutely calibrated energy
scale , harmonic component determination at a level of 1 photon in 104 andsample thickness calibration. The range of the attenuation measurement far
exceeds the Nordfors range of 2 < In ( lo/ I ) < 4, resulting in an increase of
precision and accuracy to below 0.1 % in the range from 13.5 keV to 41.5 keV.
The new result challenges available theoretical calculations and suggests thatnew methods of computation are required to approach the accuracy of theexperimental data , while also challenging us to develop a theory of XAFS
capable of understanding the absolute magnitude of fine structure oscillations.
Molybdenum· Attenuation ([" / ]) vs Energy· Near -Edge

80

20 ,../
20.00

20.05

20.10
20. 15
Energy (kcV)

20.20

20.25

Prelimin ary results of an absolute measurement of the total att enuation coefficient of
Molybdenum showing typical grid densities employed near the fine structure.

References
I
Chantler, C. T. , Tran , C. Q., Paterson , D. , Cookson , D. and Barnea , Z.
(2001) Phys. Lett. A286, 338-346.
2
Chantler, C. T. , Tran , C. 0. , Barnea , Z., Paterson , D., Cookson , D. andBalaic, D. X. (2001) Phys. Rev. A64, 062506-1 -15.

247

ATuP-61
X-RAY MASS ATTENUATION COEFFICIENT OF SILICON: THEORYVERSUS X-RAY EXTENDED-RANGE TECHNIQUE AND OTHER
EXPERIMENTS

C. T. Chantler, C. Q. Tran, and Z. Barnea
School of Physics , University of Melbourne, Parkville , Vic 3010 , Australia(chantler@ph.unimelb.edu.au)

Structural determinations near absorption edges using synchrotron
radiation sources , multiple-wavelength anomalous dispersion (MAD) techniquesand X-ray absorption fine structure (XAFS) investigations have shown manysuccesses in recent years. They provide information on local electron density
distributions, lattice spacings, atomic environments in solids and excited-state
occupation levels. However, the X-ray interaction away from edges can be justas revealing about the electronic structure , inner-shell orbitals , and relativistic
corrections to atomic structure . We compare new experimental X-ray total massattenuation coefficients of silicon obtained with the X-ray Extended-Range
Technique (XERT) [1, 2] from 5 keV to 20 keV with theoretical calculations andearlier experimental measurements over a 5 keV - 50 keV energy range . The
accuracy of between 0.27% and 0.5% of the XERT data allows us to probe
alternate atomic and solid state wave-function calculations and to test dominant
scattering mechanisms (Laue-Bragg , Rayleigh and TDS assumptions).
Discrepancies between experimental results and theoretical computations of theorder of 5% are discussed in detail. No single theoretical computation iscurrently able to reproduce the experimental results over the entire 5 keV - 50
keV energy range investigated.
References
I
Chantler, C. T. , Tran , C. Q ., Barnea , Z., Paterson, D. , Cookson , D. andBalaic, D. X. (2001) Phys. Rev. A64, 062506-1- 15.
2Tran, C. Q., Chantler, C. T., Barnea, Z., Paterson , D., and Cookson , D. J.
(2003) Phys. Rev. A in press.

248

ATuP-62

THE CRYSTAL STRUCTURE OF DOPED PEROVSKITES DERIVED FROMELECTRON SCATTERING TECHNIQUES
C. J. Maunders ," J. E. Etheridge ," C. J. Rossouw,b and H. J. Whitfieldb
aDepartment of Physics and Materials Engineering , Monash University, Clayton,
Victoria , Australia ; bCSIRO Manufacturing and Infrastructure Technology,
Private Bag 33 , Clayton South MDC , Victoria 3169, Australia(christian .maunders@spme.monash.edu.au)

Structural and electronic properties of perovskites can be manipulated
through the addition of dopant atoms. For example , stabilisation of hightemperature phases at room temperature is possible with the introduction ofsmall co ncentrations of foreign ions into the structure. The present work
considers a certain class of barium titanates , having the perovskite structure ,that have been transformed into a hexagonal phase at room temperature that is
stabilised by the addition of dopant Ru or Mn atoms . The structure focussed on
is the 6 layer (6H) hexagonal Ba 3(Ru ,,Ti 2)0 9 .
In order to understand how the dopant atoms are accommodated within
the 6 layer (6H) hexagonal Ba 3 (Ru, ,Ti 2)0 9 structure , we are investigating theunit cell configuration using a variety of electron scattering techniques . Space
group determination was performed using convergent beam electron diffraction(CBED). Local lattice parameters were determined from intersections of various
deficit lines derived from higher order Laue zone(HOLZ) beams . The sublatticesite occupancy of Ru dopant atoms was subsequently confirmed using atom
location by channelling enhanced microanalysis (ALCHEMI). Transmission
electron microscopy has been used to investigate the microstructure at lattice
resolution .
The dynamical dispersion surface excitations and spacings were observedin the quantum state line contrast in HOLZ beams . This relates back directly tothe predominant eigenstates that are excited under highly symmetric scattering
conditions , and these were observed to change with small tilt such that different
sets of eigenstates (partial waves) are excited .

249

ATuP-63
EFTEM AND HRTEM STUDIES OF METAKAOLINITE AND METADICKITE
Sujeong Lee ,a Youn Joong Kim ,b Hi-Soo Moon ,c and Won-Seon Seo•
"Ceramics Reliability Center, Korea Institute of Ceramic Engineering andTechnology , Seoul 153-801 , Korea ; bDivision of Analysis and Measurement,
Korea Basic Science Institute , Daejon 305-333 , Korea; cDepartment of Earth
System Sciences , Yonsei University, Seoul120-749 , Korea (crystal@kicet.re .kr)

Metakaolinite in the kaolinite-mullite reaction series is microcrystalline oramorphous, which makes it difficult to study by XRD , NMR and conventional
TEM analyses. However, a 14A modulation has been recently reported with theperiodicity along the c'-axis[1] . Several models of metakaolinite are proposed ,but suffer from little understanding of structural ordering along the c-axis andthe fact that the spinel-type phase is formed not by the decomposition of
metakaolinite but by a topotactic formation with respect to metakaolinite before
the decomposition of metakaolinite[2-6] . We performed EFTEM and HRTEM
studies to reexamine metakaolinite and metadickite structures , with a focus on
the short-range order. Different lengths of modulations develop along the c'-axis
from the regions where the structures are disturbed due to the OH elimination
during the progression of dehydroxylation in kaolinite and dickite. The 14A
modulation is confirmed to be the most common in BF images , which provesthat the pattern of vacant octahedral sites in successive layers changes to lose
the original symmetry. Mullite crystals are abruptly induced from the kaolinite
heated at 630C by electron beam radiation during HRTEM imaging , whichindicates the difference of the structural stability between the kaolinite
dehydroxylates at 550C and 630C. The periodicity along the c ·-axis , taken
together with all the reasonable crystallographic data in earlier works , should beconsidered to propose the metakaolinite structure .
ReferencesI
Lee , S. , Kim , Y. J. and Moon , H. -S . (2003) J. Am. Ceram . Soc. , 86[1],174-176.
2
Brindley , G. W. and Nakahira , M. (1959) J. Am. Ceram. Soc ., 42[7] , 314318.
3
MacKenzie, K. J. D., Brown , I. W. M., Meinhold , R. H. and Gowden , M. E.
(1985) J. Am. Ceram. Soc ., 68[6] , 293-297 .
4Rocha , J. and Klinowski , J. (1990) Phys Chern Minerals, 17, 179-186.
5
Gualtieri , A. and Bellotto , M. (1998) Phys Chern Minerals, 25 , 442-452 .
6
Lee , S. , Kim , Y. J. and Moon , H. -S . (1999) J. Am. Ceram. Soc. , 82[10],2841-2848.

250

ATuP-64
DEPENDENCE OF THE ACCURACY OF A CONTINUOUS PHASE
TRANSITION TEMPERATURE ON ANGULAR RESOLUTION IN POWDERDIFFRACTOMETRY

Masatomo Yashima ,8 Mizuki Mori ,8 Roushown Ali ,8 Masahiko Tanaka ,b and
Takeharu Morib
8

Department of Materials Science and Engineering , Interdisciplinary Graduate
School of Science and Engineering , Tokyo Institute of Technology, 4259
Nagatsuta-cho, Midori-ku , Yokohama , 226-8502 , Japan ; bPhoton Factory,
Institute of Materials Structure Science , High Energy Accelerator Research
Organization , 1-1 Oho , Tsukuba , lbaraki , 305-0801 , Japan(yashima@materia. titech .ac.jp)

A number of researchers have studied the structural phase transition invarious materials, because it is one of the most important topics in many fields
such as physics , chemistry, biology, geoscience and materials science. Near
the transition temperature , many materials exhibit interesting and usefulproperties. Therefore , it is of vital importance to determine accurately thetransition temperature and the temperature dependence of unit-cell parametersnear the transition point. It is often difficult to determine precise unit-cellparameters near the transition point by conventional laboratory-based X-ray
powder diffractometer, due to low angular resolution . On the contrary , thesynchrotron radiation powder diffraction has much narrower peak width and no
splitting as Kalpha1 and Kalpha2 peaks . Therefore we have investigated theunit-cell parameters near transition point by synchrotron radiation powder
diffraction technique [1 ,2] . The precision of unit-cell parameters is improved byhigher-resolution diffractometer. Therefore the precision of the transition point
would also be improved by using higher-resolution instrument. However, to ourbest knowledge, the effect of angular resolution on the accuracy of a transition
temperature has not been investigated in the literature. We have investigated insitu a continuous transition between the orthorhombic and tetragonal phases indouble-perovskite-structured La 0 _64(Tio92, Nboos)03 by three X-ray powder
diffractometers with different delta(d)/d resolutions of 0.03 %, 0.06% and 0.10%[3] . The d and delta(d) denote the lambda/(2sin(theta)) and peak width wherelambda and theta are wavelength of X-ray and Bragg angle . Only the highestresolution diffractometer of delta(d)/d =0 .03 % was able to detect the peak
splitting between 400 and 040 reflections in the temperature range of 327 to
339 deg C. It was found that the accuracy of the transition temperature isconsiderably improved with decreasing of delta(d)/d value. The maximum
temperature where the peak splitting between 400 and 040 reflections is
detectable increases , while the transition temperature determined by a powerlaw decreases with decreasing of delta(d)/d value .
ReferencesI
Ali , R. , Yashima, M. , Tanaka , M. , Yoshioka , H., Mori , T . and Sasaki , S.
(2002) J. Solid State Chem. 163, 51-59 .
2
Yashima , M., Ali , R. , Tanaka , M. and Mori , T. (2002) Chem. Phys. Lett.
363, 129-133.
3
Yashima , M. , Mori , M. , Ali , R. , Tanaka , M. and Mori , T. (2002) Chem.
Phys. Lett. in press .

251

ATuP-65
A NEW HIGH-TEMPERATURE FURNACE FOR HIGH-RESOLUTIONSYNCHROTRON RADIATION POWDER DIFFRACTION STUDY UP TO
1900K

Masatomo Yashima ,8 Masahiko Tanaka ,b Takeharu Mori ,b Kenjiro Ohouchi ,8and Daiju lshimura 880epartment of Materials Science and Engineering , Interdisciplinary Graduate
School of Science and Engineering , Tokyo Institute of Technology, 4259
Nagatsuta-cho, Midori-ku , Yokohama , 226-8502, Japan ; bPhoton Factory,
Institute of Materials Structure Science , High Energy Accelerator Research
Organization , 1-1 Oho , Tsukuba, lbaraki , 305-0801, Japan(yashima@materia. titech .ac.jp)

A number of researchers have studied the structural change and the phasetransition in various materials , because they are some of the most important topics
in many fields such as physics, chemistry, biology, geoscience and materials
science. Near the transition temperature , many materials exhibit interesting anduseful properties. Therefore, it is of vital importance to determine accurately thetransition temperature and the temperature dependence of unit-cell parametersnear the transition point. It is often difficult to determine precise unit-cell andstructural parameters near the transition point by conventional laboratory-based Xray powder diffractometer, due to low angular resolution. On the contrary, thesynchrotron radiation powder diffraction has much narrower peak width and no
splitting as Kalpha1 and Kalpha2 peaks. Therefore we have investigated the unitcell parameters near transition point by synchrotron radiation powder diffraction
technique [1 ,2]. But the previous furnace developed by Tanaka [3) could not work
well above 700 Celsius degree. In the present study we successfully devised andfabricated a new furnace that enabled in situ accurate structural study throughhigh-resolution synchrotron powder diffraction. The delta(d)/d resolution of thepresent powder diffraction data was estimated to be 0.03% from the full width at
the half maximum . It was found that thi s furnace is quite useful to distinguish a very
similar crystal structure from each other. The synchrotron powder diffraction data of
calcium titanate measured at about 1300 Celsius degree was analyzed by a
combination method of the Rietveld refinement and of a maximum entropy method
based pattern fitting where the computer programs RIETAN-2000, ENIGMA,
PRIMA and VENUS were used [4 ,5). Chemical bonding between titanium andoxygen atoms was clearly observed in the electron density map of the calcium
titanate at 1300 Celsius degree. This furnace would open a new world of the hightemperature science and technology in a variety of academic fields such as
materials science, physics, chemistry and geoscience.
ReferencesI
Ali , R. , Yashima , M., Tanaka , M. , Yoshioka , H. , Mori, T . and Sasaki , S.
(2002) J. Solid State Chem. 163, 51-59.
2
Yashima , M. , eta/. (2002) Chem. Phys. Lett. 363 , 129-133.
3
Tanaka, M. (2000). Photon Factory Activity Report 1999 #17 , KEK
Progress Report 2000-1 , edited by Y. Murakami eta/. , pp.42-44 . HighEnergy Acceleration Research Organization, Tsukuba , Japan .
4
Tanaka , H., eta/. (2002) J. Appl. Cryst. 35, 282-285.
5
Izumi F. , (2002) J. Cryst. Soc. Jpn. 44, 380-388.

252

ATuP-66
SUB-SECOND X-RAY DIFFRACTION MEASUREMENT AND STRUCTURE
ANALYSIS BY MSGC

Hidehiro Uekusa ," Yuji Ohashi, 8 Y. Tsuji,b Y. Nishi,b T. Tajima ,b and S. Adachi c
8

Department of Materials Science , Tokyo Institute of Technology, Tokyo 1528551 , Japan ; bRigaku Corporation , Tokyo 196-8666, Japan; cHARIMA Institute
RIKEN , Hyogo 679-5148 , Japan (uekusa@cms.titech.ac.jp)

Rapid X-ray diffraction measurement technique is an essential to realize
the time-resolved observations of crystalline-state reactions, unstable species in
excited state and reaction intermediates. To achieve time resolution of seconds
or sub seconds order, the use of photon counting type two-dimensional detector
is required .
Recently , MSGC (Micro Strip Gas Chamber) was developed for the rapid
X-ray data collection. MSGC is a gaseous detector having both photon counting
and two-dimensional imaging properties. The features of the detector are alarge detective area of 10 x 1Ocm , a fine positional resolution of 100 micrometerand an excellent capability for high counting rate up to 107 cps suitable for thesynchrotron radiation experiments.
With the measurement system consists of a MSGC detector, one axis
goniometer and a laboratory X-ray generator, complete data set from typicalorganic crystals were recorded within several minutes to seconds range and theresults of structure analyses were satisfactory [1]. In the experiment using thesynchrotron radiation at SPring-S, structure analysis of three dimensionalreflection data from sub-second measurement was successfully achieved . Foran application of real-time monitoring of diffraction pattern , the timing resolutionof millisecond can be achieved. By utilizing this ability and bright SR at SP8 ,time-resolved measurement of the cell dimension of photo-irradiated Platinumcomplex crystal [2] was carried out. The dimensional change caused by photoexcited Platinum complex and thermal expansion of the crystal was clearlyobserved.
References
I
Ochi , A. , Uekusa, H. , Tanimori , T ., Ohashi , Y. , Toyokawa , H. , Nishi , Y. ,Nishi, Y., Nagayoshi, T. and Koishi, S. (2001) Nucl. lnst. Meth. Phys. Res.
A467-468 , 1148-1151.
2
Yasuda , N. , Kanazawa , M., Uekusa, H. and Ohashi , Y. (2002) Chern . Lett.
31 , 1132-1133.

253

ATuP-67
THE BEAMLINE FOR MACROMOLECULAR ASSEMBLIES OF THE
INSTITUTE FOR PROTEIN RESEARCH
Masato Yoshimura ,8 Eiki Yamashita ,8 Atsushi Nakagawa ,8 Masaki Yamamoto,bShinya Yoshikawa ,c and Tomitake Tsukihara 88lnstitute for Protein Research , Osaka University, Suita , Osaka 565-0871 ,Japan ; bJASRI/RIKEN Harima Institute, The Institute of Physical and Chemical
Research , Sayo-gun , Hyogo 679-5148 , Japan; cDepartment of Life Science ,Himeji Institute ofTechnology, Ako-gun Hyogo 678-1297 , Japan(yoshimur@protein.osaka-u.ac.jp , atsushi@protein.osaka-u.ac.jp)

Biological macromolecular assemblies play significant roles in many
biological reaction systems , including energy transfer, protein synthesis , protein
analysis , DNA replication and signal transduction. More than 20 ,000 protein
structures are now known since the first crystal structures of hemoglobin andmyoglobin were determined. On the other hand , fewer than 100 structures ofmacromolecular assemblies , including viruses have been determined by X-ray
crystallography. This is because of the difficulties faced in the preparation ,crystallization , X-ray diffraction measurement , and crystal structure
determination of large molecular assemblies. A beamline for biologicalmacromolecular assemblies at SPring-8 , which is specially designed to collecthigh resolution and high quality diffraction data from crystals of macromolecule
assemblies with large unit cells , has been operating since September 1999.
This beamline uses a standard undulator of SPring-S as a light source , apiece of super mirror as a condensing device and a rotated-inclined double
crystal as a monochromator. The wavelength is usually fixed at 0.9 A, but MAD
experiments can also be performed. The size of the X-ray beam can bechanged according to the size of the crystal using a slit-system.
We recently developed a new type area detector, which is a hybrid ofimaging plates and a CCD. Thi s detector has a CCD detector (Bruker-AXS
SMART6500) surrounded by independent six imaging plates. The CCD detector
can be used both for diffraction data collection of ordinary protein crystals
diffracting below -2.0 A resolution and for checking the quality of crystals .
Imaging plates are used for diffraction data collection from macromolecularassemblies , because of the large detector area.
The present status of beamline including the new detector system andsome diffraction data will be presented.

254

ATuP-68
X-RAY MICRODIFFRACTION SURFACE AREA INVESTIGATIONS OFTUNGSTEN CLAD MAGNESIUM ALLOYS

Natasha WrighV M. Mandagie,b and G. Theodossioua•csiRO Manufacturing and Infrastructure Technology , Private Bag 33 , Clayton
South MDC , Victoria 3169 , Australia ; bCAST Cooperative Research Center forCast Metals Manufacturing (Natasha .Wright@csiro .au)

X-ray microdiffraction is a useful tool for fast , non destructive and effective
determination of crystalline phase composition in a wide range of materials[1 ,2] . Technological advancements both in the field of x-ray optics and inparticular the development of 2-dimensional area detectors have made surface
area crystalline phase mapping possible with laboratory source instruments [3].
This paper discusses one of the many unique applications undertakenusing the Bruker GADDS(General Area Detection Diffraction System)
instrument situated at CSIRO Manufacturing and Infrastructure Technology.
The material investigated was a polished cross section of an Mg Alloy that had
undergone laser cladding with a Tungsten material. Each cladding area had
undergone different laser parameters to produce different phase compositions ,with area of most interest being the interface region between the substrate andcladding.
X-ray microdiffraction maps of the entire cladding area for each laserparameter were undertaken using the GADDS surface area mapping capability.
GADDS results indicated structural changes in spots as small as 100 micron in
the cladding-substrate interface region ; these differences would have been very
difficult to detect using conventional powder diffraction techniques [1] . The area
was then analyzed using Scanning Electron Microscopy and Energy Dispersive
X-ray Spectroscopy (EDXS) so that image morphology and elemental speciesof the various regions could be obtained and to verify the chemical data
provided with phase composition results from GADDS analysis. There wasgood correlation between chemical data and phase composition. GADDS
surface area mapping , in conjunction with SEM and EDXS , was successful inthe characterization of crystalline phase composition in Tungsten Clad
Magnesium Alloys.
ReferencesI
Hay, D., Scarlett, N. and Wilson , N. (2001) Proc.Eng2001Mat, Melbourne ,Australia , IMEA press, 99-104.
2Taylor, R. C., Hinczak, I. (2001) Rietveld Made Easy, 188-194.
3
Bruker AXS , Diffraction Solutions- GAOOS. 0-76181 , (1997) , Karlsruhe ,Germany , FRG press , B86-E00001 .

255

ATuP-69
ON THE DESIGN FOR A VERSATILE IMAGING AND HARD X-RAY
BEAMLINE FOR MATERIALS SCIENCE , BIOMEDICAL, AND MEDICALAPPLICATIONS AT "BOOMERANG"

S. W. Wilkins a.b R. A. Lewis,b K. K-W. Siu,b A. W. Stevenson ,• K. A. Nugent,cand D. J. Parry•"CSIRO, Manufacturing and Infrastructure Technology PB33 Clayton Sth , Vic
3169 , Australia; bSchool of Physics & Materials Engineeri ng , Monash
University, Clayton , Vic 3168 , Australia ; cSchool of Ph ysics , University of
Melbourne, Vic 3010, Australia (Steve .Wilkins@csiro .au)
Th e development of medium-sized storage rin gs with high brightness andof new optics and imaging methods opens up exciti ng possibilities for materials
science , biomedical , clinical medical , and other research at such sources. We
outlin e key design features for a versatile imaging and hard X-ray beamline
proposed for "Boomera ng", operating in the energy range 10-90 keV and with anumber of modalities for imaging including ; in-line projection imaging (1 ,2] withboth monochromatic and "pink" beam as wel l as crysta l-based methods (3] .
The proposed insertion device for this beamline is a 6T superconducting wiggler
in order to give high flux in the hard X-ray regime, sma ll source size andrelatively wide divergence in the horizontal plane.
Key features of the beamline are the use of 2 experimental sta tions(hutches) involving a very long beamline (- 150m) for Station 2 as well as theabi lity to ope rate in a va ri ety of imaging and diffraction modes , including ; i)scanning microprobe (S tati on 1), ii) plane wave topography (Station 1 or 2) , iii)
USAXS usi ng Station 1 for sample and Station 2 for detector iv) full field
phase-contrast imaging [1 ,2] using both simp le projection from the sou rce as
we ll as an effective secondary source produced by a focusing device such as acompound refractive lens [4] as well as the double-crystal (DEl ) approach.

MONOCHROMATOR

SampleDetector
Full fi eld imaging (Large objects)
Pha se contrast imaging

Focusing device

References
I
Snigirev , A. , Snigireva , 1. , Kuznetsov, S., Schelokov, I. and Kohn , V.
(1995) Rev. Sci. lnstrum. 66 , 5486-92.
2
Wilkins , S. W ., Gureyev , T. E., Gao , D., Pogany, A. and Stevenson , A.W.
(1996) Nature 384, 335-8.
3
Forster, E., Goetz, K. and Zaumsei l, P. (1980) Krista// und Technik 15,
937-45 .
4
Snigirev, A. et al (1996) Nature 384, 49-51 . Snigireva , I. et al (2001) E.
Proc SPIE Vol 4499, 64-73.

256

ATuP-70
DIRECT OBSERVATION OF OXYGEN MOLECULES PHYSISORBED IN A
MICROPOROUS COORDINATION POLYMER
Yoshiki Kubota, a Masaki Takata,b,c Makoto Sakata ,b Ryo Kitaura ,d Ryotaro
Matsuda ,a Susumu Kitagawa ,d Tatsuo Kobayashi ," Kouichi Kindo ," Yoshimi
8Mita,1 Akira Matsuo, 8 Michihiro Kobayashi ,' Ho-Chol Chang ,d Tadashi Oszawa ,and Megumi Suzuki'
aDept. of Environmental Sciences , Osaka Women 's University, Osaka 5900035, Japan; bDept. of Applied Physics , Nagoya University; cJASRI/SPring-8;
dDept. of Synthetic Chemistry and Biological Chemistry, Kyoto University;
8
KYOKUGEN , 'Dept. of Physical Science, Osaka University, Japan(kubotay@center.osaka-wu.ac.jp)
Recently, various coordination polymers with uniform ordered nanochannels
were successfully synthesized by the combination of metal ions and organic
molecules. Many of these compounds are found to have extremely highperformance gas adsorption and are expected to be promising gas storage
materials. So far, adsorbed gas molecules were thought to be trapped in theordered nanochannels of the material. However, there is no structural evidence forthe trapped gas molecule position inside the micropore. Thus, in order to determine
the trapped gas molecule position and structure within the material, we have done
in-situ synchrotron radiation powder diffraction experiment and revealed theformation of a one-dimensional array of gas molecules along the nanochannels by
the MEM/Rietveld analysis.
The sample used in the present study is [Cu2(pzdc)2(pyz)]n (pzdc=pyrazine2,3-dicarboxylate, pyz=pyrazine), which has a pillared layer structure with onedimensional nanochannels with dimensions of about 4 x 6 A (CPL-1 :coordination
ploymer 1 with pillared layer structure) . The synchrotron powder diffraction data
was collected by the large Debye-Scherrer camera installed at SPring-8 BL02B2.
The powder sample was sealed in glass capillary. The gas import tube is attachedto the goniometer head to fill 0 2 gas in capillary. The gas adsorption is controlled
by lowering the temperature not by the gas pressure . The data measurement was
carried out from 300K to 90K under 80kPa 0 2 pressure. The fundamental crystal
structure of CPL-1 had been reported by single crystal X-ray structure analysis.
The powder diffraction pattern from 300K to 150K is almost the same with that of
the reported structure. However, we investigated the dramatic changes ofdiffraction pattern at 130K which should be due to the 0 2 molecule adsorption. In
the first Rietveld analysis of the 90K data, we started the analysis with thefundamental structure of CPL-1 without assuming 0 2 molecules. The reliability
factors based on the powder pattern, Rwp and the integrated intensities, R1were
18.5% and 54.2%, respectively. However, the MEM charge density visualized thedensity like 0 2 molecules in the middle of the nanochannels. According to the MEM
charge density, we determined the structure model of the CPL-1 adsorbing 0 2 gas
molecule. The Rwp and R1for the Rietveld analysis with the final structure model
were improved to be 2.1% and 3.9%, respectively. In the MEM charge density, thedumbbell shaped electron distribution was clearly observed in the middle of thenanochannels. The charge of the distribution was estimated to be almost 16e
indicating no charge transfer from the 0 2 molecule to CPL-1 , which means 0 2 gas
was physisorbed to CPL-1. And , we found adsorbed 0 2 molecules form onedimensional array along nanochannels. The details of the determined structure andnovel characteristic magnetic property caused by 0 2 adsorption will be presented.

257

ATuP-71
THE SELF-ASSEMBLED STRUCTURE OF A 2,6 DI(ACYLAMINO)PYRIDINE: FORMATION THROUGH N-H .... N and N-H ... O=C INTER
MOLECULAR INTERACTIONS
E. Marfo-Owusu and T. Kato
Department of Chemistry and Biotechnology, School of Engineering , The
University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-8656, Japan(emmanuel@chembio.t. u-tokyo.ac.jp)

The 2,6-di(acylamino)pyridines (hereafter, nAPys , where n = 1,2,3, .. . ,5)
form self-assembled structures through intermolecular hydrogen bonding
network. Knowledge of the hydrogen bond patterns associated with particulardonor and acceptor functional groups can be used to synthesize new functional
materials of interest. Presently , as part of an initial approach , our research teamis employing this concept to investigate the intermolecular hydrogen-bonded
network in the nAPys through X-ray single crystal diffraction studies; in order to
employ the knowledge to prepare supramolecular complexes of nAPys withalkoxybenzoic acids (hereafter , xOBA) and investigate the single crystal
complexes by X-ray diffraction studies. These complexes have potential
usefulness for generation of novel materials .
In the present study , we have examined the self assembled structures ofnAPys. It was observed that 3APy self assembles through N-H ... .N and NH ... O=C intermolecular interactions and forms a web-like pattern different fromthe other nAPys. Interestingly, N-H ... N interaction was observed only in 3APyand not in other nAPys. The structural studies revealed that the unique packing
modes of the rigid pyridine moiety and flexible alkyl chains contributesignificantly to the hydrogen bonded network observed in 3APy. In this poster
presentation , the self-assembled structure of 3APy will be exhibited.

258

Wednesday August 13

AsCA'03/Crystal-23

ABSTRACTS
ORAL SESSIONS

259

AWe1A-1
SYSTEMATIC APPROACHES FOR MEMBRANE PROTEIN STRUCTURE
DETERMINATION

Ben Hankamer." Rosalba Rothnagel ," Alasdair McDowall ," Geoff Ericksson ,bFrancis Clark ,6 Jasmine Banks ,b Bernard Pailthorpe ,b Charles Sennoga ,cAndrew Heron ,c John Seddon ,c Richard Templer,c and David Croutd
8

lnstitute of Molecular Bioscience , University of Queensland , St Lucia Campus,
Brisbane QLD 4072, Australia ; bAdvanced Computational Modelling Centre
University of Queensland , St Lucia Campus, Brisbane QLD 4072, Australia ;cDepartment of Chemistry , Imperial College London , London SW7 2AY , UK;
dDepartment of Chemistry , Warwi ck University, Coventry CV4 7AL , UK(b .hankamer@ic.ac.uk)

One of the great challenges of structural biology is to increase the rate ofproducing high-resolution structures of membrane proteins. Membrane proteins
form the responsive interface between the cell and the outside world andinclude specific receptors , signal transducers , channel forming proteins, active
transport pumps , electron transport systems and a wealth of other enzymes.
The current rate-limiting step in membrane protein structure determination ishigh quality 20 and 3D crystal production for electron and X-ray crystallography.
The development of new approaches for high-resolution structure determination
will be described. These in clude:1) Single particle analysis: Automation of the new NANO Cryo-EM facility.
2) 2D monolayer crystallization : Produ ction of synthetic lipids forcrystallization of His-tag proteins and glycoproteins3) 2D bilayer crystallization : Produ ction of large 2D crystals [eg. 1]4) 3D cubic phase crystallization : Development of systematic cubic phasecrystallization screens [2]References
I
Hankamer, B., Morris , E., Nield , J., Gerle, C. and Barber, J. (2001) ThreeDimensional Structure of the Photosystem II Core Dimer of Higher Plants
Determined by Electron Microscopy. J Struct Bio/135, 262-9.
2
Sennoga, C. , Heron, A., Seddon , J. M., Templer, R. H. and Hankamer, B.
(2003) Membrane-protein crystallization in cubo: temperature-dependent
phase behaviour of monoolein-detergent mixtures. Acta Crystallogr 0 Bioi
Crystallogr 59 , 239-46 .

260

AWe1A-2
STRUCTURAL CHANGES IN AN aJ' T-CELL RECEPTOR UPON LIGAND
BINDING

Craig S. Clements.8 Lars Kjer-Nielsen ,b Anthony W. Purcell ,b Andrew G.
Brooks ,b James C. Whisstock,a.c Scott R. Burrows ,d James McCiuskey,b andJamie Rossjohn a.c~he Protein Crystallography Unit Department of Biochemistry and Molecular

Biology School of Biomedical Sciences Monash University Clayton , Victoria ,3168, Australia
bDepartment of Microbiology & Immunology, University of Melbourne, Victori a,3010 , Australia ; cVictorian Bioinformatics Consortium , Monash University,
Clayton , Victoria , 3168 , Australia ; dQueensland Institute of Medical Research
The Bancroft Centre, Herston, Queensland , 4029 , Australia(craig.clements@med.monash .edu.au)

T-cell antigen receptors (TcRs) are heterodimeric cell-surface receptors
that play a pivotal role in the cellular immune response. The TcR interacts
specifically with a peptide-laden major histocompatability complex (pMHC) . A
human TcR has been characterized that interacts with an immunodominant
epitope, FLRGRAYGL , from the Epstein-Barr virus , a ubiquitous humanpathogen, in complex with HLA-B8. Despite the vast TcR repertoire , this TcR isfound in up to 10% of the total T-cell population in seropositive HLA-B8+
individuals. This highly selected TcR was characterized by expressing in E. coli,
refolding , purifying and crystallizing the receptor. In addition , the HLA-B8 has
been expressed in E. coli, refolded with the FLRGRAYGL peptide , and shown
to be functionally active . The TcR has been crystallized in complex with thispMHC. The crystals of the unliganded and liganded TcR diffract to 1.5 and 2.5
A respectively.
A comparison of the structures reveals that upon recognising antigen, theTcR undergoes extensive conformational changes in the complementarity
determining regions (CDRs) , including the disruption of the canonical structuresof the germ line-encoded CDR 1o: and CDR2o: loops to produce an enhanced fit
with the HLA-peptide complex . In addition , engagement of the TcR combiningsite induces conformational changes in the TcR o: constant domain thought toform part of the docking site for the TcR signaling molecule CD3 £. Thesefindings suggest a novel structural link between TcR ligation and intracellularsignaling . Further insight may be provided by the structure of the TcR bound toan HLA-B8/antagonist peptide complex.

261

AWe1A-3
A NEW MODE OF PORE ASSEMBLY BASED ON THE STRUCTURE OF
INTERMEDIL YSIN, A TOXIN SPECIFIC FOR HUMAN CELLSGalina Polekhina ," Rodney K. Tweten ,b and Michael W. Parker""St. Vincent's Institute of Medical Research , 9 Princes Street, Fitzroy, VIC 3065,
Australia; bDepartment of Microbiology and Immunology, The University ofOklahoma Health Sciences Center, Oklahoma City , Oklahoma 73104, USA(galinap@medstv.unimelb.edu.au)

The pore-forming cholesterol-dependent toxins have been identified innumerous species from five different genera of Gram-positive bacteria ,including Clostridium, Bacillus , Streptococcus , Listeria and Arcanobacterium [1] .
Their toxicity arises from the transition of a monomeric water-soluble form tolarge self-associated pores in the membrane of target cells. lntermedilysin (IL Y),
a toxin produced by Streptococcus intermedius , is of particular interest due toits exclusive specificity for human cells in contrast to other related toxins and its
role in deep-seated abscess formations in brain and liver [2]. Brain abscesses
may give rise to meningitis . It has also been shown that IL Y interacts with theprotein receptor on the target cells [3] unlike other toxins that only require thepresence of cholesterol in the target membrane.
We report the crystal structure of IL Y that has been determined by
combination of single isomorphous repla cement and multiple anomalous
dispersion techniques and has been refined to 2.3 A. The structure reveals a
profound bend to the rod-shaped molecule compared to the structure of therelated toxin from Clostridium perfringens, perfringolysin 0 (PFO). Based on the
structure of IL Y and the reported fluorescent studies performed on PFO [3] we
propose a new mode of pore assembly. We will offer an explanation as to why
certain ions are required for stability of IL Y and discuss the receptor specificity
based on comparison of the structures of IL Y and PFO .
References
I
Tweten , R. K. , Parker, M. W. and Johnson, A. E. (2002) Curr. Top.
Microbial. lmmunol. 257 , 15-33.
2
Nagamune, H. , Ohnishi , C., Katsuura , A. , Fushitani , K., Whiley , R. A. ,Tsuji, A. and Matsuda, Y. (1996) Infection and Immunity 64 , 3093-3100.
3
Ramachandran , R., Heuck, A . P., Tweten , R. K. and Johnson , A. E. (2002)
Nat. Struct. Bioi. 9, 823-827.

262

AWe1A-4
HIGH-THROUGHPUT PROTEIN STRUCTURE VALIDATION ALSO FORINTEGRAL MEMBRANE PROTEINS

W. Brei Church ,"·b and Lawrence K. Leeb
8

Molecular Biotechnology Program ; bSchool of Molecular and Microbial
Biosciences G08, University of Sydney, NSW 2006 , Australia(b.church@biotech.usyd.edu.au)

Methods for the prediction of three-dimensional protein structures
advanced over the last decade , along with the methods to assess the model
validity . The Profiles-3D[1] method is suitable for assessing the validity ofstructures in soluble proteins and an adaptation allows its application inmembrane spanning regions[2] .
A program that implements and integrates both the adaptation as well as
the original Profiles-3D method has been developed . Both water-soluble regions
and membrane spanning regions as well as entire soluble and entire integral
membrane proteins can be assessed. An integrated method can assist in theelucidation of membrane spanning domain boundaries. The program
implements a novel high-speed method for calculating solvent accessible
surface area . This allows efficient analysis of structures and a dedicated tool
ha ndling multiple structures permits high-throughput assessment ofexperimental or other sets of generated structures. 800 structures from a nonredundant data set took less than 22 minutes on a 1.2GHz PC .
Ideally, in this method each residue in the correctly folded protein scores
highly. To implement the scoring scheme for such a methodology, a techniquethat analyses a data set of protein structures is required. The program is able touse its multiple structure handling capabilities to produce scatter plots
representing environments at locations in structures or amino acid types. These
analyses can assist to identify trends between different family groups , andinconsistencies between scores and correctly folded structures . The user canalso create customised probability-based scoring schemes.
The application is currently running on Intel windows-based PC . The
graphical user interface was created with the Microsoft foundation class library.
All parameters for a calculation are retrievable and the results viewed as
spreadsheets or charts as well as displayed on the three-dimensional structurewith the basic built-in molecular viewer.
References
I
Bowie , J.U ., Luthy, R. and Eisenberg , D. (1991) Science 253 , 164-170.
2
Dastmalchi, S. , Morris, M.B. and Church , W.B . (2001) Protein Sci. 10,
1529-1538.

263

AWe1A-5
CRYSTAL STRUCTURE OF PEA TOC34- A NOVEL GTPASE OF THE
CHLOROPLAST PROTEIN TRANSLOCON

Chwan-Deng Hsiao," Yuh-Ju Sun ,"·b Farhad Forouhar," and Hsou-min li 88lnstitute of Molecular Biology , Academia Sinica, Taipei , Taiwan 115, ROC;
blnstitute of Bioinformatics and Structural Biology, National Tsing Hua
University, Hsinchu, Taiwan 300 , ROC (mbhsiao@ccvax.sinica.edu.tw)

Toc34 , a 34-kDa integral membrane protein , is a member of the Toe(!ranslocon at the QUter-envelope membrane of ghloroplasts) complex thatassociates with precursor proteins during protein transport across thechloroplast outer membrane [1-3). Here we report the crystal structure of thecytosolic part of pea Toc34 complexed with GOP and Mg 2+ at 2.0 A resolution[4). In the crystal , the Toc34 molecules exist as dimers with features
resembling the ones found in a small GTPase complexed with a GTPase
activating protein (GAP). Gel-filtration , however, revealed that dimeric andmonomeric forms of Toc34 coexisted in phosphate saline buffer (pH 7.2)
solution. Mutation of Arg 128, an essential residue for dimerization , to alanine
led to the formation of only a monomeric form whose GTPase activity issignificantly reduced compared to that of the wild-type Toc34. These results
together with a number of structural features unique to Toc34 , suggest thateach monomer acts as a GAP on the other interacting monomer.
References
I
Kessler, F., Blobe\ , G., Patel , H. A. and Schnell , D. J. (1994) Science 266 ,1035-1039.
2
Seedorf, M., Waegemann , K. and Soil , J. (1995) Plant J. 7, 401-411.
3
Chen , D. and Schnell , D. J. (1997) J. Bioi. Chem. 272 , 6614-6620.
4
Sun , Y.J. , Forouhar, F., Li , H. M., Tu , S. L. , Yeh, Y. H. , Kao , S. , Shr, H. L. ,Chou , C. C. , Chen , C. , and Hsiao, C. D. (2002) Nature Struct. Bioi. 9, 95100.

264

AWe1B-1

CHARGE DENSITY STUDY OF AN IRON NITROSYL COMPLEX

Yu Wang ," and J. J. Leeb
aOepartment of Chemistry, National Taiwan University, Taipei, Taiwan ;bNational Synchrotron Radiation Research Center, Hsin-Chu, Taiwan(yuwang@xtal.ch.ntu.edu.tw)

Charge density and bond characterization have been investigated on an
Iron-nitrosyl dithiocarbamate complex , [Fe (NO)(S2CNC2H6)2] in terms ofaccurate single crystal diffraction at 1OOK and an open-shell OFT calculation.
The iron atom is five- coordinated with four sulfur and one nitrogen atoms in asquare pyramidal geometry, the site symmetry is roughly C2v. The iron atom is0.6261 (1) A above the plane of four sulfur atoms , the nitrosyl group (NO) is in
the axial direction perpendicular to the plane. Unfortunately, the oxygen atom
exhibits positional disorder.
The complex is related to a potential free radical scavenger, this study
may shine some light on how it is so via electron density distribution, especiallyat the iron site and at the NO group. It is known that NO ligand could be served
as a radical neutral species or NO+, a nitrosyl, or NO-, a nitroxide group. Thus
the unpaired electron can be located either at Fe or at the NO group. According
to the electron density distribution based on the multipole model and on the
OFT calculation , the electronic configuration of iron atom is 4s13d6, therefore a
Fe 1 and NO+ ligand is a nitrosyl group. In other words , the unpaired electron ismostly localized at Fe not on the NO ligand, which is consistent with theconclusion made from single crystal EPR and Moessbauer measurements.
Topological analysis on the total electron density will give the bondcharacterization in terms of topological properties associated with bond criticalpoints. The VSCC of Fe in this five coordinated complex is quite interesting, thedetail description and its correlation to the metal ligand bond will be presented .

265

AWe1B-2

FINDING HYDROGEN BY SYNCHROTRON POWDER DIFFRACTION

Makoto Sakata, a Hitomi Sakai ,a Eiji Nishibori ,a and Masaki Takataa.b
aDepartment of Applied Physics , Nagoya University, Chikusa , Nagoya 4648603 , Japan ; b Japan Synchrotron Research Institute, Kouto , Mikazuki-cho ,Sayo-gun, Hyougo 679-5198 , Japan (sakata@cc.nagoya-u .ac.jp)
It is not well established whether hydrogen can be detected by X-ray
diffraction. Most work relating to finding hydrogen by X-rays is carried out using
least squares refinement, which relies on only the R-factor by introducing atomic
scattering factors of hydrogen. It is reasonable to expect that the nature ofchemical bonding nature to hydrogen in different crystals would vary considerably.
Therefore , in a rigorous sense, it may not be justified to use an atomic scatteringfactor for hydrogen in the least squares refinement. In the case of Cytidine(CgH13N30 5) , for example , atomic positions determined by various authors agreed
very well except for hydrogen[1].
Recently, a sophisticated analytical method , which is called imaging ofdiffraction data by the Maximum Entropy Method (MEM)[2], has been successfully
applied to find hydrogen in crystals[3] . MEM does not require atomic scatteringfactors of any atoms. The previously analysed materials are basically ionic crystals,
which should not be extremely difficult to analyse. In this work, we determinedcharge density distributions of hydrogen in two organic crystals - cytidine(CgH13N305 ) and monosodium L-glutamate monohydrate (C 5 H8 N04NaH 20 ) byanalysing synchrotron powder data , collected using the large Debye-Scherrer
camera installed at BL02B2, Spring-S. For cytidine, both RT and low temperature(100K) data have been analysed. It was found that finding charge densities ofhydrogen in MEM maps is much easier using low temperature data. For the Lglutamate, therefore, only low temperature (92K) data were analysed.
From the MEM charge density map obtained in this study, we found that:firstly all the charge density of hydrogen can be detected in MEM maps without any
ambiguities; secondly charge densities of hydrogen bonds are similar to weakcovalent bond ; thirdly non-hydrogen bond H shows a lobe shape charge density
distribution; fourthly in cytidine, no local maxima is found for the charge density ofhydrogen even at low temperature, while in the L-glutamate case , local maxima
are very clearly seen . In addition to these results , very interesting charge densities
of hydrogen are found for a hydrate water molecule, which does not show slightest
sign of lobe shape charge density distribution. This strongly suggests that watermolecules of hydrate are in disordered states occupying quite a few
crystallographic sites.
References
I
Furberg , S. (1950) Acta Cryst. 3, 325; Furberg , S. , Petersen , C. S. and
R0mming, C. (1965) Acta Cryst. 18, 313; Ward , D. L. (1993) Acta Cryst.
C49, 1789-92; Chen , L. and Craven , B. M. (1995) Acta Cryst. 851 , 1081-97.
2
Sakata, M. and Sato, M. (1990) Acta Cryst. A46, 263-70.
3For example, Noritake, T., Aoki, M. , Towata , S. , Seno, Y. , Hirose, Y. ,Nishibori, E., Takata , M. and Sakata , M. (2002) App. Phys. Lett. 81 , 200810.

266

AWe18-3
CHARGE DENSITY STUDIES OF POLYMORPHIC ANTI-ULCER AGENTS.
THE APPLICABILITY OF THE ELECTROSTATIC POTENTIAL IN DRUG
DESIGN

Jacob Overgaard , Mark P. Waller, and David E. Hibbs
School of Chemistry , University of Sydney , NSW 2006 , Australia
Uacobo@chem .usyd.edu.au)
The electrostatic potential (EP) has been extensively employed in theprediction of a variety of condensed phase macroscopic properties fromtheoretical calculations , and a quantitative approach has recently beensuggested based on a range of features of the EP on the molecular surface [1].
However, this method has so far been restricted to the gas-phase , thus
excluding the effect of intermolecular interactions. Nonetheless, the EP is ofparamount importance in the understanding of drug-receptor interactions. Thus,
an experimental determination of the EP including the effects of intermolecularinteractions is potentially of great use in rational drug design.
In the present work we will outline the results of a theoretical andexperimental charge density (CD) study of both known polymorphs (A and B) of
the histamine H2-receptor antagonist , famotidine (see Figure) [2] . The CD isdetermined from a combination of X-ray and neutron diffraction data collected at
100 K, using the Hansen-Coppens multipole model [3] . We will focus on acomparison of the experimental and theoretical COs and describe thesimilarities in the COs of the two polymorphic forms of famotidine . In particular,
we will discuss the observed differences in the experimental EPs of the twopolymorphs , respectively, in relation to their individual abilities to act as antiulcer agents. This work represents the preliminary steps towards a moregeneral description of a number of drug types using combined theoretical andexperimental charge density studies.

0-.::.~9\0C7- - - !Ns

/
-~N6

\

~0. 20,<J-- _.-li:j019 JS\7

\
CZ

N18

c~~-,.-'J0.........
, .• N>

N 16

51 /

'-

. .....

'-/c~ ~

C5/

6
Famotidine B

s1 1? N 15/~/c"

6 0-._\_ ~3
dC12 bFamotidine A

References :I
Politzer, P. , Murray, J. S. (2002) Theor. Chem. Ace. 108, 134-142.
2
Ferenczy, G. G., Parkanyi , L. J. , Angyan, G., Kalman , A. , Hegedus, B.
(2000) J. Mol. Struct. (Theochem) 503 , 73-79 .
3
Hansen, N. K., Coppens, P. (1979) Acta Crystallogr. Sect. A 39 , 909-921 .

267

AWe1B-4
ELECTRON DENSITY DISTRIBUTIONS ON WEAK INTERMOLECULAR
INTERACTIONS - BR··BR INTERACTIONS

Masanori Yasui ," Kouki Tamakawa ,8 Fujiko lwasaki ,8 and Daisuke Hashizumeb
0epartment of Applied Physics and Chemistry, The University of ElectroCommunications , Chofu , Tokyo 182-8585, Japan; ~he Institute of Physicaland Chemical Research (RIKEN) , Wako, Saitama 351-0198, Japan(yasui@pc.uec.ac.jp)

8Intermolecular halogen-halogen contacts of which interatomic distances
are shorter than the normal van der Waals contact are incorporated frequently
in organic crystal structures . The geometrical features of Br .. ·Br contacts show
anisotropic characters from the CSD retrieval. In this paper, the topologicalana lyses of the experimental electron density distributions of intermolecular
Br .. ·Br contacts are carried out to establish the nature of this type of interaction.
Crystals of 4-bromobenzamide show two modifications , one of which , aform , has structures with linear C-Br .. ·Br contacts (C-Br .. -Br=166°,
Br .. ·Br=3.49A) and another one , ~-form , has bent C-Br .. ·Br contacts (CBr .. ·Br=920, Br .. ·Br= 3.64A). X-ray diffraction data of these modifications werecollected at the SPring-S BL04B2 beam-line with wavelength of 0.3282A upto
sinS/A. of 1.02A·1 at 100K. The aspherical-atom refinements based on F 2 werecarried out using the XD package[1] and converged with R1(F)=0 .026 (5219
reflns. with 1>1.5o(/)) and R 1(F)=0.022 (5879 reflns .
with 1>1.5o(/)) for a - and ~ -form , respectively. Fig .1
Brshows the Laplacian maps of a - and ~-for m on theplane of the C-Br .. ·Br. The topological parameters at
the BCP of Br .. -Br interactions and intermolecular
NH .. ·O hydrogen bonds are summarized in Table 1.
Br
From these results, the Br .. ·Br interactions area -form.
revealed to be an electro-static interaction
corresponding to the dispersion force. Th e magnitudeof Br .. ·Br interactions can be estimated abou t a half of
those of the NH .. ·O hydrogen bonds according to thedissociation energy, Ecp. after Abramov[2].
Br

~'f.

Table 1 Topological parameters1p (eA" 3) V2p (eA-5 ) Ecp (kJmol- )--~ ·-·Br .. Br~-form··············-·-··

Fig . 1 Laplacia n maps on
the plane of C-Br .. ·Br

a-form(l-form

0.085
0.079

0.9 130.747-11 .1-7 .94

NH .. ·O (averaged va lue)
2.82
a-form
0.12~ -form
0.14
2.50-22 .0-22.9

References
I
Koritsanszky, T., Howard, S. T., Su, Z. , Mallinson , P. R. , Richter, T., andHansen , N. K. (1999) XD , Computer Program Package for Multipole
Refinement and Analysis of Electron Densities from Diffraction Data, Free
University of Berlin , Berlin , Germany.
2
Abramov, Y. A. , (1997) Acta Cryst. A53 , 264-272.

268

AWe18-5
CHARGE DENSITY ANALYSIS AND DIPOLE MOMENT ENHANCEMENT IN
MNA (2-METHYL-4-NITROANILINE)

Andrew Whitten ," Mark Spackman ," Peter Turner,b Wim Klooster,c Ross Piltz,cand Masaru Tachibanad
8

Chemistry , School of Biological , Biomedical and Molecular Sciences ,University of New England , Armidale , NSW 2351 , Australia ; bSchool ofChemistry, University of Sydney, NSW 2006 , Australia; cBragg Institute,
Building 58, ANSTO , PMB 1, Menai, NSW 2234 , Australia; dDepartment of
Physics , Yokohama City University, 22-2 , Seta , Kanazawa-ku , Yokohama , 2360027 , Japan (awhitten@une .edu .au)

MNA belongs to a class of substituted benzene derivatives, which possess
exceptional non-linear optical properties. Such compounds exhibit large
microscopic second order non-linear susceptibilities, and lack a centre ofsymmetry in the solid state. Another interesting property of these compounds isthe apparent enhancement of the dipole moment due to hydrogen bonding andgeneral crystal-field effects. For MNA, ab initio calculations of the free molecule
give values of the dipole moment of about 8.2 0, 111 while in-crystal estimatesobtained from a previous charge density analysis are around 25(8) 0, 121suggesting a three-fold enhancement of this molecular property . This
experimental result has been widely cited , but whether the magnitude of thedipole moment enhancement exhibited there is reasonable is of some debate
because of difficulties encountered in the analysis of X-ray diffraction data for
non-centrosymmetric space groups ; the large experimental error associatedwith the value also raises questions about the ability of the multipole refinement
procedure to reliably retrieve such values.
To independently verify this important observation , and hopefully to
improve on the results obtained in the previous study, we are making use ofexperimental data that was unavailable a decade ago , including neutron
diffraction data collected on the four-circle diffractometer (2TANA) at HIFAR, as
well as charge density quality. X-ray diffraction data collected on the Bruker
SMART 1000 CCD system at the University of Sydney, all at 100 K. We arealso performing Hartree-Fock CRYSTAL98 calculations to aid in the analysis of
the experimental data , and for comparison with experimental results . We will
discuss the difficulty in obtaining sensible estimates of one-electron properties
for non-centrosymmetric compounds from multipole refinements , and present indetail the results obtained from this study.
References
I
Daniel , C. and Dupuis , M. ( 1990) Chem. Phys. Lett. 171 , 209 .
2
Howard, S.T., Hursthouse, M.B., Lehmann, C.W. , Mallinson, P.R. , andFrampton, C.S. (1992) J. Chem. Phys 97, 5616 .

269

AWe2A-1
HOW DO TRANSLATION FACTORS CATALYSE PROTEIN SYNTHESIS?
Anders Liljas
Molecular Biophysics , Lund University, Lund, Sweden(anders.liljas@mbfys .lu .se)!RNA is the adaptor in protein synthesis . The ribosome has three bindingsites for !RNA, the A-, P- , and E-sites . The tRNAs bridge between the ribosomal
subunits with the decoding site and the mRNA on the 30S subunit and the
peptidyl transfer site on the 50S subunit.
Translation factors are needed to obtain the rate and fidelity required forprotein synthesis. They catalyse protein synthesis on the ribosome. Several of
the translation factors are GTPases and are structurally and functionally related.
They catalyse irreversible steps in the process. Other translation factors operate
in conjunction with the GTPases. Several of them bind to the !RNA binding sites
on the ribosome and some of them are also !RNA mimics. Some of these !RNA
mimics are EF-G, EF-P, SeiB , RF1 , RF2 and RRF. The range of !RNA
mimicking proteins suggest that the shape similarity is not a sufficient criterion
for binding to a !RNA binding site. Despite a !RNA similarity some factors binddifferently to the ribosome from the tRNAs.
The GTP hydrolysis of the translational GTPases leads to an irreversible
step forward in the translation process . The GTPasesare normally inactive
enzymes, but at suitable states the ribosome activates their inherent capacity tohydrolyse GTP. This is done by a protein complex (L 1O*L124) whose structureand function is slowly becoming understood .

270

AWe2A-2
EVOLUTION OF AN ORGANOPHOSPHATE DEGRADING ENZYME; A
COMPARISON OF NATURAL AND DIRECTED EVOLUTION
P. D. Carr," H. Yang ," S. Yu Mcloughlin,• J. W. Liu ,8 I. Horne,b X. Qiu ,b R. J .
Russell ,b J . G. Oakeshott,b and D. L. Ollis""Research School of Chemistry, Australian National University, GPO Box 414 ,Canberra , ACT 2601 , Australia ; bCSIRO Entomology, Canberra , ACT 2601 ,Australia (pdc@rsc.anu .edu .au)

Organophosphates (OPs) are widely used pesticides both in Australia andglobally . The build up of these chemicals in irrigation run-off leads to major
environmental management issues . Bioremediation of water contaminated withhigh levels of OPs by use of enzymes overexpressed in bacteria is an attractive
solution to the problem .
We present the X-ray structure of an organophosphate degrading enzyme
from Agrobacterium radiobacter (OPDA) , isolated from contaminated soils
located in a cotton farming region of Australia . This structure is compared toanother known organophosphate degrading enzyme (OPD) isolated in the USA
from Pseudomonus bacterium . These enzymes have differing but overlapping
substrate specificities .
In vitro directed evolution experiments were used to evolve a series of
OPD mutants that had activities similar to OPDA. These mutations tended tocluster in particular regions of the protein which , in most cases , were regions
where sequence differences exist between the two proteins. We attempt to
explain in structural terms the significance of these regions .

271

AWe2A-3
CRYSTAL STRUCTURE OF GLUTAMATE-CYSTEINE LIGASE FROMESCHERIHIA COLI B WITH SUBSTRATES

T. Hibi , M. Nakayama, H. Nii, and J. Oda
Department of Biochemistry, University of Fukui Prefectural University, Fukui
910-1195, Japan (hibi@fpu.ac.jp)

Glutamate-cysteine ligase catalyzes the ATP-dependent coupling of Lglutamate and L-cysteine to form a glutathione precursor y-glutamylcysteine. It
is the rate-limiting enzyme in glutathione biosynthesis , and the cellular level ofglutathione is controlled through the negative feed-back inhibition of GCS byglutathione. GCS is one of targets of potential therapeutic agents such as aparasiticide or a drug suppressing multi-drug resistance of cancer cells.
The GCS used in this study has been isolated from E. coli B[1] . This
procaryotic enzyme is a single polypeptide with molecular mass of 58,300 ,unlike the eucaryotic enzymes composed of two nonidentical subunits.
However, E. coli and rat kidney GCS not only show similar kinetic parameters
Theand substrate specificity but also are inhibited by glutathione[2].
crystallographic analysis of E. coli enzymes will elucidate the mechanism of
catalysis and the basis for feed-back inhibition and provide a framework forstructure-assisted drug design for any species of GCS. We report the
crystallization and structure analysis of the GCS from E. coli B and its complex
with cysteine and ATP.
Unliganded crystals of GCS were obtained as described before[3], andcomplex ones were crystallized in the presence with 1 mM ATP and 5 mM Lcysteine using sodium formate as a precipitant. X-ray diffraction data of thecrystal were collected at the beamline BL40B2 or BL38B1 (SPring-8 , Harima ,Japan). Both the crystals were found to index in rhombic lattices corresponding
to space group R3 with unit-cell parameters a=b=326.74, c=103.96 A and
a=b=326.72 , c=105 .01 A, respectively. The data of unliganded crystal were
99.8% complete to 2.8 A resolution , and that of complex crystal were 98.9%
complete to 2.8 A resolution . The unliganded crystals of the selenomethionine
substituted enzyme were used for the MAD experiments at the beamline
BL41XU , collecting three data sets at different wavelength to 3.0 A resolution.
Structure determination is on going and will be presented at this meeting.
References
I
Watanabe, K., Yamano , Y., Murata , K. and Kimura, A. (1986) Nuc. Acids
Res. 14, 4393-4400.
2
Huang, C.-S ., Moore , W. R. and Meister, A. (1988) Proc. Nat/. Acad. Sci.
USA 85 , 2464-2468.
3
Hibi, T., Hisada, H. , Nakatsu , T. , Kato, H. and Oda , J. (2002) Acta
Crystallogr. 058 , 316-318 .

272

AWe2A-4
CRYSTALLOGRAPHIC ANALYSIS OF THE MECHANISM OF HMG-CoA
REDUCTASE

Cynthia V. Stauffacher," Nicklaus Steussy," John W. Burgner," Tim Schmidt,"
and Victor W. Rodwellb•oepartment of Biological Sciences and bDepartment of Biochemistry, Purdue
University, West Lafayette, Indiana 47907, U.S.A.
(cyndy@gauguin .bio .purdue .edu)

HMG-CoA reductase (HMGR) catalyzes the first committed step in theisoprenoid biosynthesis pathway that in mammals leads to the r:>rodu ction ofcholesterol. A highly related enzyme is found in gram-positive pathogenic
bacteria , and has been shown to be essential for normal bacterial growth.
HMGR is a four electron oxidoreductase , using two molecules of NADPH toconvert HMG-CoA to mevalonate. HMGR is the target of the highly effective
stalin drugs, which mimic the substrate and block the active site pocket inboth the classes of the enzyme [1 ,2].
We have been studying the structure and mechanism of the bacterial
HMG-CoA reductase in crystals which both diffract to high resolution andallow the enzyme to catalyze the reaction . Large channels through the crystal
allow diffusion of substrates and the closing of a 50 residue flap over theactive site during catalysis [3] . Using a slow substrate, dithioHMG-CoA, wehave been able to capture a series of catalytic steps in the HMGR
mechanism , including an initial "relaxed " binding state for HMG-CoA, theconverted "strained" state just before CoA is released and the thiohemiacetalintermediate. These experiments have suggested an explanation why thealdehyde intermediate is not observed in the reaction , as well as an analysisof the stopped-flow kinetics results. Time and exposure experiments indicatethat the thioester bond of the substrate is susceptible to breakage in thesynchrotron beam , resulting in rearrangement of the substrate in the active
site . Initial experiments are also being done to establish the feasibility of atime-resolved x-ray analysis of the HMGR mechanism and the inhibition withstalin drugs.
References
Istvan , E. S. and Deisenhofer, J. (2001) Science 292, 1160-1164.
I
Tabernero, L. , Rodwell , V. W. and Stauffacher, C. V. (2003) J. Bioi.
2
Chern .. epub Mar03 213006200 .
Tabernero, L., Bachar, D. A., Rodwell , V. W. and Stauffacher, C. V.
3(1999) PNAS. 96 , 7167-7171 .

273

AWe2A-5
STRUCTURE AND SIGNALING IN THE EPIDERMAL GROWTH FACTOR
RECEPTOR FAMILY
T. P. J. Garrett." M-Z Lou ," N. M. McKern,b T. E. Adams,b G. 0 . Lovrecz,b R. N.
Jorissen ,c E. C. Nice,c A.W. Burgess,c and C. W. Ward 2"Walter and Eliza Hall Institute; bCSIRO Division of Health Science andNutrition; cludwig Institute for Cancer Research , Parkville, Victoria 3050 ,Australia (tgarrett@wehi.edu .au)

Epidermal growth factor receptor (EGFR) is the cell surface receptor for
EGF , a small polypeptide cytokine that stimulates proliferation in a wide variety
of epithelial tissues . Upon the binding ligand outside the cell , receptors dimerise
into a novel 2:2 complex which then initiates intracellular signaling via
cytoplasmic tyrosine kinase domains. The EGFR family contains three otherreceptors , erbB2 (neu or HER-2), erbB3 and erbB4, with each member having
its own identity. For example , erbB2 has no ligand and the erbB3 kinase isinactive. Thus hetero- as well as homo-dimerisation is important in this complex
signaling network.
Medically, increased or aberrant signaling via these receptors ischaracteristic of many cancers . For example, elevated levels of receptor or
ligand have been observed in tumours of the brain , head and neck , lung,pancreas and colon. Furthermore, antibodies to EGFR have been shown to
inhibit growth of epithelial cell lines in the laboratory and an antibody to erbB2 iscurrently in clinical trials as a therapy for breast cancer
We have determined the structures of complexed and uncomplexed
members of the EGFR family at near atomic resolution and these structures
show that the receptors undergo a surprisingly large conformational change
upon ligand binding. The structure of erbB2 also shows why it does not bind
ligand and , indeed, why it does not need to. Unlike its relatives, it exists in a
pre-activated state, ready to interact with potential partners. Closer comparisonsof the receptor structures also reveal some more subtle differences. Twists andbends in the dimerisation domains of up to 40" hint that different ligands may
have some fine specificity in receptor signaling .
Thus , structures of these receptor fragments provide substantial insight
into the extracellular events leading to mitogenesis signaling via members of the
EGFR family. However they also raise questions about the details of these
events. A number of follow-up experiments have confirmed our initial
hypotheses and results will be presented about a more detailed understandingof how EGFR family members interact.

274

AWe2B-1
SYNCHROTRON X-RAY AND MOLECULAR DYNAMICS STUDIES OF
La2.xSrxCU04 WITH x! 1/8
Nobuo lshizawa , Kenji Suzuki, Katsumi Suda , and Douglas du Boulay
Materials and Structures Laboratory, Tokyo Institute of Technology, 4259
Nagatsuta Midori, Yokohama 226-8503 Japan (nishizaw@n.cc.titech .ac.jp)

Although the tetragonal-orthorhombic structural phase transition in the
La 2-xSrxCu04 high Tc super conductors has been studied and discussed
extensively since their discovery, there is still some mystery about the role
played by the Sr dopant in the phase transition mechanism . In our study, theelectron density distribution of La2-xSrxCU04 with x! 1/8 determined at 297K
using single-crystal synchrotron X-ray diffraction revealed not only the d x2-y2
orbital hole of Cu but also the disordered nature of the La(Sr) and 0
constituents , even though the crystal exhibits the archetypal K2NiF 4 structurewith tetragonal 14/mmm symmetry.
Molecular dynamics (MD) calculations were applied to examine thestructural disorder in more detail. By averaging related atomic positions acrossthe MD unit cell and across all MD time steps, calculated at 2fs intervals, the Sr
and La atoms were found to vibrate harmonically about slightly displaced mean
atomic coordinates, with Sr displaced by 0.02A along the c axis with respect to
La . In addition, four in-plane 02 atoms localized around Sr were typicallydisplaced by a mean of 0.15A furtherzalong < 11 0> vectors , and the closest
apical 02 atom by 0.08A along <001>, inorder to accommodate larger radii Srcations , as shown in the figure . The
directions of these 0 atom displacements
are incompatible with those that facilitate
01
01
Cu
Cu
the collective tilting mechanism of theCu01 402 2 octahedra in the lowtemperature orthorhombic form . The local
steric hindrance identified around Sr
probably impedes the cooperative02
deformation of the octahedral sheet and02
helps to explain the experimentallyobserved decrease in tetragonaltransition
phase
orthorhombic
temperature with increasing Sr content in
01
La2.xSrxCU04 .
01
Analysis of the mean La atom
01
01
positions in the MD study indicates that
their equilibrium positions are slightly
displaced along <11 0> from their ideal
positions on the c axis, indicating thateven in the tetragonal archetypal phase they favour a locally orthorhombic
distortion.

275

AWe2B-2
CORRELATION OF METAPRISM TWIST ANGLE WITH DISEQUILIBRIUM IN
CALCIUM-LEAD FLUORO-VANADINITE APATITES

Z.L. Dong and T.J.White
Centre for Advance Research of Ecomaterials , Institute of Environmental
Science and Engineering , Innovation Centre , Blk 2, Unit 237 , Nanyang
Technological University, Singapore 637723 (zldong@ntu.edu.sg)

The synthetic vanadinites (PbxCa 10.x)(V04)6 (F 2. 2yOy). O<x<9 and O<y<0.35
adopt the P6:fm apatite structure with 9.7073(4) ~ a ~ 10.1179(1) A and7.0153(3) ~ c ~7.4021(1) A. For mixed metal compounds (x 1 0) the partitioningof ca lci um and lead over the A 1(4f) and A 11 (6h) positions is nonstoichiometricwith lead preferentially sequestering to the larger A 11 site , as determined throughthe refinement of powder X-ray diffraction data . High resolution electron
microscopy , supported by multislice ca lculations , revealed that samples
annealed for 10 hrs at 800°C show great disparity in Ca/Pb partitioning , withdomains that are essentially calcium or lead pure co-existing at unit cell scales.
Only longer sintering in excess of 2 weeks enabled the metals to ordermacroscopically. As annealing progresses the lattice parameters adjust firstthrough dilation of a (within 1 week) followed by c contraction (between 1 - 2
weeks) . The A10 6 metaprism twist angle <1> is a sensitive measure of
disequilibrium and can be used to derive ideal cell parameters from triangularanion networks such thata =t

1 3-28sin ' (~)+l6 sin ' (~)

where t = 2.729 + 0.017x is the triangle edge , h 9=o = 3.576 + 0.017x is themetaprism height at <1> = 0°, and x is the stoichiometry in (PbxCa 10.x)(V0 4)6 (F 2.
2y0y).

276

AWe28-3
NEGATIVE THERMAL EXPANSION IN CYANIDE-BRIDGED
COORDINATION FRAMEWORK MATERIALS

Karena W. Chapman , Andrew L. Goodwin, and Cameron J. Kepert
School of Chemistry , University of Sydney , NSW 2006 , Australia(chapmank@chem .usyd.edu .au)

The current interest in coordination framework materials derives from thewide range of possible functionalities that can be achieved and the exciting
potential to tailor these properties towards specific applications throughsystematic variation of metal ion , ligand and included guest species . Reported
functionalities have included those of a photochemical , mechanical , optical ,electronic and magnetic nature, allowing applications in selective sorption ,catalysis, sensing , switching and data storage .
We have synthesised and characterised a versatile family of
cyanidebridged coordination framework materials that display negative thermal
expansion (NTE) behaviour: contracting upon heating. These have diverse
potential applications in high precision and low thermal shock materials (in zerothermal expansion composites) where the positive thermal expansion exhibitedby the vast majority of materials may be a hindrance.
The thermal expansion in these frameworks have been monitored withvariable temperature single crystal and synchrotron powder x-ray diffraction ,6 1
recording coefficients of thermal expansion (a = d /dT) up to 21 x 10 K ,more than twice that of the previous record held by zirconium tungstate.
This NTE behaviour arises from a contraction of M ... M· distances due tothe increased amplitude of M-CN-M ' transverse vibrations at high temperature .
This is crystallographically evident in the atomic displacement parameters of thecyanide ligand perpendicular to the M ... M· axis as shown in the single crystal
structural models and powder neutron diffraction.

277

AWe2B-4

PHASE TRANSITION AND STRUCTURAL CHANGE OF TRICALCIUM
PHOSPHATE AT HIGH TEMPERATURES UP TO 1900 K
Masatomo Yashima ," Atsushi Sakai ," Keisuke Yamamoto,8 Yoshisato Kimura, 8
Yoshinao Mishima,8 Masahiko Tanaka ,b Takeharu Mori ,b Kenji Ohoyama,c andYasuo Yamaguchic
8

Department of Materials Science and Engineering , Tokyo Institute ofTechnology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, 226-8502, Japan;
bPhoton Factory, Institute of Materials Structure Science, High Energy
Accelerator Research Organization , 1-1 Oho, Tsukuba , lbaraki, 305-0801,
Japan; clnstitute for Materials Research , Tohoku University, Katahira 2-1-1 ,Aoba-ku , Sendai, 980-8577, Japan (yashima@materia .titech .ac.jp).

Tricalcium phosphates [TCPs: Ca 3(P04)2] have been of considerable
interest to biologists , mineralogists , and inorganic and industrial chemists,
because the TCPs are some of the most important biomaterials as is apatite .
The crystal structure-property correlation is one of the most important topics incurrent science and technology [1] . However, for the TCP materials it has been
insufficiently understood and studied , probably due to their complicated crystal
structures. In this study, we investigated the a-a' phase transition of TCP using
high-temperature powder neutron and synchrotron diffraction and differential
thermal analysis (DTA) . High-purity a-TCP was prepared by solid-state
reactions from CaHP04 and CaC0 3 . To investigate the temperaturedependence of the crystal structure of TCP , neutron powder diffraction
experiments were carried out at high temperatures in air with a 150-detector
system , HERMES, installed in the JRR-3M reactor at the Japan Atomic Energy
Research Institute, Tokai , Japan . A furnace with MoSi2 heaters was placed on
the sample table , and used for the neutron diffraction measurements at hightemperatures [1] . The unit-cell and structural parameters of the TCP wererefined by Rietveld analysis, using the RIETAN-2000 computer program . Highresolution synchrotron powder diffraction experiments were carried out for thea'-TCP at beam line 3A in the Photon Factory to confirm the space group at
1577 Celsius degree. DT A measurements were also done to determine theprecise transition points and transition entropy . The a -a' transition occurs
between 1458 and 1508 Celsius degree. Hysteresis is not observed between
heating and cooling within the observed temperature interval of 25 Celsius
degrees. Structural refinement of the a'-TCP was successfully performed by thetrigonal structure with space group P3m . The temperature dependence of unitcell parameters of the TCP was determined around the a -a' phase transition
point for the first time. At the a-a' phase transition point, the unit-cell parametersa , c, y angle , and unit-cell volume discontinuously changed , indicating that thetransition is of first order.
References
I
Yashima, M., (2002) J. Am. Ceram. Soc. 85, 2925-2930.

278

AWe2B-5
IN-SITU STRUCTURE SOLUTION AND PHASE TRANFORMATION STUDIESOF DRUG POL YMORPHS USING HIGH RESOLUTION SYNCHROTRONPOWDER DIFFRACTIONW I F David and K Shankland
ISIS Facility, Rutherford Appleton Laboratory, Chilton , Oxfordshire , OX11 OQX ,UK (Biii.David@rl.ac.uk)

With third generation synchrotron powder diffractometers, it is possible tocollect high resolution diffraction patterns on 50-100 atom structures in a matterof minutes. This enables the rapid scanning of temperature to monitor structuralphase transformations and search for new drug polymorphs . We show that it ispossible to study the effects of dehydration and to discover new polymorphic
form s as a matter of routine. The technique is essentially the structural
equivalent of a combination of differential scanning calorimetry and thermogravimetric analysis. Three examples will be illustrated that show (i) the subtle
effects that occur with the transformation from a hemihydrate to an anhydrous
form , (ii) the detailed characterisation of a drug polymorphic phasetransformation and (iii) the discovery and crystal structure solution of a new
crystal polymorph .

279

PL-5
THE ROLE OF NON-MEROHEDRAL TWINNING IN SOME PHASE
TRANSITIONS
Victor G. Young, Jr. ," Maren Pink,b Neil R. Brooks ,c and William Brennessella
8

Chemistry Department, University of Minnesota , 207 Pleasant St. S.E .,Minneapolis , Minnesota 55455 , USA; biUMSC , Chemistry Department, Indiana
University, Chemistry Building A421 , 800 E. Kirkwood Ave., Bloomington ,Indiana 47405-7102 ; cSchool of Natural Sciences , Bedson Building , Universityof Newcstle upon Tyne , NewCastle upon Tyne NE1 7RU , United Kingdom(young@chemsun .chem .umn.edu)

We have found numerous examples of materials where the twinning is so
intimate that no single twin component can be separated from the other in orderto pursue a normal single-crystal , crystallographic investigation . Some of thesematerials are single crystals at one temperature, but exhibit phase changes
associated with the onset of non-merohedral twinning at either lower [1-4] orhigher [5] temperatures. A number of these examples will be presented anddiscussed . The interface between twin components, or composition planes , areof particular interest, because the memory of the symmetry lost in the phaseNon-merohedral twins pose certaintransition is retained within these .
problems not experienced by single crystals or even merohedral twins. Asidefrom the obvious problem of indexing the reciprocal lattices of competing twin
components, non-merohedral twins pose a more serious problem in theacquisition of accurate intensities from interfering reflections . The attribute ofpartially overlapped reflections acquired from non-merohedral twins has been asignificant challenge for crystallographi c programmers. However, recent
advances in software now provide all the basic tools to index, integrate , andrefine data acquired from non-merohedral twins.

References
I
Jazdzewski , B. A. , Holland , P. L. , Pink , M ., Young , Jr., V. G., Spencer, D.
J. E. and Tolman , W. B. (2001) lnorg. Chem. 40 , 6097 .
2
Reger, D . L. , Little , C. A. , Young , Jr. , V. G. and Pink, M. (2001) lnorg.
Chem. 40 , 2870.
3
Colombo, D. G., Young , Jr., V. G. and Gladfelter, W . L. (2000) lnorg.
Chem. 39 , 4621 .
4Schweitzer, J. W., Martinson , L. S. , Baenziger, N. C. , Swenson , D. C. ,Young , Jr. , V. G. and Guzei , I. (2000) Phys. Rev. 862, 12792.
Choe , W. , Pecharsky , V. K., Pecharsky, A. 0 ., Gschneidner, K. A. , Young ,5Jr., V. G . and Miller, G . J. (2000) Phys. Rev. Let. 84,4617.

280

PL-6
MECHANISMS OF SELF-ASSEMBLY AND SWITCHING OF THE
BACTERIAL FLAGELLUM

Keiichi Namba
Graduate School of Frontier Biosciences, Osaka University Protonic
NanoMachine Project, ERATO , JST, & Dynamic NanoMachine Project, ICORP,
JST, 3-4 Hikaridai, Seika, Kyoto 619-0237 Japan (keiichi@fbs.osaka-u.ac.jp)
The bacterial flagellum is made of a rotary motor and a long helicalfilament by means of which bacteria swim. The size of the bacterial cell body isabout 1 11m by 2 J.tm , but the flagellum grows to about 15 11m long. The flagellar
motor at its base rotates at around 300 Hz and drives the rapid rotation of eachflagellum to propel the cell movements in viscous environments . The diameterof the flagellar motor is 30 to 40 nm , ant it consists of many proteins including
membrane spanning proteins : a rotor ring , made of about 25 copies of FliF/FiiG
complex; about eight stator units, made of MotA/MotB complex ; other parts
such as the rotation switch regulator, bushing, and drive shaft, all made ofdifferent proteins. The long helical filament , which is a tubular structure with adiameter of about 20 nm, is made of 20 ,000 to 30 ,000 copies of a single protein
flagellin, and yet the filament can form left-handed or right-handed helical forms
and switch between these two in response to the twisting force produced byquick reversal of the motor rotation. This allows bacteria to alternate theirswimming pattern between running and tumbling , which is essential for theirtactic behavior. The flagellum also has a short, highly curved segment thatconnects the motor and the helical propeller, and this segment is called hook.
Its bending flexibility makes it function as a universal joint, while the filament isrelatively more rigid to work as a propeller. There is a very short segment called
the hook-filament junction, which is made of HAP1 and HAP3. This junction isthought to play a mechanical buffer to connect the two mechanically distinct
structures. The flagellum is constructed through various self-assembly
processes , in which all the axial structures growing towards the cell exterior are
constructed by the flagellar component proteins translocated from thecytoplasm to the distal end of the growing structure , where three cap complexes
help efficient self-assembly of these proteins in different stages.
We have been trying to visualize the structure of the flagellum in atomic
detail to understand how it self-assembles and works . We solved crystal
structures of core fragments of the flagellar axial component proteins by X-ray
crystallography . X-ray fiber diffraction gave high-resolution structural
information. Electron cryomicroscopy also visualized the structures of thefilament , cap and cap-filament complex. All these structures present interesting
implications for the function of each molecule , demonstrating the importance ofdual nature of protein molecules, flexibility and precision .

281

282

Thursday August 14

Biological Structure Workshop

ABSTRACTS
ORAL SESSIONS

283

BTh1-1
CELL FREE PROTEIN SYNTHESIS AND STRUCTURAL/FUNCTIONALPROTEOMICS

Shigeyuki Yokoyama ,"·b,c and Takanori Kigawa a
8
RIKEN Genomic Sciences Center; bRIKEN Harima Institute at SPring-8;
cDepartment of Biophysics and Biochemistry, Graduate School of Science, The
University of Tokyo (yokohama@biochem .s.u-tokyo.ac.jp)

The RIKEN Institute has started the Structural Genomics/Proteomics
Initiative (RSGI ) (http://www .rsgi.riken.go.jp) at the Genomic Sciences Center(GSC) and the Harima Institute at SPring-S . RSGI is now integrated into theJapanese national project, National Project on Protein Structural and Functional
Analyses , which studies both structures and functions of proteins in selectedbiological systems. We have been determining the three-dimensional
structures of proteins of sequence families and analyzing molecular and cellularfunctions of these proteins in order to establish the structure-function
relationships . Key technologies are essential to conduct the research in a highthroughput way. In particular, cell-free protein synthesis is highly suitable forhigh-throughput preparation and screening of protein samples for structuralproteomics.
Proteins are expressed from libraries of genes/cDNAs by cell-free protein
synthesis methods and/or conventional recombinant methods. In particular, cellfree protein synthesis is highly suitable for high-throughput preparation andscreening of protein samples for structural proteomics . The system may
produce proteins directly from PCR-amplified linear DNA fragments , requiring
no cloning procedures. Hundreds of proteins and protein domains can be
expressed from eDNA clones within a day. By using the dialysis method
developed by Professor A. Spirin , production of proteins has reached the levelof milligram quantities . The system is useful to assess the solubility ,productivity, and structural stability of proteins and thus practical for selecting
protein samples for larger scale production . 1 H- 15 N HSQC spectra aremeasured to screen the domain/proteins, suitable for structure determination.
His tag removal , changes in domain boundary , and optimization of the solvent
condition may improve NMR spectra . After the screening , the selected"excellent" proteins are prepared by cell-free method as labeled protein
samples , the uniformly C3C, 15 N)-Iabeled proteins for NMR structure
determination. Selenomethionine substituted proteins for X-ray crystallography
are also prepared by cell-free method[1).
Reference
I
Kigawa, T. , Yamaguchi-Nunokawa , E. , Kodama , K., Matsuda, T ., Yabuki ,T. , Matsuda, N., lshitani, R. , Nureki , 0 . and Yokoyama , S. (2002) J. Struc.
Func. Genomics 2, 29-35.

284

BTh1-2
A STRUCTURAL GENOMICS APPROACH TO TUBERCULOSIS

Edward N. Baker, Vickery L. Arcus, Kristina Backbro , Graeme L. Card , Jodie M.
Johnston, Moyra Kamen , Nayden Koon , Simon Li , Andrew A. McCarthy,
Rochelle J. Ramsay, Miriam L. Sharpe, and J. Shaun LottSchool of Biological Sciences , University of Auckland , Auckland , New Zealand(ted.baker@auckland.ac.nz)

The availability of ever-increasing numbers of complete genome
sequences is revolutionising the biological sciences . A challenge now in this"genomic revolution " is to add value to the sequence data by focusing on the
structure and function of gene products. Current initiatives in structural
genomics have a number of objectives , both structural and functional, including
the discovery of new folds, determination of representative structures for all
protein families , discovery of function from structure, and the characterisation ofpotential drug targets.
We are participants in a worldwide structural genomics consortium
focused on Mycobacterium tuberculosis, the cause of TB , and one of theworld's most devastating pathogens . Around 3 billion people die annually fromthe disease. Athough drugs exist, resistance is rising and treatment iscomplicated by the unusual nature of the organism , with its dense, waxy cellwall , and its ability to persist in a dormant state in the lung for long periods.
The TB Structural Genomics Consortium [1] has central facilities for the
benefit of all participants, but individual labs pursue their own objectives, withcoordination to try to avoid overlap . Our focus is on two types of target, (a)enzymes from key biosynthetic pathways which are potential drug design
targets , and (b) proteins of uncertain or unknown function that are implicated in
key aspects of TB biology. In the first category we have chosen enzymes
involved in the biosynthesis of essential amino acids and of menaquinone andthiamin . In the second category we focus on proteins of unknown function thatare implicated by microarray experiments either in antibiotic resistance or in the
hypoxic response (and possibly persistence).
The approaches taken in our laboratory to cloning, expression ,purification , crystallization and structure determination will be reviewed . The
major bottlenecks to date have been in obtaining soluble expression and in
crystallization, and we are reviewing our approaches in both these areas. So far
from about 100 genes cloned we have 9 protein structures, with more to come .
The solved structures include several proteins of unknown function, two others
that appear to be good drug targets , and one protein whose structure suggeststhat it is mis-annotated in this and other genomes.
References
1
TB Structural Genomics Consortium : See http://www.doe-mbi.ucla .edu/TB .

285

BTh1-3
STRUCTURAL GENOMICS OF NOVEL MACROPHAGE PROTEINSASSOCIATED WITH INFLAMMATORY DISEASE AND CANCER

Pawel Listwan ,"·c Nathan Cowieson ,8 Anna Aagaard ,a,c Robert Serek ,a Carmel
Walsh ,8 ' Timothy Ravasi ,a,c Christine Wells,a,c Thomas Huber,b David Hume,a,c
Jenny Martin, a,c and Bostjan Kobea,c8

Department of Biochemistry and Molecular Biology, and Institute for Molecular
Bioscience, University of Queensland, St. Lucia QLD 4072 , Australia ;bDepartment of Mathematics, University of Queensland, St. Lucia QLD 4072 ;
cCRC for Chronic Inflammatory Diseases (listwan@uq.edu.au)

Most of the potential pathogens that attempt to invade a mammalian cell
fail at the very first stage due to the remarkable effectiveness of innate
immunity. The presence of the potential pathogens is detected via receptors
that recognise generic non-mammalian structures including cell wallcomponents including lipopolisaccharides, peptidoglycans , lipotechoic acids
and microbial DNA [1] . The first line of defense is the macrophage, which
comprises 15-20% of the cells in the most organs , and is particularly abundantat the routes of pathogen entry such as lung , skin , gut and genitourinary tract[2] . When the potential pathogen is recognised , the macrophage engulfs andattempts to destroy the foreign organism . The knowledge of regulation ofmacrophage function will form the basis of two classes of therapeutics.
Amplification of the toxic function of macrophages to destroy foreign organisms
or tumor cells more effectively is one option , the other being the selective
suppression of some components of the macrophage activation response.
These then can be used to treat conditions like septicaemia and toxic shock ,arthritis , atherosclerosis and other chronic inflammatory diseases the other one.
To define the molecular functions of proteins with roles in macrophages ,we set out to characterise them structurally using X-ray crystallography. We
identify proteins with roles in macrophages through expression profiling using
microarray technology . We select and prioritise the proteins for structural
analysis according to a number of criteria such as anticipated insight intofunction and feasibility for structure determination . We have developed
protocols for cloning , expression and crystallography that can be adapted fo r
high-throughput approach. To the best our knowledge , this project is the firststructural genomics effort in Australia , and the microarray-to-structure pipeline
is unique among the structural genomics initiatives worldwide. Our initial list of
40 proteins resulted in 7 soluble proteins, 2 targets are currently in
crystallisation trails and one is ready for MAD data measurement. Currently weare optimising this system and here we present our strategy for the selection,prioritisation , cloning , expression and crystallisation of a number of protein
targets.
References
1
Hoffman , J.A., Kafatos, F.C. , Janeway, C.A. , And Ezekowitz, R.A. (1999)
Phylogenetic perspectives in innate immunity, Science 284, 1313-1318.
2
Gordon , S. , and Hume, D. A. (1986). Localization and function of tissue
macro-phages, Ciba FoundSymp 118, 54-67 .

286

BTh2-1
ELECTRON CRYOMICROSCOPY OF VIRUS PARTICLES AT SUBNANOMETER RESOLUTION
Wah Chiu ," Z. Hong Zhou,b Matthew L. Baker," Wen Jiang ," Joanita Jakana, 8Matthew Dougherty, a Brian R. Bowman,c Florante A. Quiocho,c and Frazer J.
Rixond8

National Center for Macromolecular Imaging, Baylor College of Medicine,
Houston, TX 77030, USA; bUniversity of Texas Houston Medical School,
Houston , TX 77030; cHHMI, Baylor College of Medicine, Houston, TX 77030;
dMRC, Institute of Virology, Glasgow, G11 5JR, Scotland, UK(wah@bcm .tmc.edu)

Electron cryomicroscopy can resolve three-dimensional structures of large,
icosahedral virus particles at sub-nanometer resolution (7-9 A). At thisresolution, we can clearly identify long helices and recognize beta sheets . A
combined use of bioinformatics, x-ray crystallography of individual components
together with the medium resolution structure of the whole virus can enable us
to derive pseudo-atomic model of the virion . We will demonstrate this approachwith the human herpesvirus capsid.
The herpesvirus capsid is made up of four proteins (VP5, VP26 , VP23 and
VP19C) with a diameter of 1250 A and a total mass of 0.2 billion daltons. The
three-dimensional structure of the intact capsid has been determined at 8.5-A
resolution by electron cryomicroscopy . The crystal structure of the upperdomain of VP5 has been recently solved . There is an excellent match of thesecondary structure elements in the upper domain of VP5 between the crystal
structure and the electron cryomicroscope map . The helix bundle in the middle
domain of VP5 has been found to be structurally homologous to annexin
domain . These helices are located at domains that undergo conformationalchanges during capsid assembly and DNA packaging . The lower domain of the
VP5 forms a floor linking the adjacent capsomere subunits responsible for thestability of the capsid in its mature state . With all the structural and chemical
informatics of the VP5, we can conclude that the VP5 is made up of two newfolds and one old fold to form the 149kD polypeptide . The graphicalsegmentation of the triplex from the electron cryomicroscopy map has shown
the unique spatial arrangement of the two copies of VP23 and one copy of
VP19C. The arrangement of this heterotrimer at the local 3-fold positions
accounts for the asymmetric interactions with adjacent capsid components andthe unusual co-dependant folding of its subunits.
Acknowledgements: This research has been supported by NCRR and NIAID.

287

BTh2-2
CATCHING CATALYSIS IN THE ACT: PROBING ENZYME MECHANISMS
USING SINGLE CRYSTAL MICROSPECTROPHOTOMETRY AND X-RAY
CRYSTALLOGRAPHY
Arwen R. Pearson and Carrie M. Wilmot
Biochemistry, Molecular Biology and Biophysics, The University of Minnesota, 6155 Jackson Hall, 321 Church St SE , Minneapolis , MN 55455 , USA,
(pears079@umn.edu)

Traditionally X-ray crystallography has provided important insights into themechanisms of enzyme catalysis. However, X-ray structures often represent
reaction starts , endpoints or kinetic deadends , and are not direct visualizationsof reaction intermediates formed during turnover. The marriage of spectroscopic
techniques and crystallography in the development of single crystal
microspectrophotometers has revolutionised the field of structural enzymology[1 ,2] .
Many enzymes have been shown to be catalytically active in the
crystalline state and , if there are no major conformational changes associatedwith catalysis , will often remain crystalline during turnover. If an enzyme
reaction involves a chromophore, either as a cofactor or substrate , single crystal
microspectrophotometry can be used to monitor the reaction in the crystal.
When an intermediate of interest is observed to accumulate in the crystal, it canbe flash frozen in a cold nitrogen stream for X-ray structure determination.
I will present an overview of the commercially available 4DX system [3-5] ,as well as methods used in our laboratory to trap reaction intermediates ofmethylamine dehydrogenase for structural studies.
References
1
Hajdu eta/. (2000) Nature Structural Biology 7 1006-1012
2
Wilmot eta/. (2002) Met. Enzymol. 353 301 -318
3
Hadfield & Hajdu (1993) J. Appl. Cryst. 26 839-842
4
Sjogren eta/. (2002) J. Appl. Cryst. 35 113-116
5http://www.4dx.se/spectrop .htm

288

BTh3-1
STRUCTURE MODELLING AND VALIDATION

T. Alwyn Jones, Mark Harris, and Gerard J. Kleywegt
Department of Cell and Molecular Biology, Uppsala University, BMC , Box 596 ,SE- 751 24 Uppsala, Sweden (alwyn@xray.bmc.uu .se)

The recent developments in computer hardware have greatly benefited
crystallography in general, and molecular modelling in particular. I will present
my most recent developments in the use of secondary structure templates
during map interpretation as implemented in the program 0 [1], and ourdevelopment of web-based systems of interest to the crystallographic
community. The latter include MOLRAY [2], X-TRACK [3] and EDS (to be
published , 2003 , I hope).
Model coordinates are usually perceived as the final result of acrystallographic experiment. Unfortunately they suffer from a number of inherent
problems that are best overcome my direct visualization of the structure with theexperimental electron density. This can only be accomplished if theexperimental data (the so-called structure factor amplitudes) are also depositedat the public data banks. We have calculated electron densities for all structuresat the PDB that also have structure factors deposited. They are made available
to users via the world-wide-web, together with derived goodness-of-fit
indicators , via the Uppsala Electron Density Server , EDS(http://fsrv1.bmc.uu .se/eds/).
EDS is also useful as a new kind of structure validation resource. Without
the diffraction data one is restricted to stereochemical-based indicators thatcompare a particular structure with expectations based on the analysis of otherstructures , one's own chemical and biological knowledge, or empirical formulae.
Even so , such indicators will often recognize a sloppily refined structure.
However, only if an electron density map is available can one properly assess
what is wrong and what is more-or-less correct in the deposited model.
References
1
Jones, T. A., Zou , J-Y. , Cowan , S. W. and Kjeldgaard , M. (1991) Acta
Crystallographica , A47 , 110-119.
2Harris, M. and Jones, T. A. (2001) Acta Crystallographica, D57 , 1201 1203.
3
Harris, M. and Jones, T. A. (2002) Acta Crystallographica, D58 , 18891891 .

289

BTh3-2
THE PROTEIN DATA BANK AND STRUCTURAL GENOMICS

Helen M. Bermana
Protein Data Bank; Research Collaboratory for Structural Bioinformatics,
aRutgers, the State University of New Jersey, Department of Chemistry, 610
Taylor Road , Piscataway, NJ 08854-8087 USA (berman@rcsb .rutgers.edu)

The Protein Data Bank (PDB ; http://www.pdb.org/) is involved in several
aspects of structural genomics. The PDB developed and currently maintains
the Target Registration Database (TargetDB ; http://targetdb .pdb .org/),organizes the data dictionaries that will define the specification for the exchange
and deposition of data with the structural genomics centers(http ://deposit.pdb .org/mmcif/) , and creates and maintains software tools to
capture data from standard structure determination applications(http://deposit.pdb.org/software/). Our progress in these efforts will be
described.
The PDB is supported by funds from the National Science Foundation , theOffice of Biology and Environmental Research at the Department of Energy,
and two units of the National Institutes of Health: the National Institute ofGeneral Medical Sciences and the National Library of Medicine.

290

Friday August 15

Biological Structure Workshop

ABSTRACTS
ORAL SESSIONS

291

BFr1-1
CASSIOPEIA- A PROGRESS REPORT FROM THE DEVELOPMENT OFFIVE BEAM-LINES AT THE MAX SYNCHROTRON LABORATORY

Anders Liljas
Molecular Biophysics, Lund University, Lund , Sweden(anders.liljas@mbfys.lu.se)

In a Danish -Swedish collaboration involving many scientists, a new datacollection facility has been built up at the synchrotron laboratory at Lund
University, MAX. The facility is using the MAX-II storage ring run at 1.5 GeV,
where a 3.5 T multipole wiggler provides X-rays of high intensity around 1A
wavelength for the Cassiopeia project. The beam is split into three main
directions. The middle beam is used for a MAD station and the two beams on
the sides are used for two stations each. The two front stations use diamondmonochromators in the Laue mode and the back stations are using Bragg
monochromators. The four side stations have essentially fixed wavelengths
around 1A. Details of the project as well as the initial experiences will bereported.

292

BFr1-2
BUILDING A USER-FRIENDLY BEAM LINE

Aina Cohen, and Paul Ellis
Structural Molecular Biology, Stanford Synchrotron Radiation Laboratory,
SLAC, MS 69, 2575 Sand Hill Road , Menlo Park, CA 94025, USA(acohen@slac.stanford .edu) (ellis@ slac.stanford.edu)

A user-friendly beamline is one that gives visiting researchers the ability to
get maximum value from their synchrotron visit. This means that this beamline
will let them conduct a wide variety of experiments as rapidly and easily as
possible. The protein crystallography group at SSRL has been working toward
this goal in two ways: by building new beamlines optimised for the experimentsthat users want to do, and by implementing new instrumentation, computers,
control systems and software to take maximum advantage of existing stations.
This talk will focus on the expectations of synchrotron users and the ways
in which beamline builders can address them . Topics will include the use ofadvanced control systems to give fixed-wavelength wiggler sidestations MAD
and SAD capability , automated screening with a robotic crystal mounting
system , fluorescence analysis for SAD and MAD, and some of the newtechniques being exploited at SSRL, particularly derivatising with quick soaks inhigh concentration salts , krypton and xenon pressurisation, SAD phasing, andusing low energy x-rays to maximise anomalous signal.
Acknowledgements: SSRL operations are funded by DOE BES, and the SSRL
Structural Molecular Biology program by DOE BER, NIH NCRR BTP and NIH
NIGMS. The JCSG is funded by the Protein Structure Initiative of the National
Institutes of Health, National Institute of General Medical Sciences.

293

BFr2-1
NEW BEAMLINES FOR MACROMOLECULAR CRYSTALLOGRAPHY
Janet L. Smith. 8 Robert F. Fischetti,b L. E. Berman,c W. Diete,d R. Signorato,d R.
Benn,b S. Stepanov,b R. Sanishvili,b S. Xu, b A. Urakhchin,b 0 . Makarov,b and W.
W. Smithb
8
Dept. of Biological Sciences, Purdue University, West Lafayette, IN 47907
USA; bBiosciences Division, Argonne National Laboratory, Argonne, IL 60439
USA; cNational Synchrotron Light Source, Brookhaven National Lab, Upton , NY
11973 USA; dACCEL Instruments GmbH , Friedrich Ebert Str. 1, 51429
Bergisch-Giadbach, Germany (smithj@purdue.edu)
X-ray crystallography applied to current biological problems is entirely
dependent on synchrotron radiation. A greatly improved success rate forbiological diffraction experiments with synchrotron radiation transformed thepractice of macromolecular crystallography in the 1990s. Today, the vast
majority of crystal structures published or deposited in the PDB are
determined with data from synchrotron X-ray sources. Technologies large
and small contribute to the improved success rate . Compared to 1993,
today's synchrotron sources produce X-ray beams that are brighter, moreparallel and more stable ; today's beamlines are more numerous, user
friendly and accessible ; today's detectors are faster , more sensitive and wellmatched to the brighter sources; and today's cryoprotected samples travel
more safely and withstand greater radiation doses.
Multiwavelength anomalous diffraction (MAD) is the most frequently
employed method of phase determination for structures that are not
Of all biological diffractionaccessible to molecular replacement.
experiments, MAD places the greatest demands on a synchrotron beamline.
The beam must be highly monochromatic, stable in position and energy, andrapidly tunable . Although improvements in synchrotron beams, beamline
optics and sample stability have made MAD accessible to mostcrystallographic problems, experimental design still must be done carefully,
with an understanding of the likeliest sources of error.
Undulator sources at 3'ct-generation synchrotrons are best known for
their brightness .
However, crystals of biological macromolecules areradiation sensitve, even when frozen, and features beyond simple brightness
account for the success of 3'ct-generation undulator sources for thisexperiment. Bright, stable , small , parallel undulator beams are ideal for
beamlines that must be robust to changes in beam size , energy and focus.
To exploit the special properties of the undulator source, especially for MAD
experiments , we are developing a new crystallography facility (GM/CA CAT)at the Advanced Photon Source (APS) . Two beaml ines will be based on the
APS dual canted-undulator geometry, which incorporates two independent,
hard X-ray devices in one straight section . The particle beam trajectorythrough the devices introduces a 1-milliradian horizontal separation between
the two X-ray beams . The novel beamline design will provide a 500-mm
separation between the beams at the first sample position . A pair ofadaptive bimorph mirrors will focus each beam . Beamline controls based on
EPICS and Blulce will provide automated beamline setup, and sample
mounting and centering . The GM/CA CAT project is sponsored by the
National Institute of General Medical Sciences (GM) and the National Cancer
Institute (CA) of the US National Institutes of Health for their grantees andthe biological research community.

294

BFr2-2
BIOLOGICAL APPLICATIONS AT THE AUSTRALIAN SYNCHROTRONFACILITYJose Varghese
CSIRO Health Sciences and Nutrition, 343 Royal Pd . Parkville, Victoria 3052,
Australia (Jose.Varghese@csiro.au)

First light at the new Australian synchrotron radiation source, to be locatednear the Monash University Campus in Melbourne, will appear in 2007. Whiledesign work on the machine facility and building have been finalised , planningfor the beam-lines is ongoing and offers opportunities for the Australian
biological sciences unprecedented access to high brilliance light ranging fromthe infrared to hard X-rays . This facility will be a great boost to structural
biologists who represent the largest single user community. However this facility
will also enable biologists to have access to a number of other techniques likecircular dichromism spectra , small angle solution scattering , fluorescence
spectroscopy, micro probes, biological and medical imaging, radiology, surface
scattering, X-ray microscopy and general spectroscopy. Proposals for beamlines that will support these techniques will be discussed, and the applications
to biological sciences that this infrastructure will enable shall be presented .

295

296

Thursday August 14

Sagamore XIV

ABSTRACTS
ORAL SESSIONS

297

STh1-1
BONDING EFFECTS IN LARGE METAL CLUSTER MOLECULES
Piero Macchi, and Angelo Sironi
Dipartimento di Chimica Strutturale e Stereochimica lnorganica, Universita di
Milano, via Venezian 21 20133, Milano, Italy (piero.macchi@unimi.it)

The chemistry of medium and high nuclearity transition metal clusters [1]is particularly intriguing because of the bonding mechanism that characterizes
the metal cages, somewhat intermediate between that of simple metal bonded
molecules and that of bulk metals themselves .
In this context , our experimental and theoretical studies on somemolecules of general formula [M 6 (C0) 16 2" (M =Co , Rh; n = 0-2) were carriedout [2] with the intent of characterizing the source of stabilization for the cluster
cages and the role of different ligands or stereochemical arrangements. The
comparison with dimeric species previously studied (3] allows a generalizationof the bonding mechanisms.
Moreover, we have investigated the changes occurring upon introducing
interstitial species (like hydrides) in the metal cavities. A comparison with simple
metal hydrides and metal-metal bonds supported by hydrides is proposed .

.nrReferences
I
Mingos, D. M. P. and Wales, D. J . Introduction to cluster chemistry;
Prentice-Hall, London , 1990.
2
Macchi, P ., Garlaschelli, L., Sironi, A., work in progress.
3(a) Macchi, P., Proserpio, D. M. and Sironi , A. (1998) J. Am. Chern. Soc.
120, 13429; (b) Macchi, P., Garlaschelli , L. and Sironi , A. (2001) J. Am.
Chern. Soc. 124, 14173.

298

STh1-2
EXPERIMENTAL RESULTS ON COUPLED ANALYSIS OF SPIN AND
CHARGES DENSITIES OF Y AND Gd COMPLEXES

N. Claiser." B. Gillon,b M. Souhassou, 8 C. Lecomte, 8 N. K. Hansen, 8 Y.
Pontillon, c A. Caneschi,d D. Gatteschi,d C. Carbonera,d A. Bencini,d A.
Cousson ,b and E. Lelievre-Bernae
8
L.C.M.3B., UMR CNRS 7036, Faculte des Sciences, BP 239, 54506
Vandoeuvre-les-Nancy, France; blaboratoire Leon Brillouin , CEA-CNRS,
Centre d'Etude de Saclay, 91191 Gif/Yvette, France; cORN/DEC, Centred'Etudes Nucleaires de Grenoble, 17 rue des Martyrs, 38054 Grenoble Cedex
9, France; dDepartment of Chemistry, University of Florence, Via Maragliano 77,
50144 Firenze, Italy; elnstitut Laue-Langevin, 6 rue Jules Horowitz, BP 156,
38042 Grenoble Cedex 9, France (claiser@lcm3b.uhp-nancy.fr)
Within the vast field of molecular magnetism, we have studied two complexes
in which the semiquinoato radical (DTBSQ=3,5-di-tertbutyl- semiquinonate, S=1/2)
coordinates a heavy atom (Yttrium, S=O or Gadolinium, S=7/2). Two HBPZ3(hydrotrispyrazolylborate) complete the coordination sphere (1]. On the basis of theexperimental electron and spin densities, our aim was to highlight the interactions
at the microscopic level that play an important role in the magnetic behaviour
observed in these two complexes.
The total electron density, obtained by a high resolution X-ray diffraction
experiment, and the spin density, obtained by a polarised neutron diffraction
experiment, were determined on the two complexes: Y-SQ and Gd-SQ. The
topological analysis of the total electron density [2, 3] was used to characterise
quantitatively the interatomic interactions, particularly between the ligands and thecentral ion. This method gives also access to the net atomic charges, useful for thecomprehension of the charge transfer inside the complexes. In this study, we will
present the experimental spin density distribution and the topological properties ofthe electron density in the two complexes and confront them to the OFT
calculations results.

Eifh_L Projected spin density induced at 1.9 K
under 9.5 T on the semiquinoato ring plane of Y2
SQ . Contours: ±0.005 with steps of 0.010 ma/A

Fig. 2: Static deformation density in thesemiquinoato plane of Y-SQ. Contours of
3
0.05 eA· : positive (solid), negative (shortdashed) and zero (long dashed).

References
1
Dei, A., Gatteschi, D., Pecaut, J., Poussereau, S., Sorace, L. and Vostrikova,
K. (2001) C.R. Acad. Sci. Paris, Chemistry 4, 135-141.
2
Bader, R. F. W. (1990) Atoms in molecules: a quantum theory. The
International Series Monographs in Chemistry. Oxford Clarendon Press.
3
Souhassou, M. and H. Blessing, R. (1999) J. Appl. Cryst. 32,210.

299

STh1-3
SCATTERING FACTOR CALCULATIONS AND DISPERSION CORRECTIONSFOR HEAVY ATOMS

C. T. Chantler
School of Physics, University of Melbourne, Parkville , Vic 3010 , Australia(chantler@ph .unimelb.edu .au)

Reliable knowledge of the complex X-ray form factor and the photoelectricattenuation coefficient is required for crystallography , deformation density
bonding studies and refractive index studies . Dispersion corrections areimportant in DAFS , MAD analyses , and XAFS. Discrepancies between currently
used theoretical approaches of 200% exist for numerous elements from 1 keV
to 3 keV X-ray energies, and at higher energies these discrepancies can persist
at the 10% level or more . Recent tabulations [1) improve upon the theoreticaluncertainty in some of these reg ions by a factor of 10 and reduce the error ofthis approach to below one standard deviation. Recent experimental
developments [2) have begun to probe alternate theory, provid ing a tool toinvestigate the significance of relativistic corrections and convergence criteria
across a range of atomic number. In part , this has revealed that moretheoretical work will be required in future years.
References
I
Chantler, C. T., Olsen K. and Zucker, D. S. (2003) X-Ray Form Factor,
Attenuation and Scattering Tables (version 2.0) . [Online)
http://physics.nist.gov/ffast [2003 , March 31] . National Institute ofStandards and Technology, Gaithersburg , M D; Chantler, C. T. (2000) J.
Phys. Chem. Ref. Data 29(4), 597-1048; Chantler, C. T. (1995) J. Phys.
Chem. Ref. Data 24, 71-643.
Chantler, C. T. , Tran , C. Q. , Paterson , D., Cookson , D. and Barnea , Z.
2
(2001) Phys. Lett. A286, 338-346; Chantler, C. T. , Tran , C. Q ., Barnea , Z. ,Paterson , D., Cookson , D. and Balaic, D. X. (2001) Phys. Rev. A64,
062506-1- 15.

300

5Th1-4
MULTI-TEMPERATURE EDD MEASUREMENT IN RARE-EARTH
HEXABORIDES LB 6 (L=La, Ce, Sm)
K. Tanaka, S. Funahashi, and S. Takagi
Department of Materials Science and Engineering , Nagoya Institute ofTechnology, Gokiso-cho, Showa-ku, Nagoya 466-8555, Japan(kiyo@tana.mse.nitech.ac.jp)

Rare-earth hexaborides LB 6 (L=La, Ce, Sm) have cubic crystal structurewith metal atoms at body-center and the centers of regular 8 6 octahedra atcorners with B atoms on edges. They have very interesting physical properties.
Sm8 6 is a Kondo insulator and Sm 3+ has formally five 4f-electrons. La 3+ in La8 6
has formally no 4f-electrons. Ce8 6 is a famous Kondo crystal and its EDD at thefour temperatures were analyzed with X-ray AO analysis method exhibiting theelectron transfer from Ce-4f and 8-2p electrons to the (8-8)out bonds connecting
two 8 6 regular octahedra[1]. This causes anharmonic vibration (AHV) at low
temperature and entropy increases. Since the entropy increment caused by the
4f-electron donation to (8-8)out bonds increases entropy it cannot be stopped.
Therefore the EDD of the three title compounds were measured at 100 , 165,
230 and 298 K to compare the EDD of the three complexes. The relationshipbetween electron transfer and AHV at low temperatures in these complexes
with different physical properties is also interesting.
Highly accurate structure factor measurement of EDD of rare-earth
complexes is necessary. Especially multiple diffraction (MD) easily affects thediffracted intensities more than 1 % of the observed ones while the number of
4f-electrons is very small compared to the total ones in the unit cell forcing us
the measurement with the accuracy less than 1%. Therefore the sample wasrotated around the scattering vector (\l'-scan) and the intensity were measured
where intensity perturbation due to MD is calculated to be less than 0.5 %[2].
The deformation density of La8 6 at 165 K exhibited deep troughs andpeaks which alternately distribute spherically around La 3+. It was analyzed with
the X-ray AO analysis method . A part of the 5pU=3/2) as well as 8-2Pz electrons
are transferred to 4f(fs) and 4f(r7) orbitals and both are occupied by 0.09(1)electrons making spherical EDD. The residual density is very small indicating
the success of the refinement. The deformation density of Sm8 6 at 100 and
165K revealed striking peaks along <1 00> directions. The 5pU=3/2) and fourfold 4f(f8 ) orbitals are fully occupied. However two-fold 4f(r7) orbitals , each ofwhich is supposed to accommodate 0.5 electrons, are occupied by only
0.08(23) and 0.1 0(2) electrons at 100 and 165 K, respectively. Instead of it Sm5d(f8, j=5/2) orbitals are occupied fully and 8-2p electrons are transferred to Sm
atoms. There is no indication of AHV of Sm atoms . The X-ray AO analysis forLa86 and Sm86 at the other temperatures are being done and the variation of
8-8 bond lengths with temperature are also presented in conjunction with thechange in electron configurations.
References
I
Tanaka , K. and Onuki , Y. (2002) Acta Cryst. 858, 423-436.
2
Tanaka, K. and Saito, Y. (1975)Acta Cryst. A31, 841-845.

301

STh2-1
OPPORTUNITIES FOR RESEARCH AT AUSTRALIA'S REPLACEMENTRESEARCH REACTOR

R. A. Robinson
Bragg Institute, ANSTO , Lucas Heights, NSW 2234, Australia(rro@ansto .gov.au)

The 20-MW Australian Replacement Research Reactor represents
possibly the greatest single research infrastructure investment in Australia 's
history. Construction of the facility has commenced, following award of theconstruction contract in July 2000, and the construction licence in April 2002 .
The project includes a large state-of-the-art liquid deuterium cold-neutron
source and supermirror guides feeding a large modern guide hall , in which mostof the instruments are placed . Alongside the guide hall, there is good provisionof laboratory, office and space for support activities . While the facility has"space" for up to 18 instruments, the project has funding for an initial set of 8
instruments, which will be ready when the reactor is fully operational in January
2006. Instrument performance will be competitive with the best research reactor facilities anywhere, and our goal is to be in the top 3 such facilities
worldwide . Staff to lead the design effort and man these instruments have been
hired on the international market from leading overseas facilities , and fromwithin Australia , and 6 out of 8 instruments have been specified and casted. At
present the instrumentation project carries -15% contingency. An extensive
dialogue has taken place with the domestic user community and ourinternational peers, via various means including a series of workshops over thelast 2 years covering all 8 instruments, emerging areas of application likebiology and the earth sciences , and computing infrastructure for the
instruments.
In December 2002 , ANSTO formed the Bragg Institute, with the intent of
nurturing strong external partnerships , and covering all aspects of neutron and
X-ray scattering, including research using synchrotron radiation .
I will discuss the present status and predicted performance of the neutronbeam facilities at the Replacement Reactor, synergies with the synchrotron in
Victoria, in-house X-ray facilities that we intend to install in the Bragg Institute,
at Lucas Heights, and the tremendous opportunities that all of this presents forresearch in Australia .

302

STh2-2
ENPI- THE EUROPEAN NEUTRON POLARIMETRY NETWORK, A STATUSREPORT

Francis Tassel
lnstitut Laue-Langevin, BP 156, F-38042 Grenoble Cedex 9, France(tasset@ill.fr)

Instrumentation for polarised neutron science, including for atomic
magnetisation maps measurements, is being renewed and extended in aradical way. Last decade, revolutionary tools were introduced both for the
production and the analysis of the neutron beam polarisation as well as for themeasurement of the associated 3d-vector quantity. These last three years,
such advanced modular tools, like the 3He Neutron-Spin-Filter, and the Zerofield polarimeter Cryopadum, were actively developed and commissioned
within the frame of EC-FP5 RTD-Network ENPI. A status report of thissuccessful collaboration involving 8 European neutron groups interested in
Polarimetric Neutron Scattering will be presented.

303

STh2-3
CURRENT STATUS AND FUTURE PLANS AT THE AUSTRALIANSYNCHROTRON PROJECT

S. W. Wilkins
CSIRO , Manufacturing and Infrastructure Technology PB33 Clayton Sth , Vic
3169 , Australia (Steve.Wilkins@csiro.au)

The Australian Synchrotron Light Source , will be a 3 GeV double bend
achroma! (DBA) ring with low emittance (- 8 nm rad) that is scheduled tocommence construction works in mid 2003 and to be commissioned in 2007. It
will be sited adjacent to the campuses of Monash University and CSIRO in
Clayton , Victoria .
The ring will be a medium-sized (216m circumference) one with highbrightness such as to approach in performance in the - 10 keV regime (of typicalinterest to crystallographers) some of the very large third generation rings. The
ring will have 14 (12 useable) straight sections and be able to accommodate up
to 30 beamlines.
Early stage beamlines under consideration and of interest to
crystallographers and materials scientists include those designed for; i)macromolecular crystallography, ii) small molecule and charge-density studies;iii) infrared spectroscopy , iv) high performance scanning microprobe ; iv) a
mi crodiffraction microprobe high-resolution powder diffraction , and v)
SAXS/WAXS .
References
http://www.synchrotron .vic.gov.au/general_info/beamline_proposals.asp
I
Boldeman , J. W. , Th e Australian Synchrotron Light Source , paper2
presented to EPAC 2002 .

304

STh2-4
CHARGE DENSITIES OF PHOSPHORUS CONTAINING COMPOUNDSAT20 K
Marc Messerschmidt, and Peter Luger
Institute for Chemistry/ Crystallography, Free University Berlin , 14195 Berlin ,Germany (mcmesser@chemie.fu -berlin .de)

All measurements are performed on a Huber 4-circle-goniometer with a 2stage-helium-cryostat and a Bruker-Apex detector. This setup benefits from thelow running costs and good temperature stability of the closed cycle Helium
cryostat. While th ese cryostats are normally usedwith carbon or beryllium vacuum chambers , that
produce a lot of powder lines, we have developed
a new vacuum chamber, which is constru cted
from 0.1mm Kapton film . This gives small andun structured ba c kground . The cylinder isstabilized through spanning inside the large Huber
Eulerian cradle . This mounting only on top andbottom avoids any shadowing of the beam path.
Measurements of some weeks at 20 K are easily
possible. The crystal is normally centered optical ,because transparent kapton film is used . Charge
densities of phosphorus compound have normallyhigh residual densities, when measured at liquid
nitrogen temperature . This phenomenon is often
explained with inharmonic thermal motion. Our
first system is Adenosinemonophosphate and as a model system we want to
use Phosphoruspentoxide. Therefore we present results of 20 K measurements
and compare it with results from 1OOK.

305

STh3-1
EXPERIMENTAL ATTEMPTS TO MEASURE NONCOLLINEAR LOCALMAGNETISATION

P. J. Brown
lnstitut Laue Langevin , BP 156, 38042 Grenoble, France (brown@ill.fr)

The representation of atomic magnetic moments as simple vectors , shownas arrows in the pictorial representation of a magnetic structure , has proved avery useful one; but it should not be pushed too far. In a solid, themagnetisation is a continuous function , a property of the electron wavefunctions , and there is no requirement that it should be collinear. Neverthelessthe assumption of a collinear magnetisation distribution is widely made and one
should therefore give some thought to the circumstances in which it might not
be valid. The first and most obvious is that of a non-collinear magnetic
structure . When the atomic moments themselves are not parallel it would be
naive to suppose that there is a well defined boundary between atoms at which
the magnetisation changes abruptly from one general direction to another. A
second example occurs in anisotropic systems; if the local easy axes ofmagnetisation of atoms are not parallel to one another then the magnetisation
distribution induced by an applied field will be non-collinear. Furthermore evenin very simple systems in which the orbital moment is not fully quenched there
may be non-collinearity due to spin-orbit interaction. In fact the spin-orbit
interaction is by far the most important cause of non-colinearity in magnetic
systems, being the principal means by which an atom's spin direction is coupled
to the orientation of its ligand environment. In all the examples which will begiven , in which a non-collinear magnetisation distribution has been sought orfound , this non-collinearity is primarily due to the presence of orbital
magnetisation .
Several experimental techniques are available to probe non-collinearity ofthe magnetisation distribution . The most direct is to measure both themagnitude and direction of the magnetic interation vectors which give its fouriercomponents.
Such measurements are now becoming possible for
antiferromagnets with the advent of a new generation of neutron polarimeterswhich will allow both greater geometric flexibility and higher precision. However
up to now non-collinear magnetisation distributions have been revealed bymore indirect means. Polarised neutron flipping ratio measurements can give
only a single component of the magnetic interaction vector directly. However
the special geometric properties of the interaction vector and the symmetry
breaking properties of an applied field can be exploited to obtain evidence of
non-collinearity in the magnetisation distribution even from such limited data.

306

STh3-2
MAGNETIC EXAFS AS A TOOL TO MEASURE RADIAL DISTRIBUTION OF
SPIN AND ORBITAL MAGNETIC MOMENTS

Andrei Roqalev, and Jose Goulon
European Synchrotron Radiation Facility (E .S.R.F .), BP-220 , F-38043 Grenoble
Cedex, France (rogalev@esrf.fr)

Over the past decade , X-ray Magnetic Circular Dichroism (XMCD) has
developed as a useful/oca/ probe of magnetic properties in ferro(i)magnetic andparamagnetic compounds. In XMCD experiments , one measures the differencein the X-ray Absorption Spectra recorded with left and right circularly polarized
photons while the sample magnetization is kept parallel or antiparallel to thedirection of propagation of the incident X-ray beam. What made XMCD
attractive is the possibility to access, using magneto-optical sum rules , toorbital-projected magnetic moments both in magnitude and direction with thefull benefit of the element selectivity that characterizes X-ray absorption
spectroscopy. From the very early work it was realized that magnetic dichroism
was not restricted to only the x-ray absorption near edge structure (XANES)
region but contributed also to the extended x-ray absorption fine structure(EXAFS) region .
In this presentation we will show that the magneto-optical sum rules intheir differential form allow one to extract from the Magnetic EXAFS spectra theradial distribution of spin and orbital magnetic moments around the absorbing
atom in ferromagnet. The validity and great potentiality of this approach will beillustrated using Magnetic EXAFS spectra recorded at the L2 .3-edges of Eu in
the ferromagnetic semiconductor EuS . The results can be nicely correlated withthose derived from conventional XMCD measurements in the XANES region.

307

STh3-3
TWISTED STATES OF Fe/Tb MULTILAYERS

Katsuyoshi Takano ,8 Kazuhiro lkeuchi ,b Hiroshi Sakurai ,b Hiromi Oike ,b andFumitake ltohb
8

Satellite Venture Business Laboratory, Gunma University, 1-5-1 Tenjin-cho ,Kiryu , Gunma , 376-8515, Japan ; bDepartment of Electronic Engineering ,Gunma University, 1-5-1 Tenjin-cho, Kiryu , Gunma , 376-8515, Japan(ktakano@el.gunma-u .ac.jp)

The magnetic structures of multilayers have been understood as interface
effects. Thus the multilayers with a long artificial period have been thought tohave bulk like behaviour. Therefore there are a few investigations about
multilayers with the long period . However we found that the Tb magnetic
moments in [Fe(12.4nm)/Tb(15 .2nm)]2 5 multilayer shows twisted state
structures at a low temperature and a certain magnetic field , wh ich are different
from bulk Tb metal.
In order to see the local magnetic structures , the magnetic moment of Fe
and Tb were measured by x-ray magnetic circular dichroism (XMCD) at the Fe
K-edge at the Tb L2.3-edges. The magnitude and direction of magnetic moments
were derived from the XMCD intensities and signs.
We have measured the magnetic field dependence of the XMCD intensity[1]. [2] . The sample was at first demagnetized . Then the XMCD intensity wasmeasured at a magnetic field with reversing the field using fi xed circularly
polarized x-rays. This measurement was repeated by stepwise increasing themagnetic field from 0.2 kG to 6.2 kG . Thus obtained information corresponds tothe initial magnetization of each element in the M-H curve [2] .
Above 150 K, both Fe and Tb moments increase proportionally withincreasing the magnetic field up to 1.5 kG , keeping the coupling
ferrimagneticaly. Below 150 K, the Fe moment increases , while the Tb moment
decreases with increasing the magnetic field . This behaviour can be explainedby a twisted state ; the magnetic moments of Fe and Tb align anti-parallel in the
low field . But the magnetic moment of Tb begins to turn to the applied field ,keeping the Fe moment constant.
ReferencesI
ltoh, F., Nakamura, M., Sakurai , H., Kiriaake , H. , Nawate, M., Honda, S.
and Kawata , H. (1993) Proc. 7th Int. Conf. X-Ray Absorption Fine
Structure, Kobe, 1992, Jpn. J. Appl. Phys. 32 Sippi. 32-2 , 326 .
2
Koizumi , A. , Takagaki , M., Suzuki , M. , Kawamura , N. and Sakai , N. (2000)
Phys. Rev. B 61 , 14909.

308

Thursday August 14

Sagamore XIV

ABSTRACTS
POSTER SESSIONS

309

SThP-01
THE ATOMISTIC ORIGIN OF THE INVERSE PIEZOELECTRIC EFFECT IN
a-Si02 AND a-GaP04

Jav Davaasambuu ,8 Vasili Kochin ,8 Andreas Pucher,8 Semen V. Gorfman ,8Vladimir G. Tsirelson ,8 Peter Blaha ,b and Ullrich Pietschc
8
Quantum Chemistry Department, Mendeleev University, Moscow, Russia ;blnstitute of Materials Chemistry, Technical University of Wien , Austria ; clnstitute ofPhysics, University of Potsdam , Potsdam , Germany (upietsch@ullipc.physik.unipotsdam .de)
The inverse piezoelectric effect of a-quartz can be observed applying an
external electric field parallel to the non-centrosymmetric [11 .0] direction. In aprevious paper we have shown that the model of field induced mutual
displacement of ionic sublattices fails for the explanation of the atomic origin of themacroscopic measurable effect. Therefore we proposed an alternative model
which is based on the rotation of nearly rigid Si04 tetrahedra under influence of theexternal electric field considering the strong covalent bond between silicon andoxygen .
Meanwhile this model has been verified by measuring the changes ofintegrated intensities of selected Bragg reflection DRJR of a-Si0 2 and theisostructural a -GaP0 4 under influence of a periodic external high electric field of E
11 8 kV/mm . For the first time a similar experiment was performed at low
temperatures (50 < T < 300 K) .
The received data were interpreted in terms of a semi-empirical structure
model and by ab-initio calculations. Nine structural parameters of the semiempirical model were refined using nine selected Bragg reflections which were
measured at different field strength . For the refinement we used the constraint ofrigid Si04 tetrahedra . In addition , the form factor variation was neglected because
the quantum-mechanically predicted field dependence is two orders of magnitude
smaller than the experimental data. Our model fits all measured DRJR in aqualitative right manner. At E=3kV/mm the Si-0-Si angle in direction parallel andperpendicular to the applied field change by about 0.05° and 0.02°, respectively. In
GaP04 the Ga-0-P angles parallel to the field alter by about 0.12° reflecting thehigher piezoelectric coefficient d111 compared to a-Si02.
The temperature dependence of DRJR "s was measured down to 50 K. They
can be interpreted mainly by the temperature dependence of Debye-Waller factors
but an additional contribution caused by the field-induced rotation of Si04 and(Ga ,P)04 tetrahedra , respectively.
Ab-initio calculations have been performed using the WIEN2k-package. Here
we defined a supercell of reduced symmetry along the [11 .0] direction of the quartz
structure containing 72 atoms. The external electric field of about 5 kV/mm ismodelled by an additional saw-like potential. The relaxed atomic positions within a
sub-unit of the supercell with constant field strength were used as input for thesemi-empirical model, mentioned above. Although the calculations are not finishedyet, the results seem to verify our predictions.
References
I
Tsirelson, V. G. , Gorfman, S. V. and Pietsch, U. Acta Cryst A. submitted .
2
Davasambuu , J., Kochin , V., Pucher, A. and Pietsch , U. (2002)
Europhys.Lett. submitted.
3
Stahn , J. , Pietsch , U. , Blaha, P. and Schwarz, K. H. Phys.Rev. B63 , 165205.

310

SThP-02
SIMULATION OF COMPTON DOUBLE SCATTERING

Yukinobu Kakutani, Akihisa Koizumi , and Nobu hiko Sakai
Graduate School and Faculty of Science , Himeji Institute of Technology, Hyogo
678-1297, Japan (yukinobu@sci.himeji-tech .ac.jp)
In 1987, a sim ul ati on of magnetic Compton double scattering of circu larly
po larized photons by mag netic electro ns was repo rted by Sakai [1] . Thi ssimu lation code was suitabl e for the mag netic Compton scatte ring (MCS)
experiments using gamma-ray sources , in whi ch no linear pola rization of theincident gamma-rays presented .
We have made a new simulation code including both linea r and circularpolarizations of inciden t photons , which is su itable fo r the MCS expe rime nts
utilizing synchrotron radiation x-rays .
First , the validity of the prese nt simu lation was confirmed by the
reproduction of the experimenta l ratio between Compton double scatteringresult on Ge measured by Pasic et a/[2]. The agreement between the si mulationand expe rimental result is good , as shown in Fig . 1. Second , it was confi rmed
th at the intensity of Compton do uble scattering depends on po larization ofincident photons, material, incident energy and sample volume.
Concernin g to th e spin-dependen t Compton double scattering , a resu lt of
simula tion on Fe (2 mm heig ht, 10 mm wide and 10 mm thickness), showedthat the influence of mag netic Compton double scattering on 3d transition metal
is neg lig ible for ordinary measurements .
10'
O•>«<

10'

l(j'

A

y
t 1d

I
. /

s 10'

n

:

e

i

~

•.,? ••
\

.'

. "
~

n
I 102

103

10'

0

z

~

.•

1
t 10

10'

10'

10"'

10

20

30

40

so

4.0

U.O

24.0

34.0

04.0

54.0

Energy lk•VJ(b)(a)
Fig.1: Resu lts of Compton dou ble scattering on Ge. (a) present simu lation , a
Lorenz type fun ction is ass umed to simu late Compto n broadeni ng. (b)experiment by Pasic et a/[2].
References
Sakai, N. (1987) J. Phys. Soc. Jpn. 56 ,2477-2485.
1
Pasic, S. and ll akovac, K. (1997) Phys. Rev. A 55, 4248-4252.
2

311

SThP-03
DIRECT PHASE DETERMINATION OF FRACTIONAL REFLECTION IN
CHARGE-DENSITY-WAVE CRYSTALS USING X-RAY MULTIPLE
DIFFRACTION

Shih-Lin Chang ," Chao-Hong Ou,b.c Mau-Tsu Tang ,c Yu . P. Stetsko ,c Yen-Ru
Lee ," Tsong-Tze Lin ," Shih-Chang Wong ,8 and Wen-Shien Suna
80epartment of Physics , National Tsing Hua University; bOepartment of
Physics, Tamkang University; cNational Synchrotron Radiation ResearchCentre , Hsinchu , Taiwan, 300 , R.O.C . (slchang@phys.nthu .edu .tw)

We report the direct determination of collective phase of charge-density
wave (COW) [1 , 2) in a quasi-two-dimensional material 2H-NbSe 2 using themultiple diffraction technique . Via the coherent interaction between the X-ray
waves propagating in the COW modulated structure and the host structure , thecollective phases of COW were determined to be either 0" or 180" from theanalyses of the asymmetry of the diffraction profiles along the azimuth scans ofa COW fractional reflection . The phases were observed not to vary withchanging temperature , suggesting that the phases are pinned. This finding may
be useful for the direct observation of the dynamic phenomena caused by thephase of the density waves.
References
1
Thorne, R. E. (1996) Physics Today, May 42-43.
2Overhauser, A. W. (1978) Advances in Physics 27 , 343-357 .

312

SThP-04
ELECTROSTATIC PROPERTIES OF THE MOLECULAR SIEVE AIP04-15
E. Aubert, F. Porcher, M. Souhassou, and C. Lecomte
Laboratoire de Cristallographie et Modelisation des Materiaux Mineraux et
Biologiques, CNRS UMR 7036 , Universite H. Poincare - Nancy I, BP 239 ,
54506 Vandceuvre-les-Nancy, France (aubert@lcm3b.uhp-nancy.fr)

Charge density and electrostatic potential analyses are of special interestin characterizing host I guest systems like zeolites or AI PO systems[1).
Single crystal of AIP04-15 (NH4Aiz(OH)(HzO)(P04)2HzO) were obtained byhydrothermal synthesis (180°C); the X-ray diffraction data were collected on a
Non ius K CCD diffractometer, Mo(Ka) radiation, P2 tl n, a=9.556(1) A,
b=9.563(1) A, c=9.615(1) A, b=1 03.58(1The charge density was modeledaccording to the multipolar formalism of Hansen and Coppens using program
MoPro[2). The final residual indices are R=1.02 % , Rw=0 .66%, Nobs=4725 ,Npar=51 0, (sin8/A.)max=0 .90A- 1 . The analysis of the topology of the electron
density was performed on the multipolar and lAM models in order tocharacterize interactions between framework atoms (P,AI-0) and between
framework and guest molecules (hydrogen bonds).
The electrostatic potential (EP) was derived from two representations . The
first one consists of point charges placed at atomic positions. The potential was
obtained trough a summation in direct space V(r)=S;Q;Ir,,; using different set of
charges (issued from a Pv/K refinement or topological analysis). The second
one used the charge density issued from the multipolar model and calculations
were performed with summation in direct and reciprocal spaces[3,4). Fromthese two representations, electrostatic interaction energies were derived . For
the second one, it was evaluated for a molecule A as EA=l'o/t-A(r)pA(r)dr, where
Vt-A(r) is the EP that is felt by molecule A (generated by all the crystal except
molecule A) and PA(r) is the charge density of molecule A. Thus , electrostaticinteraction energies for water molecules , ammonium cation and hydroxyl groupoccluded in the molecular sieve are compared with results obtained from adifferential scanning calorimetry experiment.

t.

References
I
Lecomte , C. (1999). In Implications of Molecular and Materials Structure
for New Technologies , pp. 23-44. Kluwer Academic Publishers.
2
Guillot, B. , Viry, L., Guillot, R. , Lecomte , C. and Jelsch , C. (2001) J. Appl.
Cryst., 34, 214-223.
3
Stewart, R. F. (1979) Chem. Phys. Lett. 65, 335-338.
4
Ghermani , N. E ., Bouhmaida , N. and Lecomte , C. (1992) ELECTROS,STATDENS. Internal report URA CNRS 809. Universite Henri Poincare ,Nancy 1, France.

313

SThP-05
VIRTUAL EXPERIMENTS FOR THE BUILDUP OF ASPHERICAL ATOMSCATTERING FACTORS OBTAINED BY A NOVEL PARTITIONING SCHEME
AND APPLICATION TO A TRIVALINE STRUCTURE
Birqer Dittrich,a and Dylan Jayatilakab
aFreie Universitat Berlin , lnstitut fuer Chemie/Kristallographie, Takustr. 6, 14195
Berlin , Germany, Tel.: +49 30 83853450, Fax.: +49 30 83853464; bUniversity ofWestern Australia , Chemistry, 35 Stirling Highway, Crawley WA 6009 , Australia ,Tel.: +61 8 93808563, Fax.: +61 8 93801005 (birger@chemie.fu-berlin.de)
Following a route recently described by Koritsanszky et al. [1] we havecalculated theoretical data sets for geometry optimized [2] model compounds. The
theoretical structure factors are fitted with the Hansen and Coppens multipole
model [3] using the XD program package [4] treating the theoretical Fe's as Fa's.
Starting from [1] a generalized scheme for a partitioning of any structure intotransferable atoms is proposed. These transferable atoms are called invarioms(from invariant atoms) and are similar in a transfer process from one molecule toanother because they mimic the same chemical environment with respect to thenearest neighbors of the atom of interest. To minimize the size of the modelcompounds the valences of the nearest neighbors of the atom of interest are
saturated with hydrogen atoms. This partitioning scheme is used to build up alibrary of multipole parameters , in a similar manner as realized by Pichon Pesme etal. [5] and successors for experimental data.
Amino acids and peptides consist of only 30 invarioms. The database usedhere already contains these 30 invarioms and an application to experimental data
as a test of the method will be presented. The test structure, WV * EtOH * TFA,
was recently determined in our lab. It crystallizes in the space group P2 1 , a =9.705, b = 19.270, c = 11.820 A and y= 100,26° with Z=2 and four independent
molecules in the asymmetric unit. The spherical R-factor using the independent
atom model is 4.2%. The structure is not suited for a high resolution data collection
I multipole refinement due to the four independent molecules in the asymmetricunit and the presence of trifluoracetic acid , but is an ideal test case for theapplication of a transfer of the theoretically obtained multi pole parameters.
The expected outcome is not only a lower R-factor. Using only the sphericalstructure the electrostatic potential as well as the dipole and multipole moments
can be calculated from the transferred aspherical electron density. This approach
could , if successful , be generalized to any crystal structure without a limit in thenumber of atoms.
·
References
I
Koritsanszky, T., Volkov, A. and Coppens, P. (2002) Acta Cryst. A58 , 464.
2
Gaussian 98, Revision A.11 .3, M. J. Frisch et al. , Gaussian, Inc., Pittsburgh PA,
2002.
3
Hansen, N. and Coppens, P. (1978) Acta Cryst. A34 , 909.
4
Koritsan szky, T., Howard , S., Richter, T., Su , Z., Mallinson , P. and Hansen , N. K.,
XD - A program package for Multipole Refinement and Analysis of Electron Densities
from Diffraction Data. User Manual. Freie Universitat Berlin , 1996.
Pichon Pesme, V., Lecomte, C. and Lachekar, H. (1995) J. Phys. Chern. 99, 16.
5Help from T. Koritsanszky for stru cture factor calculation is gratefully acknowledged.

314

SThP-06
THE NEW QUASI-LAUE DIFFRACTOMETER AT THE REPLACEMENTRESEARCH REACTOR
Wim T. Klooster
Bragg Institute, ANSTO , PMB 1, Menai , NSW 2234 , Australia(wim@ansto.gov.au)

The new single-crystal diffractometer for the Replacement Research
Reactor will be a quasi-Laue diffractometer, similar to VIVALDI at ILL, France. It
will be competitive with the best instruments currently available . Data collection
times for a normal structure determination will be less than a day , aconsiderable improvement on current data collection times , typically a few
weeks at HIFAR. Also , the crystal size needed for an experiment can as small
as about 0.1 mm 3 , opening up new research areas where it has proved difficult
to grow crystals sufficiently big (several mm 3 ) which are currently needed .
Another area of research opening up will be multiple temperature and/orpressure measurements.
This new instrument will be a useful tool to obtain structural information ina timely fashion , where x-rays do not provide enough detail.
The instrument will be on the end of a thermal supermirror guide , and weare exploring the possibility of enhancing the flux further by using a converging
guide section immediately before the instrument itself.
More detailed information on the instrument will be presented.

315

SThP-07
NEW IONIC MODEL POTENTIAL FOR SEMICONDUCTORS WITH
APPLICATION TO Si

Teiji Kobayasi ," and Hisashi Narab•General Education , College of Medical Sciences, Tohoku University, Sendai ,Miyagu Prov. 980-8575 , Japan; bDepartment of Systems and Information ,Hachinohe Institute of Technology (cobalt@clg .niigata-u.ac.jp)

A new ionic model potential for semiconductors is proposed , which
consists of a set of continuous exponential functions. Introduced damping andamplitude parameters into the model potential are to be treated as adjustable.
Unlike the ionic model potentials of the Heine-Abarenkov and Topp-Hopfield
types , the proposed model potential has no artificial sharp cut-off parameter forthe repulsive core-orthogonality condition and has continuous derivatives ofarbitrary orders . The reasons of the proposition are discussed in relation withlight metals where the ionic model potentials with the cut-off parameter work
successfully . In particular, an unphysical and artificial oscillation of the potential
form factor in high momentum region , which is introduced by the potential
discontinuity, will be discussed. The proposed model potential is applied toconstructing crystal potential of Si semiconductor and the adjustableparameters are determined so as to be consistent with the Si crystal pseudopotential of high quality by taking a valence electron dielectric screening effectinto account. The effectiveness of the proposed model potential is discussed by(1) comparing the calculated ionic energy levels of Si with experiments , (2)checking the consistency between the ionic and crystal potentials for Si , and so
on.

316

SThP-08
EFFECTS OF ELECTRON CORRELATION ON MAGNETIC COMPTONPROFILES OF Ni IN THE GW APPROXIMATION

Yasunori Kubo
Department of Physics , College of Humanities and Sciences , Nihon University,
Tokyo 156-8550 ( kubo@chs .nihon-u .ac.jp)

The magnetic Compton profiles (MCP's) are studied with the conventionalband theory based on the local-density approximation(LDA) and so-called GW
approximation (GWA) connected band theory. In the GWA , the basis sets ,eigen-energies and eigen-states generated by the full-potential linearized
augmented-plane wave method(FLAPW), are used.
Since the magnetic moment of Ni is 0.6 ,u e , which is about 4 times smaller
than that of Fe , it is not easy to measure MCP with good statistical accuracy.
However, recent MCP 's [1 ,2] using Storage-Ring have demonstrated
discrepancies between the experiments and conventional band calculations
using LOA in lower momentum region , where the Fermi surface structures andthe hybridization between the 3d- and s,p- electrons predominantly influence
the momentum distributions of magnetic electrons. The discrepancies are
examined from the point of view of electron correlation effects. The occupation
number densities N(k)'s are evaluated from a first-principle calculation of thespectral function within the GWA. The MCP's are calculated using the N(k)'s.
References
1
Dixon , M.A. G., Duffy , J. A. , Gardelis, S. , McCarthy, J. E. , Cooper, M. J. ,Dugdale , S. B. , Jarlborg , T. and Timms , D. N. (1998) J. Phys.: Condens.
Matter 10 , 2759-2771 .
2
Kakutani , Y. , Kubo , Y. , Koizumi , A. , Sakai , N. , Ahuja , B. L. and Sharma , B.
K. (2003) J. Phys. Soc. Jpn. 72, in print.

317

SThP-09
CHARGE DENSITY ANALYSIS AND DIPOLE MOMENT ENHANCEMENT IN
MNA (2-METHYL-4-NITROANILINE)

Andrew Whitten ,a Mark Spackman ,a Peter Turner,b Wim Klooster,c Ross Piltz,cand Masaru TachibanadaChemistry, School of Biological , Biomedical and Molecular Sciences ,University of New England , Armidale , NSW 2351 , Australia ; bSchool ofChemistry , University of Sydney, NSW 2006, Australia ; cBragg Institute,
Building 58 , ANSTO, PMB 1, Menai , NSW 2234, Australia ; dDepartment of
Physics , Yokohama City University, 22-2 , Seto , Kanazawa-ku , Yokohama , 2360027 , Japan (awhitten@une.edu .au)

MNA belongs to a class of substituted benzene derivatives, which possess
exceptional non-linear optical properties. Such compounds exhibit large
microscopic second order non-linear susceptibilities , and lack a centre ofsymmetry in the solid state. Another interesting property of these compounds isthe apparent enhancement of the dipole moment due to hydrogen bonding andgeneral crystal-field effects. For MNA, ab initio calculations of the free molecule
give values of the dipole moment of about 8.2 D,111 while in-crystal estimatesobtained from a previous charge density analysis are around 25(8) D,i21
suggesting a three-fold enhancement of this molecular property. This
experimental result has been widely cited , but whether the magnitude of thedipole moment enhancement exhibited there is reasonable is of some debate
because of difficulties encountered in the analysis of X-ray diffraction data for
non-centrosymmetric space groups ; the large experimental error associatedwith the value also raises questions about the ability of the multipole refinement
procedure to reliably retrieve such values.
To independently verify this important observation , and hopefully to
improve on the results obtained in the previous study , we are making use ofexperimental data that was unavailable a decade ago , including neutron
diffraction data collected on the four-circle diffractometer (2TANA) at HIFAR, as
well as charge density quality X-ray diffraction data collected on the Bruker
SMART 1000 CCD system at the University of Sydney , all at 100 K. We arealso performing Hartree-Fock CRYST AL98 calculations to aid in the analysis of
the experimental data , and for comparison with experimental results. We will
discuss the difficulty in obtaining sensible estimates of one-electron properties
for non-centrosymmetric compounds from multipole refinements , and present indetail the results obtained from this study.
References
I
Daniel , C . and Dupuis, M. (1990) Chern. Phys. Lett. 171 , 209 .
2
Howard , S. T., Hursthouse, M. B. , Lehmann , C. W., Mallinson , P. R. , andFrampton , C. S. (1992) J. Chern. Phys. 97 , 5616.

318

SThP-10
MOLECULAR ELECTRIC PROPERTIES USING HIRSHFELD SURFACES: A
NOVEL APPLICATION OF SURFACE INTEGRALSMark Spackman ," Andrew Whitten ," Joshua McKinnon ," Xiaoxiong Meng ," andChristopher Radfordb
8

Chemistry, School of Biological , Biomedical and Molecular Sciences,
University of New England , Armidale NSW 2351 , Australia ; bSchool ofMathematics, Statistics and Computer Sciences , University of New England ,Armidale NSW 2351 , Australia. (mspackma@une.edu.au)

The Hirshfeld surface was originally devised [1] as a novel partitioning ofmolecules in crystals , for the purpose of providing a simpler route to estimating
electric properties, especially dipole moments. of molecules in crystals. In thatoriginal communication dipole moments were presented for three small
molecules in crystals , using a rather crude numerical integration over thevolume inside the surfaces . We have recently taken advantage of thetrangulated nature of these surfaces to convert volume integrals to surface
integrals, using standard methods in vector calculus .
The method is based on that of Popelier, who has described in somedetail the computation of the atomic charge inside surfaces defined by thequantum theory of atoms in molecules (QTAM) [2] . This is quite astraightforward property to compute , and the relevant expression is (in atomic
units):
q=III p(r )dV = 4~ II (E n)dS
\1s

In this manner the net charge within the relevant surface can be obtainedby integration of the electric field projected onto the surface normal , summed
over the oriented surface. In a similar manner the dipole moment of the charge
distribution within the surface can be expressed in terms of two surface
integrals, one involving the electrostatic potential , and the other the electricfield ; second moments also require a volume integral , which is directly related
to the average of the electrostatic potential within the enclosed volume.
For integration over QTAM surfaces , Popelier employed a parametricrepresentation of the various surfaces. However, all of our work on Hirshfeld
surfaces [3] has taken advantage of their description as smooth isosurfaces of areadily defined weight function , and from this , their representation as
triangulated surfaces . A triangulated surface automatically provides a set of
surface points and their connectivity as triangles on the surface . From thisinformation , relevant electric properties are readily computed at all points on thesurface (from either theoretical - Gaussian98 or Crystal98 - or experimental Valray or XD- charge distributions). and surface normals are obtained trivially.
Results will be presented for dipole moments of a variety of molecules inmolecular crystals, and compared with relevant QTAM results.
References

I
2
3

M. A. Spackman and P. G. Byrom (1987) Chem. Phys. Lett., 267 , 215.
P. L.A. Popelier (2001) Theor. Chem. Ace., 105, 393 .
J. J. McKinnon , A. S. Mitchell & M.A. Spackman (1998) Chem. Commun .,2071 ; J. J. McKinnon, A. S. Mitchell & M. A. Spackman (1998) Chern. Eur.
J. , 4 , 2136 ; M. A. Spackman & J. J. McKinnon. CrystEngComm , 4 , 378.

319

SThP-11
STUDY OF ANISOTROPY IN MOMENTUM DENSITY OF COBALT
B. K. Sharma ," B. L. Ahuja ,b S. S. Asawa!," V. Purvia ," Y. Kakutani ,c A.
Koizumi ,c and N. Sakaic
aDepartment of Physics , University of Rajasthan , Jaipur 302015 , India ;bDepartment of Physics , College of Science Campus , M. L. Sukhadia
University, Udaipur 313001 , India; cGraduate School and Faculty of Science ,Himeji Institute of Technology, Aka-gun , Hyogo 678-1297 , Japan(bkrish@sancharnet.in)

The directional Compton profiles of hcp cobalt have been measured at
0.42 a.u . momentum resolution using synchrotron radiation at SPringS , Japan .
The measurement is compared with the available APW calculation of
Matsumoto et al [1]. It is seen that the APW calculation describes qualitatively
the anisotropy of the electron momentum distribution, which is influenced by the
Fermi surface topology . The lack of quantitative agreement between theoreticaland experimental anisotropies may be due to insufficient treatment of the
momentum component above 6.5 a.u. and electron-electron correlation effect.
The data points to the need for a better theoretical calculation incorporating theabove mentioned features .
References
I
Mastumoto, M., Tomimoto , K. and Wakoh , S. (1993) J. Phys. Soc. Jpn 62 ,2734 .

320

SThP-12
THE STUDY OF THE PHASES OF COWs UNDER THE APPLICATION OF
ELECTRIC FIELDS USING MULTIPLE X-RAY DIFFRACTION
Chao-Hung Du ." Mau-Tsu Tang ,b Yuri P. Stetsko,b.c Yen-Ru Lee,c J. -J. Leeb
and Shih-Lin Changb.c"Department of Physics , Tamkang University, Tamsui 25137 , Taiwan ;bSynchrotron Radiation Research Center, Hsinchu Science-Based Industrial
Park, Hsinchu 30077 , Taiwan; cDepartment of Physics , National Tsing Hua
University, Hsinchu 30043 , Taiwan (chd@mail.tku.edu .tw)

We report the electric field effects on the COWs' (charge density waves)phases in a quasi-one dimensional material Ko.3Mo03 using multiple x-ray
diffraction. K0 .3Mo0 3 undergoes a metallic-insulator transition due to theformation of charge density waves (COWs) at temperature Tcow - 180 K.
Conventionally , the dynamic behavior of the COWs have been widely studied
using the transport measurements , and the non-linear response to theapplication of electric fields exceeding the threshold value has been known tobe due to the deformation of the COWs' phases . The use of the multiple x-ray
diffraction allows us to directly probe the phases of the COW modulation ,further , we observed that the COWs' phases shifted under the application of anelectric field . We demonstrate that the use of multiple diffraction and theapplication of electric fields allow the direct observations of the deformation of
the COWs' phases.

321

SThP-13
CHARGE DENSITY STUDIES OF POLYMORPHIC ANTI-ULCER AGENTS.
THE APPLICABILITY OF THE ELECTROSTATIC POTENTIAL IN DRUG
DESIGN
Jacob Overgaard , Mark P. Waller, and David E. Hibbs
School of Chemistry, University of Sydney, NSW 2006 , Australia
Qacobo@chem.usyd .edu .au)
The electrostatic potential (EP) has been extensively employed in theprediction of a variety of condensed phase macroscopic properties fromth eo reti ca l calculations , and a quantitative approach ha s recently beensuggested based on a range of features of the EP on the molecular surface [1].
However , this method has so far been restricted to the gas-phase , thus
excluding the effect of intermolecular interactions . Nonetheless , the EP is ofparamount importance in the understanding of drug-receptor interactions. Thus ,an experimental determination of the EP including the effects of intermolecularinteractions is potentially of great use in rational drug design.
In the present work we will outline the results of a theoretical andexperimental charge density (CD) study of both known polymorphs (A and B) of
the histamine H2-receptor antagonist, famotidine (see Figure) [2]. The CD isdetermined from a combination of X-ray and neutron diffraction data collected at
100 K, using the Hansen -Coppens multi pole model [3] . We will focus on acomparison of the experimental and th eo retical COs and describe th esimilarities in the COs of the two polymorphic forms of famotidine. In particular,
we will discuss the observed differences in the experimental EPs of the twopolymorphs , respectively, in relation to their individual abilities to act as antiulcer agents . This work represents the preliminary steps towards a moregeneral description of a number of drug types using combined theoretical andexperimental charge density studies.

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Famotidine A

References
I
Politzer, P. and Murray , J. S. (2002) Theor. Chern. Ace. 108, 134-142.
2
Ferenczy , G. G., Parkanyi , L. J., Angyan , G. , Kalman , A. and Hegedus , B.
(2000) J. Mol. Struct. {Theochem) 503 , 73-79.
J
Hansen, N. K. and Coppens, P. (1979) Acta Cryst. Sect. A 39 , 909-921.

322

SThP-14
CHARGE DENSITY ANALYSIS OF p-Si3N4
Doug du Boulay," Nobuo lshizawa ," and Victor Streltsovb"Materials and Structures Laboratory, Tokyo Institute of Technology, Nagatsuta ,Midori-Ku Japan ; bCSIRO HSN , 343 Royal Parade, Parkville VIC 3052,
Australia (ddb@R3401 .msl.titech.ac.jp)
f:l-S bN4 is important in both electronics and mechanical fabricationsindustries because of its intrinsic hardness and resistance to oxidation . Despitewidespread use its structure is still somewhat controversial. The controversy
concerns the existence , or not, of mirror planes normal to the hexagonal 53screw axes which decide the issue of centricity versus acentricity.
Using BL-14A of the Photon Factory synchrotron , Tsukuba , Japan , threelargely absorption and extinction free 0.75A data sets were measured at threedifferent temperatures , 295K , 200K and 150K. We found no compelling,
reproducible evidence to support the acentric model and therefore believe that
the P6:/m symmetry is preferable , despite earlier conflicting reports[1-3] . An
electron microscopy study has subsequently supported these conclusions[4] .
With greater faith in our experiments we have applied multipole population andtopological analyses[5] . These analyses agree largely with more theoreticalmodeling derived from Density Functional Theory using the Linear Augmented
Plain Wave approach as implemented in Wien2k[6] .
The results of these analyses are consistent regarding the magnitude andtopography of the charge density along the interatomic interactions. The
coordination geometries of two independent NSi 3 groups is trigonal planar,
while that of the SiN 4 group is tetrahedral. The three symmetry distinct Si-N
bonds exhibit pronounced charge density accumulation near the bondmidpoints , characteristic of covalent sp 2 and sp 3 hybridization schemes for N
and Si respectively.
Topological analysis of the electron density revealed the existence ofadditional (3,-1) critical points at the high symmetry (-6) sites midway along the
2.9A N-N contacts. This feature was also reproduced by OFT calculations. The
magnitude of the Laplacian of the density at the N-N critical point is around 20
times smaller than for the other (3 ,-1) critical points along the N-Si shared
1electron interactions , with the local electron density at that point around / 4 ofthat appearing in the N-Si bonds. This could be interpreted as evidence of weak
N-N shared electron interactions , i.e. partial covalent bonding . By comparison ,all other Nand Si bonds are of order 1.73A in length.
References
I
Banda , Y. (1983) Acta Cryst. B39 , 185-189.
2
Grun , R. (1979) Acta Cryst. B35, 800-804.
3
Schneider, J., Frey , F. , Johnson, N. and Laschke , K. (1994) , Zeit. fur Krist.
209 , 328-333.
4
Tsuda , K. (2002) private communication .
5
Blaha , P., Schwarz , K., Madsen , G. K. H. , Kvasnicka, D. and Luitz, J.,
WEIN2k , (Karl heinz Schwarz Tech. Universitat Wien , Austria (2001) ISBN
3-9501031-1-2 .
6
Stewart , R. F., Spackman , M. A. and Flensburg, C. (1998) VALRAY98 .

323

SThP-15
CHARGE DENSITY STUDY UNDER HIGH PRESSURE

Makoto Sakata ," Takafumi ltsubo, 8 Eiji Nishibori ,8 Yutakata Moritomo,8Norimichi Kojima ,b Yasuo Ohishi ,c and Masaki Takataa.c8Department of Applied Physics, Nagoya University, Chikusa , Nagoya 4648603 , Japan ; bGraduate School of Arts and Science, University of Tokyo , Tokyo
153-8902, Japan; cJapan Synchrotron Research Institute, Kouto, Mikazuki-cho ,Sayo-gun , Hyougo 679-5198 , Japan (sakata@cc.nagoya-u.ac.jp)

It is very well known that physical properties of materials can be drasticallychanged by applying pressure , such as emergence of superconductivity ofladder compounds. It is also very common that materials undergo structuralphase transitions when they start to show very different physical properties
under high pressure . It is , therefore , highly desirable to determine structuralchanges accurately , preferably at electron density level , under high pressure. Itis , however, not easy task to carry out accurate structure analysis under highpressure because of experimental restrictions, which prevent from the collectionof an accurate X-ray diffraction data. The present state-of-art of structurerefinements under high pressure is far from matured.
In order to produce high-pressure conditions , we have to use highpressure cell, such as diamond anvil cell (DAC), which limit the amount ofspecimen to be used in the X-ray diffraction experiment to micro-gram order.
Under such a condition , there is no doubt that third generation SR source has agreat advantage. In this study, an accurate structural analysis of Cs 2Au 2Br6 byusing SR powder data collected at BL 1OXU , Spring-S will be described. Goldatoms in Cs 2Au2Br6 are a mixed valence state at ambient pressure .
In this study, a DAC with large culet is used to have the powder specimen
as much as possible. Because of this , the highest pressure to be reached by
the DAC has to be limited to a few tenth GPa. The specimen was oscillated
about 3.5 degree at all the pressure points , where the experiments were done.
The oscillation was very effective to have homogeneous intensities along
Debye ring , which is essential for the accurate structure analysis like charge
density study. The collected data at 2.2GPa and 8.1Gpa are analysed by
MEM/ Rietveld analysis[1] to obtain the expe rimental charge density
distributions.
In the Rietveld refinements , which is done as a preliminary analysis before
MEM , the R-factors based on integrated Bragg intensities became as small as
1.28% and 1.05% at 2.2GPa and 8.1 % GPa , respectively . It has to be admitted
that the refinements is done satisfactorily to proceed further MEM analysis.
From the MEM charge density map obtained in this study, it is revealed that the
network structure is formed by covalency between Au and Br atoms at 8.1 GPa ,while at 2.2GPa Au and Br atoms form clusters. It is also recognised that themixed valence state of Au at 2.2GPa transfers to the charge order states of Au+
and Au3+ at 8.1 GPa. The present resu lts may represent the present state-of-art
of charge density studies under high pressure.
References
I
Takata, M., Nishibori , E. and Sakata, M. (2001) Z. Kristallogr. 216, 71 .

324

SThP-16
FERMI SURFACE OF A SHAPE MEMORY ALLOY OF TiNi

N. Shiotani ." I. Matsumoto," H. Kawata ," J. Katsuyama ,b M. Mizuno,b
H. Araki ,b andY. Shiraib"Photon Factory, KEK, Tsukuba , lbaraki 305-0801 , Japan ; bDepartment ofMaterials Science and Engineering , Osaka University, Suita , Osaka 565-0871 ,Japan (shiotani@post.kek.jp)

The TA 2 [11 0] phonon anomaly observed in the pre-martensitic phase of
the equiatomic intermetallic compound , TiNi , by inelastic neutron scattering has
suggested nesting of the Fermi surface. So far, however, no direct observationof the Fermi surface has been reported.
We study the Fermi surface of Ti4a9Ni 5u via high resolution Compton
scattering . The Compton profiles are measured along 28 directions in theirreducible orientation triangle of cubic symmetry. Using Fourier-Bessel
reconstruction scheme the 3-dimensional electron momentum density is
obtained. The LCW-folding procedure is employed to map out the occupation
number density in k-space. The results are compared with band theoreticalpredictions by Kakeshita et al. [1) and Zhao and Harmon [2) .
References
1
Kakeshita , T., Fukuda , T. and Saburi , T . (2000) Sci. Tech. Adv. Mat. 1, 63.
2Zhao, G. L. and Harmon , B. N. (1993) Phys. Rev. B48, 2031.

325

SThP-17
PRECISE CHARGE DENSITY STUDY OF CYTOCHROME c-553 BY MAXIMUMENTROPY METHOD

Masaki Takata,a,b Kenichi Kato,b Hiroshi Tanaka ,c Atsushi Nakagawa ,dand Makoto Sakata 880epartment of Applied Physics , Nagoya University, Nagoya 464-8603, Japan;
bJapan Synchrotron Radiation Research Institute, Hyogo 679-5198 , Japan ;coepartment of Material Science , Shimane University, Mtasue 690-8504 ,Japan; dThe Institute for Protein Research , Osaka University, Suita 565-0871 ,Japan (takatama@spring8.or.jp)

Structures of various protein molecules are now studied extensively to
explore the structural basis of the protein function. Therefore , th e seve ral
experimental and analytical techniques have been developed in order to get a
hig h-resolution crystallographic structure of protein crystal. However, most of
the studies have been carried out for the atomic arrangement. In order to havea better and deeper understanding for functions and properties of the protein
molecule, a precise charge density study is required to reveal bonding nature ofmolecule especially for an active segment. Recently , we have developed a newprogram of the Maximum Entropy Method, ENIGMA(Eiectron and Nuclear
Image Generator by Max-ent Analysis)[1], for the charge density study of hugesystems, such as proteins and polymers. By ENIGMA , we tackled cha rge
density study of cytochrome c-553 , and revealed precise charge density
showing characteristic bonding nature of Heme group.
In the present study, we have employed synchrotron radiation single
crystal data of cytochrome c-553 , of which structure was solved by the multiple
wavelength anomalous diffraction method [2] . The reliab ility factor of theobtained charge density is 2.4%, which is far beyond the value, 19.6%, of theprevious conventional structure determination . The obtained charge density
clearly exhibits the covalent bonding networks of atoms and the characteristic
anisotropy of the Fe-N coordinate bonds in the heme group. Furthermore , theability of the structure prediction by MEM revealed the solvent water molecule
image in the crystal without assuming the existence of water molecule. The
present result shall open the door to an accurate charge density study for the
structure-function relationship of proteins .
ReferencesI
H.Tanaka, et al. (2002) J.Appl. Cryst. 35, 282-286 .
2
A.Nakagawa , et al. (1990) J.Biochem. 108, 701-703.

326

SThP-18
AN EXPERIMENTAL CHARGE DENSITY STUDY OF SINGLE-COMPONENTMOLECULAR METALS, Ni(TMDT)2 AND Au(TMDT)2.
E. Nishibori," Y . Fujishiro ," M. Takata ," M. Sakata ," A. Kobayashi ,b W. Suzuki ,bE. Fujiwara ,b H. Tanaka ,c and H. Kobayashid•oepartment of Applied Physics, Nagoya University, Nagoya 464-8603 , Japan;bResearch Centre for Spectro-chemistry , Graduate School of Science , The
University of Tokyo, Hongo, Bunkyo-ku , Tokyo 113-0033, Japan;
cNanotechnology Research Institute, National Institute of Advanced Industrial
Science and Technology, Umezono, Tsukuba 305-8568 , Japan ; dlnstitute for
Molecular Science and CREST, Myodaiji, Okazaki 444-8585, Japan(eiji@mcr.nuap. nagoya-u.ac.jp)
Recently, the molecular conductors, which consist of single-component
molecules, have been attracted much interests, because of metallic behavior
under certain circumstances. First metallic single-component molecule
confirmed by the conductivity measurement was Ni(tmdt}2 (tmdt: tri-methylenetetra-thiafulvalence-dithiolate), which showed metallic behavior at very low
temperature, i.e. below 0.6K[1]. After discovery of this material, similar singlecomponent molecules with same extended-TTF (tetra-thiafulvalene) ligands
were synthesized, such as Cu(tmdt}2 and Au(tmdt}2. Surprisingly enough ,Au(tmdt} 2 showed metallic behavior at room temperature. The conductivity ofAu(tmdt}2 was 15Scm·1 at room temperature[2] . This value was over ten times
1smaller than that of Ni(tmdt} 2(200Scm· }[1]. Au(tmdt)2 and Ni(tmdt)2 are isostructure substances[1 ,2]. It would, therefore , be very important to study theelectron density level structure to have better understanding of the difference ofconductivity. In this study , the experimental charge density distributions of bothAu(tmdt)2 and Ni(tmdt)2 were derived by the Maximum Entropy Method(MEM)
using synchrotron radiation(SR) powder data.
SR powder experiment were carried out by the large Debye-Scherrer
camera installed at BL02B2, Spring-S for both Ni(tmdt)2 and Au(tmdt}2. The
wavelength of incident X-ray was 1.0A, which is rather long wavelength as third
generation SR source . The reason for choosing this wavelength is to try to havebetter peak-separations of Bragg reflections. The collected data were analysed
by MEM/Rietveld method(3] to derive experimental charge densities , whichallows us to investigate the difference of charge densities of these compounds.
From the comparison of obtained charge densities, it was found that there are
distinct differences in Metal-S bond . The minimum electron density between AuS bond were 0.18[e/ A 3] in Au(tmdt)2, which is much lower than that of Ni-S in
Ni(tmdt)2, i.e. 0.33[e/A 3] . It was also found that electron density of TTF ligands
in Au(tmdt}2 was elongated toward the direction of adjacent molecule. Thistendency was not seen in the case of Ni(tmdt)2. These differences of charge
density level structures would be related to the different behaviours of theelectronic conductivity of these compounds.
References
I
Tanaka , H. et al. (2001) Science 291 , 285-287 .
2Suzuki , W. et al. (2003) J. Am. Chem. Soc. , 125, 1486-1487.
3
Takata , M. et al. (1995) Nature 377,46-49.

327

SThP-19
MUL TIPOLE REFINEMENTS WITH RIGID-BOND AND LINK CONSTRAINTS

T. Koritsanszky
Department of Chemistry, Middle Tennessee State University, TN , USA(tkoritsa@mtsu .edu)

Controlling an often over-parametrized multipole refinement is an ultimate
but seldom achieved goal. In this respect , model restrictions supporting thephysically most significant least-squares solution , are always helpful. While
preconceptions on the static density are routinely invoked (chemical and local
symmetries), atomic anisotropic displacement parameters (ADP) are usuallytreated as free variables disregarding supportive information accessible fromspectroscopic data and theoretical calculations .
This presentation describes easy-to-handle constraints applied to theshifts of ADP 's that result in a linear least-squares cycle . The core property
considered is the difference mean-squares displacement amplitude (DMSDA)
matrix[1] corresponding to the intra-molecular vibrational modes that are readily
obtained from theoretical force fields for geometry-optimized , isolated
molecules:

A"" =r~o (U " -U n) •·""
where A and B refers to the nuclei linked and rAs is the interatomic unit vector.
The refinement starts with the calculated intra-molecular ADP 's(transformed to the crystal system) whose shifts are constrained , after each
least-squares cycle, to yield a vanishing DMSDA matrix (all links are assumed
to be rigid) . The linearly independent links are derived via singular value
decomposition of the matrix of constraints . This means , in general , 6N-M
constraints , where N is the number of atoms in the molecule and M is thenumber of independent tensor elements of the rigid-body model[2] . The
procedure described corresponds to a fit of the T, L and S tensors against thestructure factors in the course of which the contributions of the intra-molecularmodes to the ADP 's are preserved . The method has several extra features : itprovides rigid-body ADP 's free of contaminations from intra -molecularvibrations, eliminates singularities and assigns ADP 's also to hydrogen atoms.
An alternative approach starts the refinement with a set of rigid-body
ADP 's (yielding vanishing DMSDA matrix) and invokes a partial set of rigid-link
constraints , only those that are consistent with a desired segmentation of themolecule into rigid atomic groups. This refinement corresponds to a fit of ADP'sof the segmented rigid-body model to the structure factors.
Both options have been implemented into the new release of XD . Resultsfrom small molecule refinements are presented .
References1
Hirshfeld, F. L. (1976) Acta Crystallogr. A32, 239.
2
Schomaker, V. and Trueblood , K. N. (1968) Acta Crystallogr. 824, 63 .

328

SThP-20
STRUCTURAL RELATIONSHIP OF p-SODIUM (X=0.33) AND pi-COPPER(X=0.65) VANADIUM BRONZES MxV20s

Ruslan Ozerov ," Victor Streltsov ,b and Alexander Sobolevb"Mendeleev University of Chemical Technology of Russia , 125047 Moscow,
Russia ; bCrystallography Centre and Department of Chemistry, The Universityof Western Australia, Nedlands 6907 , Western Australia, Australia(RPOzerov@www.mail.ru) and (Victor.Streltsov@csiro .au)

The W-copper vanadium bronze single crystal structure Cuo.ssV20 s has
been studied at room , 75, and 9K temperatures and compared with the ~ ­sodium vanadium bronze Na 0.33 V20 5 structure (Ozerov et al 2001 ).
Temperature changes have not significantly affected the crystal structure.
The centrosymmetric space group C2/m was accepted for the crystal structurestudied. However, there are three space groups with the same extinction laws:
centrosymmetric C2/m and two non-centrosymmetric Cm and C2 . To ourknowledge there are no information on possible ferroelectricity in this compoundallowing to make the choice between them .
It was found that the copper atoms in the C2/m space group, contrary to
the sodium compound , occupy three positions: Cu1 is in 4(i) position withcoordinates x=0 .541 , y=O and z =0 .344 and Cu2 atoms in 8U) position withcoordinates x=0 .529 , y=0 .038 and z =0 ,358 . In the sodium compound , the Na
atoms occupy only half of 4(i) positions in ordered or disordered manner whilein the copper compound Cu atoms are distributed over three positions . Similar
triple splitting of the copper atoms positioning in ED maps in copper bronze has
been found by Kato et al, (1989). However these authors attributed it to theanharmonicity of the thermal vibration of the copper atoms. The splitting of the
Cu position observed presently has been well confirmed at 9K in our studies.
This suggests that distribution of copper atoms among three positions (one Cu1
and two Cu2) is rather static than dynamical one.
References
Kato , K. , et al. (1989) Acta Cryst. C45 , 1845-1847.
I
Ozerov, R.P ., et al. (2001) Acta Cryst. 857 , 244-250.
2

329

SThP-21
VALENCE STATE OF VANADIUM ATOMS IN ji-NaxV20s BRONZE

Ruslan P. Ozerov ." Alexandra A. Alexa ." and Victor A. Streltsovb
aMendeleev University of Chemical Technology , Miusskaya Sq. 9, Moscow
125047, Russia ; bCSIRO HSN , Parkville Vic 3052 , Australia (rpozerov@mail.ru)

There are three types of vanadium atoms (V1 , V2 and V3) in the crystal
structure of ~-phase of alkali vanadium bronze M0 .3N 20 5 (M=Na , K and someother ions) [1-2] . They form a rigid oxygen-vanadium framework with alkali
atoms disposed in the channels. It is well known that the two types of oxygen
polyhedra around V1 and V2 atoms are nearly regular octahedra , however thethird, around V3 atom , is strongly deformed resembling a trigonal bi-pyramid.
There is an intriguing question concerning the valence states of the Vatoms in the structure which determine many properties of this crystal. It issuggested that one electron of the alkali atom is moved over to vanadium
atom(s) influencing the change of their valence state. The question is to which
vanadium atom(s) the electron is transferred . An attempt has been maderecently to use the multipole model in the accurate crystal structure
investigation of the Na-V-bronze [3] . However, the precision was not enough tomake a definite conclusion .
The aim of this study is to apply the band-valence method to the problem.
This method suggests the definite valence state to the central atom of theoxygen polyhedron on the base of the examination of the Me-0 distances [4-5].
Using the valence band theory the valence state of all three vanadium atoms for
Na 0286 V20 5 have been calculated and the results be discussed.
There were no unambiguous evaluations of the method accuracy.
Moreover, one should notice that the results strongly depend on some values
chosen a priory. Therefore , we can conclude that in this respect the most useful
are the relative valences values of several ions in the same compound (seetable 1) but not their absolute values .
References
I
Wadsley , A. D. (1955) Acta Cryst. 8, 695-699 .
2Ozerov, R. P., Gol'der, G. A. , and Zhdanov , G. S. (1957) Kristallogr. 2 ,217-225 .
3
Ozerov, R . P ., Streltsov , V . A. , Sobolev , A. N. , Figgis , B. N. and Volkov , V .
L. (2001) Acta Cryst. 8 57 , 244-250 .
4
Brese , N. E. and O'Keeffe , M. 0 . (1991)Acta Cryst. 847 , 192-197.

330

SThP-22
DEVELOPMENT OF MEASURING MAGNETIC COMPTON PROFILES BYGRAZING INCIDENT GEOMETRY
Hiroshi Sakurai ,a Fumitake ltoh ," Minoru Ota ,a Katsuyoshi Takano,b Xioxi Liu,band Hiroshi Kawatac
8

Dept. Electronic Engineering , Gunma University, Kiryu , Gunma 376-8515,
Japan; bSVBL , Gunma University, Kiryu , Gunma 376-8515 , Japan; clnst.
Material Structure Science, KEK, Tsukuba , lbaraki 305-0801, Japan(sakuraih@el.gunma- u.ac.jp)

Recent nano-structure in magnetic thin films becomes important for data
storage devices such as MR head and perpendicular anisotropic media . A
magnetic Compton profile (MCP) is agood ca ndidate to measure thewavefunction of nano-structured films . However, it is difficult to measure the
MCP's of the thin film because of strong scattering from substrates.
We have suggested to measuring MCP 's by grazing incident geometry,and succeeded in measuring a thin Fe film with thickness of 200nm on a thi ck
glass substrate as shown in Figure .
MCP measurements of a multilayer (Pd/Fe) and granularmaterials(MgF2/Fe) are under way.

s~~~~;.~~~X rays,-'l l~a r

51i I

.. -~

SSil

...__.

· · -·· ··D--

D•·D -··I on

Inc idPn l.

X 1·ay( •I:JkeV)

Pro nl. sli tchamber

Elec l.r ic
nagnc l.

lx lO ~J 6 .-----,~-----,

.f

0.8
0.6

]

0.4

'

Fe 200nm

i~\

~ 0.2

10

0.1
!J.1 degrec
Figttr('

331

SThP-23
MAGNETIC COMPTON PROFILES OF MAGNETIC THIN FILMS AND
ANISOTROPY OF Co/Pd MULTILAYER
M. Ota ," H. Sakurai ," F. ltoh ," M. ltou ,b andY. Sakuraib•oepartment of Electronic Engineering , Gunma Univ., Japan , bSPring-8 , Japan(harasawakoike@excite.co.jp)

Magnetic Compton scattering is a good candidate to probe the electronic
structures. However there are few measurements of thin films because ofstrong scattering from substrate . In this study we have succeeded in observing
the magnetic Compton profile of magnetic thin film with substrate and theanisotropy of Co/Pd multilayer for the first time .
Fe 1~m was sputtered on the polyethylene terephtalate (PET) film with
4~m thickness. ( Co(0.8nm)/Pd(1.6nm) )417 multilayer with 1 ~m was alsofabricated on the PET film. The films were folded in 16 to increase the effective
volume . Magnetic Compton profiles of these samples were measured at thehigh-energy beamline BL08Wat the SPring-8, Japan . The incident X-ray energy
was 174keV and the scattering angle was 175.8 degree. The incident beam andapplied field (2 .5T) were parallel or perpendicular to the sample plane.
Figure (1-a) shows magnetic Compton profiles of Fe 1~m sample on PET
substrate together with Fe 10~m reference sample . Figure (1-b) showsdifferential profile of Figure (1-a). The difference is close to about 0. This result
demonstrates that the measurement of magnetic Compton profiles in magnetic
thin films is possible .
Figure (2-a) shows anisotropy of magnetic Compton profiles on(Co(0.8nm)/Pd(1.6nm) )417 multilayer sample. Figure (2-b) shows differential
profile of Figure (2-a). The difference is remarkable in the region of Pz<2(a.u.).
This suggests that the da states of Co 3d-band is responsible for the
anisotropy. Further theoretical calculations are in progress .
ma •netic Compton pro fi l~s·

F~ I 0 ~~ m rd~ r~n c .: :s..1 m pll.'
F~ I p m on PET sub:' tmt.:•

in pl a n ~out o r pbth.'

10

">;L

! 0. 1-0. 1

F.: I Op m-1 pm

0. 1

-Q. I

( 1-b)
10

6

p, lrL.u.J

332

10

SThP-24
THE ELECTRON DENSITY TOPOLOGY CHANGES DUE TO THE PHASE
TRANSITION IN KmNF 3

Yury V. Ivanov, and Kiyoaki Tanaka
Department of Material Science and Engineering, Nagoya Institute ofTechnology, Gokiso-cho, Showa-ku , Nagoya 466-8555, Japan(yury@tana.mse.nitech.ac.jp)
Three high-precision X-ray diffraction experiments (MoK", T=190 , 240 and
298K) for cubic perovskite potassium manganese trifluoride , KMnF 3 , werecarried out. The data obtained were approximated by Hansen-Coppens
multipole model expanded up to hexadecupoles [1], the anharmonicity of atomic
displacements up to 4-th level was considered . Figures of merit were:R( fFf)=0.0060 , Rw([Ff)=0.0086 , 5=0.99 (for T=190K) ; R( fFf)=0 .0065 ,Rw([Ff)=0.0089, 5=1.00 (for T=240K); R( fFf)=0.0053 , Rw([Ff)=0.0071 , 5=0.99 (forT=298K).
The maps of the model total static electron densities (ED) were calculated ,and ED topological analysis was performed. At room temperature the ED
exhibits 6 symmetry-equivalent bond critical points (CPs) on Mn-F lines and 12
on K-F lines. Thus, geometrical and topological coordination numbers of Mn
and K atoms are the same: 6 and 12, correspondingly. The shapes of atoms in
KMnF 3 defined by zero-flux surfaces in the gradient of ED are far fromspherical. The ED basin of Mn atom separates the basins of neighboring F
atoms in spite of the fact that F-F distance is the same as the K-F one . So ,fluorine atom forms the bond paths with two Mn and four K atoms. Thus , it's
topological coordination number is six , whereas geometrical coordination
number is 12. At lower temperature the formation and strengthening of a new
Mn-K bond path is observed. The topological coordination numbers become 20
and 14 for K and Mn , respectively. The weakening of K-F interaction issimultaneously observed.
The consideration of atomic displacements detects that the probability
density function (PDF) of the F atom has single maximum at 298K and four
maxima at 190K. So , fluorine position is split towards structural holes with theshift of 0.2A. These pictures are in a good agreement with existence of point ofphase transition at 186K. The crystal structure changes from Pm3m to 14/mcm,
it can be described as a tilting of MnFs octahedron about c axis.
The ED values and curvatures at the bond CPs in KMnF 3 indicate theclosed-shell type interactions between pairs K-F and Mn-K, whereas Mn-F bondcan be considered as an intermediate type.
The topology of the electrostatic potentials (ESP) was studied as well. The
pattern of (3 ,-1) CPs doesn 't depend on temperature . These CPs were found on
Mn-F, K-F , Mn-K, and K-K lines. Three of them correspond to the bond CPs in
the ED , while the last appeared on the same points , where the global minimumin the ED exists . The bonded radii of K and Mn on cation-anion bonds derived
from the ESP are vastly larger than those derived from ED . The fluorine anions
show reverse picture. Thus, in terms of ESP the conventional concept of crystal
structures depicting arrangement of small cations in cavities between large
adjoining anions isn 't justified. The notion about a cationic grid as a basis of
structure is more adequate here.
Reference
I
Hansen, N. K. and Coppens , P. (1978) Acta Cryst. A34 , 909-921.

333

SThP-25
STRUCTURE ANALYSIS OF GAS MOLECULES ADSORBED IN THE
NANOCHANNEL OF A COORDINATION POLYMER BY THE
MEM/RIETVELD METHOD
Yoshiki Kubota ." Masaki Takata ,b,c Makoto Sakata ,b Ryo Kitaura,d Ryotaro
Matsuda,d Susumu Kitagawa ,d Tatsuo Kobayashi ,8 Kouichi Kindo ,8 Yoshimi Mita,'
Akira Matsuo,8 Michihiro Kobayashi,' Ho-Chol Chang ,d Tadashi Oszawa, 8 andMegumi Suzuki'•oept. of Environmental Sciences, Osaka Women 's University, Osaka 590-0035,
Japan; bDept. of Applied Physics, Nagoya University; cJASRI/SPring-8; dDept. ofSynthetic Chemistry and Biological Chemistry, Kyoto University; 8 KYOKUGEN;'Dept. of Physical Science, Osaka University, Japan (kubotay@center.osakawu.ac.jp)
Recently, various coordination polymers with uniform ordered nanochannels
were successfully synthesized by the combination of metal ions and organic
molecules. Many of these compounds are found to have extremely highperformance gas adsorption and are expected to be promising gas storage
materials. So far, adsorbed gas molecules were thought to be trapped in theordered nanochannels of the material. However, there is no structural evidence forthe trapped gas molecule position inside the micropore. Thus, in order todetermine the trapped gas molecule position and structure within the material , wehave done in-situ synchrotron radiation powder diffraction experiment and revealed
the formation of a one-dimensional array of gas molecules along the nanochannels
by the MEM/Rietveld analysis.
The sample used in the present study is [Cu 2(pzdc) 2(pyz)]n (pzdc=pyrazine2,3-dicarboxylate, pyz=pyrazine), which has a pillared layer structure with 1D
nanochannels with dimensions of about 4 x 6 A (CPL-1 :coordination ploymer 1
with pillared layer structure). The synchrotron powder diffraction data was collectedby the large Debye-Scherrer camera installed at SPring-8 BL02B2. The powder
sample was sealed in glass capillary. The gas import tube is attached to thegoniometer head to fill 0 2 gas in capillary. The gas adsorption is controlled bylowering the temperature not by the gas pressure. The data measurement was
carried out from 300K to 90K under 80kPa 0 2 pressure. The fundamental crystal
structure of CPL-1 had been reported by single crystal X-ray structure analysis.
The powder diffraction pattern from 300K to 150K is almost the same with that of
the reported structure. However, we investigated the dramatic changes ofdiffraction pattern at 130K which should be due to the 0 2 molecule adsorption. In
the first Rietveld analysis of the 90K data, we started the analysis with thefundamental structure of CPL-1 without assuming 0 2 molecules. The reliability
factors based on the powder pattern, Rwp and the integrated intensities, R1 were
18.5% and 54.2% , respectively. However, the MEM charge density visualized thedensity like 0 2 molecules in the middle of the nanochannels. According to the
MEM charge density, we determined the structure model of the CPL-1 adsorbing
0 2 gas molecule. The Rwp and R1for the Rietveld analysis with the final structure
model were improved to be 2.1 % and 3.9%, respectively. In the MEM charge
density, the dumbbell shaped electron distribution was clearly observed in the
middle of the nanochannels. The charge of the distribution was estimated to bealmost 16e indicating no charge transfer from the 0 2 molecule to CPL-1 , whichmeans 0 2 gas was physisorbed to CPL-1. And , we found adsorbed 0 2 molecules
form one dimensional array along nanochannels. The details of the determined
structure and novel characteristic magnetic property caused by 0 2 adsorption will
be presented.

334

SThP-26
MOMENTUM TRANSFER DEPENDENCE OF X-RAY RAMAN SCATTERING
AT THE BERYLLIUM K-EDGE
M. Volmer." C. Sternemann ,8 J. A. Soininen,b.c H. Nagasawa ,d M. Paulus .a H.
Enkisch ,8 G. Schmidt." M. Tolan ,8 and W . Schi.ilke 88lnstitute of Physics , University of Dortmund , D-44221 Dortmund , Germany;bDepartment of Physics , University of Washington , Seattle , Washington 98195,
USA; cOpticaiTechnology Division , National Institute of Standards andTechnology, Gathersburg , Maryland 20899 , USA; dFaculty of Economics , Seikei
University , Tokyo , 180-8633, Japan ; "DELTA, University of Dortmund , D-44221
Dortmund , Germany( schenkel@physik.uni-dortmu nd .de)

We studied the Beryllium K-edge using non-resonant x-ray Raman
scattering at different momentum transfers , thus probing the unoccupied densityof states with access to different symmetries of the final states of the excitedelectrons . We measured data for a Be polycrystal as well as for a single crystal
with momentum transfer both parallel and perpendicular to the c-axis. The
measurements have been carried out at the superconducting wiggler beamline
SAW2 of the DELTA synchrotron [1] making use of the standard IXSS setup [2].
Energy loss spectra were measured at momentum transfers q=0 .64 (1 .27) a.u.
where the dipole approximation is appropriate to describe the excitation process
so that 1s ~ p transitions dominate the x-ray Raman scattering cross section. Bychanging the scattering angle, q has been increased up to 4.78 a.u. making
1s~ s transitions possible, resulting in a strong change in shape of the K-edgeenergy loss spectra . Additionally the single crystal spectra show distinct
differences for a momentum transfer parallel and a momentum transfer
perpend icular to the c-axis at low q. This directional dependence vanishes athigher q.
The experimental data are compared with first principles calculations
modeling x-ray Raman scattering and its momentum transfer dependence [3-4] .

References
I
Dortmund Electron Accelerator (DELTA) , University of Dortmund, MariaGoeppert-Mayer-Str. 2, D-44221 Dortmund , Germany(www.delta. uni-dortmund.de).
2
Berthold, A., Mourikis, S., Schmitz, J. R. , Schulke , W . and SchulteSchrepping , H. (1992) Nucl. lnstr. Methods A 317 , 373.
Soininen, J. A. and Shirley, E. L. (2001) Phys. Rev. B 64 , 165112.
3
Soininen , J. A. , Hamalainen , K., Caliebe, W . A., Kao , C. -C . and Shirley,
4E. L. (2001) J. Phys.: Condens. Matter13 , 8039.

335

SThP-27
CONSTRAINED DENSITY FUNCTIONAL THEORY USING X-RAY
DIFFRACTION DATA

Daniel J. Grimwood
Chemistry, School of Biomedical & Chemical Sciences , University of Western
Australia , Crawley, WA 6009 , Australia (reaper@theochem .uwa.edu.au)
A constrained density functional method using X-ray diffraction data isdeveloped. The method is applied to N20 4. A comparison is made with theconstrained Hartree-Fock method [1], to determine which method is better
suited to reproduce experimental structure factors.
References
I
Jayatilaka , D. and Grimwood , D. J. (2001) Acta Cryst. A57 , 76-86.

336

SThP-28
A WAVEFUNCTION CONSTRAINED JOINTLY TO X-RAY AND POLARISED
NEUTRON DIFFRACTION DATA FOR THE Cs 3 CoCI 5 CRYSTAL

Dylan Jayatilaka
Chemistry, School of Biomedical & Chemical Sciences, University of Western
Australia , Crawley, WA 6009 , Australia (dylan@theochm .uwa.edu .au)

The experimental wavefunction technique [1 ,2] is extended , to implement
the joint refinement of X-ray and Polarised Neutron Diffraction (PND) data .
Results are presented for the CoCI/· ion in the Cs 3CoCI 5 crystal.
References
See, e.g., Grimwood , D., Bytheway, I. and Jayatilaka, D. (2003) J. Camp.
I
Chern . 24, 470-483 .
Grimwood , D. and Jayatilaka, D., TONTO: A System for Computational
2
Chemistry, www.theochem.uwa .edu.au/tonto/index.html .

337

SThP-29
CRYSTAL EXPLORER: A GRAPHICAL USER INTERFACE FORDISPLAYING AND MANIPULATING HIRSHFELD SURFACES AND
FINGERPRINTS FOR CRYSTAL ENGINEERING APPLICATIONS

Dylan Jayatilaka, Daniel Grimwood and Stephen Wolff
Chemistry, School of Biomedical & Chemical Sciences , University of Western
Australia , Crawley, WA 6009 , Australia (dylan@theochem.uwa .edu .au) .
Th e Hirshfeld surface is a region enclosing a moeity in a crystal , wi thinwhich more than 50% of the electron density comes from that moeity [1] . The
surface can be coloured in a number of ways , to highlight local packing
interactions in the crysta l [2 ,3] . In addition , a fingerprint of the surface can bemade which quickly and clearly displays in a 2D format inter-moeity interacti ons- thus maki ng comparison of crystalline interactions in different crystal
structures straightforward [4].
Crysta l Explorer is a graphica l user interface (G UI ) for manipulating
Hirshfeld surfaces [5] and the associated fingerprints. Examples demonstrating
the use of the GUI will be presented .
References
I
Spackma n, M.A. , Byrom, P.G. (1997) Chem. Phys. Lett., 267, 215-220.
2
McKinnon , J.J., Mitchell , A.S ., Spackman , M.A., (1998) Chem. Eur. J. , 4 ,2136-2141 .
3
McKinnon, J.J., Mitchell , A.S., Spackma n, M.A. , (1998) Chem. Comm. , 4 ,2071-2072 .
4
Spackman , M.A. , McKinnon, J.J, (2002) Cryst. Eng. Comm. , 378-392 .
5
Crystal Explorer: A GUt for manipulating Hirshfeld Surfaces,
www.theochem.uwa.edu .au/crystal_explorer.

338

SThP-30
STUDY OF METAL-INSULATOR TRANSITION IN Rb4Cso BY COMPTONSCATTERING, UNDER PRESSURE

Genevieve Loupias ,a A. A. Sabouri-Dodaran ,a M. Marangolo,a Ch . Bellin ,a F.
Mauri ,a S. Rabii ,a· 6 Th . Buslaps,c M. Mezouar,c and W. Crichtonc
alaboratoire de Mineralogie-Cristallographie de Paris, Univ. Paris VI , case 115,
4 pl. Jussieu, F-75252 Paris Cedex 05, France; bOept. of Elect. Eng ., Univ. of
Pennsylvania , Philadelphia , PA 19104-6390, USA; cEuropean Synchrotron
Radiation Facility (ESRF), BP 220 , F-38043 Grenoble-Cedex, France(loupias@lmcp.jussieu .fr)

LOA band structure calculations on the bet Rb4Cso [1] claim a metallic
behavior for this material but they are stro ngly at odds with the NMR andphotoemission finding of an insulating ground state .
Compton scattering was used to measure the ground state momentum
density in Rb4C60 and theoretical directional Compton Profiles , obtained fromwave-function calculations, was used for comparison [2]. In this molecular solid ,the Jahn-Teller distortion of the C60 molecules was not taken into account by
previous LOA calculations and was assumed to be responsible of the mismatch
between theoretical and experimental Compton Profile of ~C so (A=Rb and K)
compounds . In particular, this effect - which has not yet been clearlyexperimentally observed - is invoked to be respo nsible of the Mott insulatingphase in ~Cso .
In order to switch off the Jahn Teller effect, we have performed newmeasurements of Rb 4C60 Compton Profiles below and above the metal-insulatortransition at 0.8 GPa (respectively 0.1 and 1.9 GPa). The differen ce ofCompton Profiles will be compared with corresponding calculated results ,obtained from our recent ab-initio energy band structure calculations. In
particular, these calculations allowed us to quantitatively discriminate kinetic
energy effect induced by pressure and Jahn-Teller effect , on momentum
densities.
As a consequence , a new model will be presented to explain metalinsulator transition , supported by both new experimental and theoretical
Compton results.
References
Erwin , S. C. and Bruder, C. (1994) Physica B 199, 600 .
I
Marangolo, M., Bellin , Ch., Loupias , G. , Rabii , S. , Erwin , S. C. and2
Buslaps , T. (1999) Phys. Rev. B, 17084.

339

SThP-31
ARE ELECTRON CORRELATION EFFECTS OBSERVABLE IN ELASTIC
X-RAY SCATTERING EXPERIMENTS?

Graham Chandler, lan Bytheway, Brian Figgis , and Dylan Jayatilaka
Chemistry, School of Biomedical & Chemical Sciences, University of Western
Australia , Crawley WA 6009, Australia (gsc@chem.uwa.edu.au)

Difference density maps clearly show shifts in the density when HartreeFock calculations are compared with those incorporating correlation effects [1] .
However,as pointed out by Wiberg et at. for many stable molecules the charge
redistribution from electron correlation should be a small correction comparedwith the accuracy of experimental observations[2] . Are they large enough to be
detectable?
To test this matter X-ray structure factors which include thermal smearing
effects taken from experimental measurements , have been calculated for arange of small-molecule molecular crystals from spherical atom procrystal
electron densities , and Hartree-Fock, QCISD , and density functional (B3L YP)
electron densities using the superposition of independent molecules method.
These calculations were carried out to assess whether the effects of electron
correlation on the electron density cause sufficient change in structure factors
when compared with those from Hartree-Fock to enable the correlation effect tobe experimentally detectable.
The spherical atom procrystal calculations have been used in showing themagnitude of the effect which chemical bonding makes on structure factors . Xray data was shown to be capable of distinguishing the effects of chemicalbonding long ago [3]. However, the specific effect of bonding on structure
factors has not been examined before . It was included in our calculations for theadded insights it may give to the determination of bonding effects from X-ray
data and also to demonstrate the great difference in magnitude of the changes
in structure factors generated by correlation when compared to the changes
caused by bonding .
The results of this investigation will be presented.
References
I
Boyd , R. and Wang , L. (1989) J. Comput. Chern. 10, 367.
2
Wiberg , K. , Hadad, C., LePage , T., Breneman , C. and Frisch , M . (1992) J.
Phys. Chern. 96 , 671 .
3
Coppens , P. (1997) X-ray Charge Densities and Chemical Bonding,(Oxford University Press , New York); Dawson , B. (1967) Proc. Roy. Soc.
A298 , 255 .

340

Friday August 15

Sagamore XIV

ABSTRACTS
ORAL SESSIONS

341

SFr1-1
INELASTIC MAGNETIC X-RAY SCATTERING FROM HIGHLY CORRELATEDELECTRON SYSTEMS

P. A Montano a,b Y Li b.c J F Mitchell c P. E. Mijnarends,d.e S. Kaprzyk, d.f
B. B~rbiellini.a'and
Ban~ild .
'A.

•Materials Sciences and Engineering , SC-13Germantown Bldg . U.S.
Department of Energy, 1000 Independence Ave. SW, Washington DC 20585 ,USA; bDepartment of Physics , University of Illinois, Chicago IL 60680 , USA;cMaterials Science Division , Argonne National Lab., 9700 South Cass Ave.
Argonne IL 60439 ,USA; dDepartment of Physics , Northeastern University,
Boston , MA 02115 , USA; eDelft University of Technology, Delft, The
Netherlands; 'Academy of Mining and Metallurgy, al. Mickiewicza 30 , 30-059
Cracow, Poland (pedro.montano@science.doe.gov)
We have used the magnetic Compton scattering (MCS) technique todetermine the spin distribution in highly correlated electronic systems. Thesesystems have extremely interesting physical properties such as their electronictransport and magnetic behavior as well as their interrelationship. We report
MCS experiments on colossal magneto resistance (CMR) perovskite manganite
La 0.7Sr0 .3 Mn0 3 , bilayered perovskite manganite La 1.2Sr,sMn20 7, and magnetite
Fe 30 4. The experiments were carried out at various temperatures along
different crystallographic directions and at different magnetic fields. Spin
moments are calculated and their changes with temperature along different
directions at different external magnetic fields are presented . For this purpose
magnetic Compton profiles (MCP) along low-index crystallographic directions
were measured using the elliptical multipole wiggler (EMW) installed atbeamline 11-ID-B of the Advanced Photon Source (APS) . The line shapes ofthe Magnetic Compton profiles are analyzed using a simple approximation withatomic d orbitals and free electron gas model. The modeling was used toinvestigate the electron distribution in the ground state. The band structure of
the La 12 Sr1.8Mn 20 1 was computed semi-relativistically within the conventional
local-spin-density approximation based band theory framework and spin selfconsistent KKR framework. The experimental MCPs were compared with thecorresponding first-principles computations and a very good overall level ofaccord was found . Within the resolution of the experimental data, some Fermi
surface signatures in the MCPs could be identified in accord with theoreticalpredictions. Our analysis indicates that the MCPs are well-explained in terms ofspin contribution and that orbital effects are negligible for La ,.2Sr1.8Mn20 7. It isobserved that in La 0.7Sr0 .3Mn0 3 , the spin moment changes insignificantly from
5K to 1OOK and then drops rapidly at temperatures above 1OOK. At the sametime , an itinerant electron feature observed at 5 K disappears for temperatureshigher than 1OOK . The magnetite Fe 30 4 MCP show an itinerant electron feature
at all temperatures from 1OK up to 300K. This result suggests a significant role
for the itinerant electrons even in the low temperature region, which is in
disagreement with a simple charge ordering picture. The spin moment behaviorof magnetite also shows correlation with the conductivity around Verweytransition temperature.
This work was supported by the US DOE .

342

SFr1-2
ELECTRON CORRELATION EFFECTS IN NOVEL MATERIALS: RECENTSTUDIES OF CUPRATES, MANGANITES AND 3D QUANTUM DOTS

Arun Bansil
Department of Physics, Northeastern University, Boston , MA 02115, USA(bansil@neu .edu)
Electron correlation effects are becoming an increasing focus of attentionin understanding the behavior of wide classes of novel materials. This talkpresents some of our recent work concerning several systems of current
interest. In connection with the cuprate superconductors , we show how theFermi surface evolves with electron doping in Nd 2.xCexCu04-> as the Matt
pseudogap collapses , in the light of recent high resolution ARPES experiments
and related mean field Hartree-Fock and self-consistent renormalization
computations within the framework of the one-band t-t'-t"-U Hubbard model
Hamiltonian. We also discuss how the ARPES matrix element via its selectivity
properties can be exploited to focus on interesting physics in the cuprates (e .g.
the issue of coherence effects and bilayer splitting in Bi2212). In connection
with quantum dots, we discuss an exactly solvable model Hamiltonian for
describing the interacting electron gas in a quantum dot. Results for a sphericalsquare well confining potential are presented . The ground state is found to
exhibit striking oscillations in spin polarization with dot radius at a fixed electron
density. These oscillations are shown to induce characteristic signatures in the
momentum density of the electron gas , providing a novel route for direct
experimental observation of the dot magnetization via spectroscopies sensitive
to the electron momentum density. Finally, brief comments are made on recent
magnetic Compton scattering measurements on La 1.2Sr 18$Mn 2$0 7 from which
we adduce that orbital effects on the momentum density in this CMR material
are quite small.

343

SFr1-3
SUPERCONDUCTIVITY AND FERROMAGNETISM OF ZrZn 2

Zs. Major,8 S. B. Dugdale ,8 R. Watts ,8 G. Santi ," M.A. Alam ,8 S. M. Hayden,8 J.
A. Duffy ,b J. W. Taylor,b T. Jarlborg ,c E. Bruno ,d D. Benea ,e and H. Eberte
8

H.H. Wills Physics Laboratory, University of Bristol , Tyndall Avenue , Bristol
BS8 1TL, UK; bDepartment of Physics , University of Warwick, Coventry CV4
7AL , UK; cDPMC , University of Geneva , 24 quai Ernest Ansermet, CH-1211
Geneva 4, Switzerland ; dDeparment of Physics , Univeristy of Messina , Sal ita
Sperone 31 , 98166 Messina, Italy; elnstitute for Physical Chemistry, LudwigMaximilians University, Butenandtsrasse 5-13, 81377 Munich , Germany(zs.major@bristol.ac.uk)

The discovery of the ferromagnetism co-existing with superconductivity inthe compound UGe 2 [1], followed by similar discoveries in ZrZn 2 [2] and URhGe[3], has re-opened the debate about the relationship between magnetism andsuperconductivity. At the centre of this debate is the question of the pairing
mechanism for the superconductivity, with the speculation that it is magneticallyrather than phonon-mediated .
Knowledge of the topology of the Fermi surface (FS) is vital to anunderstanding of the superconductivity. Furthermore, such measurements are astringent test of electronic structure calculations, on which our models for thesuperconductivity rely. Our recent quantum oscillatory measurements of the FS
of ferromagnetic ZrZn2 [4] have revealed a FS topology that is in agreementwith our LMTO band structure calculations ; however, the quasiparticles arestrongly renormalized , to such a degree that there is no clear experimental
evidence of the heaviest sheet . This sheet is important because it contributes
about half of the density-of-states at the Fermi level. Also , there is someindication that FS nesting could be important, both in terms of the possibility ofa Fulde-Ferreii-Larkin-Ovchinnikov (FFLO) superconducting state [5], and also
in terms of spin-fluctuations and magnetically mediated pairing [6 ,7] . Given its
likely dominance in determining physical properties , information about thisunobserved sheet is vital.
We present the results of our investigation into these specific aspects ofthe superconductivity and ferromagnetism in ZrZn 2 using two different
momentum density measurements. First, our positron annihilation study of the(paramagnetic) FS , and our search for signatures of the heavy sheet, isdiscussed . Secondly , we have used magnetic Compton scattering to address
the issue of the delocalisation of the magnetic moment as an additional insight
into the electronic structure. Both these measurements are supported by firstprinciples electronic structure calculations , and their implications discussed interms of possible mechanisms for the superconducting pairing.
References

1
2
3
4
5
6
7

Saxena , S. S., eta/. (2000) Nature (London) 406, 587.
Pfleiderer, C., eta/. (2001) Nature (London) 412, 58.
Aoki , D. , eta/. (2001) Nature (London) 413, 613.
Yates , S. J. C. , et at. (2003) Phys. Rev. Lett. 90, 057003 .
Singh , D. J. and Mazin , I. I. (2002) Phys. Rev. Lett. 88, 187004.
Santi, G., eta/. (2001) Phys. Rev. Lett. 87, 247004.
Fay, D. and Appel, J. (1980) Phys. Rev. B 22, 3173 .

344

SFr2-1
WAVE-FUNCTION-BASED AB INITIO METHODS FOR ELECTRONICSTRUCTURE CALCULATIONS ON INSULATORS

Alok Shukla
Physics Department, Indian lnstititute of Technology, Powai , Mumbai 400076 ,India (shukla@phy.iitb.ac.in)

Traditionally, the ab initio electronic structure calculations for crystalline
systems have been performed within the framework of density functional theory(OFT) . However, it is a well-known fact that the OFT does not perform
satisfactorily for systems in which electron correlations are strong. As far as
excited state properties are concerned , OFT-based approaches systematicallyunderestimate the band-gaps and band-widths of even weakly correlated
systems such as semiconductors . Additionally, OFT-based approaches are notamenable to systematic improvements. Therefore , there is a need to go back tothe basics and investigate the feasibility of computing the electronic structure ofsolids via the wave-function route , i.e. , by directly solving the Schroedinger
equation . The advantages of such an approach are obvious - one can perform
both the mean-field (Hartree-Fock) as well as many-body ca lculations (CI ,coupled-cluster etc.) within the same formalism .
Over last several years we have pursued such an approach for crystalline
insulators using the Wannier-functions (as against the Bloch orbitals) as the
single-particle orbitals , and have performed both Hartree-Fock and thecorrelated calculations on several ionic and covalent systems. In our talk, wewill describe our approach whose implementation resulted in the computer
program WANNIER [1 ,2] and also present results concerning electronic andlattice properties of several crystalline insulators [3,4]. We will argue that suchan approach can also be extended to metallic systems , provided one uses anonorthogonal set of localized orbitals .
References
Shukla , A., Dolg , M. , Fulde, P. and Stoll , H. (1998) Phys. Rev. B 57 , 1471.
I
Shukla , A., Dolg , M. , Fulde, P. and Stoll , H. (1999) Phys. Rev. B 60 , 5211 .
2
Shukla , A. (2000) Phys. Rev. B 61 , 13277.
3
Abdurahman , A. , Shukla , A. and Dolg , M. (2002) Phys. Rev. B 65 ,
4125204.

345

SFr2-2
THE SIESTA METHOD: PRESENT STATUS AND FUTURE PROSPECTS

Julian D. Gale ," Emilio Artacho,b Alberto Garcia,c Javier Junquera ,d Pablo
Ordej6n ,• Daniel Sanchez-Portal ,' and Jose M. Solerg"Department of Chemistry, Imperial College London , South Kensington , SW7
2AZ , U.K. ; bDepartment of Earth Sciences, University of Cambridge, Downing
Street, Cambridge , CB2 3EQ , U.K. ; cDepartamento de Fisica de Ia Materia
Condensada , Universidad del Pais Vasco , Apt. 644 , 48080 Bilbao , Spain ;dlnstitut de Physique , Batiment B5, Universite de Liege, B-4000 Sart-Tilman ,Belgium ; • tnstitut de Ciencia de Materials de Barcelona , CSIC , Campus de Ia
UAB, Bellaterra , 08193 Barcelona , Spain ; 1Dep . de Fisica de Materiales and
DIPC , Facultad de Quimica , UPV/EHU , Apt. 1072 , 20080 Donostia , Spain ;gDep. de Fisica de Ia Materia Condensada , C-111 , Universidad Aut6noma de
Madrid , E-28049 Madrid , Spain U.gale@imperial.ac.uk)

In order to achieve the goal of being able to perform ab initio electronic
structure calculations on very large molecular and condensed matter systems it
is necessary to address the issue of the calculation scaling with increasingsystem size. Here the details of the SIESTA method [1 ,2] will be presented,
which makes it possible to perform calculations that scale linearly withincreasing numbers of atoms , both in computational expense and memory
usage . This is achieved through the use of radially confined basis functions thatlead to sparse matrices , in combination with an auxiliary basis of a real spacemesh for the evaluation of the Hartree and exchange-correlation potentials . In
addition , linear scaling requires the use of functional minimization approaches
to solve for self-consistency , though conventional matrix diagonalisation is alsoavailable . Through the use of parallel computing , and the above methodology, it
is now quite feasible to perform ab initio calculations on thousands of atoms.
Many standard observables of electronic structure theory may be obtained
including electron and spin densities , optimized structural configurations ,phonons , as well as dynamical information. Examples will be given of theapplication of the technique , as well as possible directions for futureadvancement.
References
I
Artacho , E., Sanchez-Portal , D., Ordej6n , P., Garcia , A. , and Soler, J. M.
(1999) Phys. Stat. Sol. 8 215, 809-817 .
2Soler, J. M. , Artacho , E., Gale, J. D., Garcia , A. , Junquera , J. , Ordej6n , P.
and Sanchez-Portal , D. (2002) J. Phys.: Condens. Matter 14, 2745-2779 .

346

SFr2-3
SOME NEW DEVELOPMENTS WITH WAVEFUNCTIONS CONSTRAINED TO
EXPERIMENTAL SCATTERING DATA

Dylan Jayatilaka
Chemistry, School of Biomedical and Chemical Sciences, University of Western
Australia , Crawley, WA 6009 , Australia (dylan@theochem.uwa .edu .au)

Over the last few years we have developed methods to constrain ab initio
Hartree-Fock wavefunctions to reproduce observed X-ray structure factors formolecular crystals [1 ,2]. In the talk I will outline some new developments under
way in our group:
I . The estimation of errors in derived properties obtained from the constrained
wavefunctions , due to errors in the experimental measurements.
2. The use of constrained density functional theory (DFT) wavefunctions .
3. The use of X-ray and Polarised Neutron Diffraction (PND) structure factors tojointly constrain the wavefunctions.
4. An idea of how to constrain non-variational wavefunctions , such as thecoupled cluster type wavefunctions , to reproduce experimental scattering
data .
References
See , e.g., Grimwood , D., Bytheway, 1. , Jayatilaka, D. , (2003) J. Camp.
I
Chem . 24, 470-483 , and references therein.
Grimwood , D., Jayatilaka, TONTO: A System for Computational Chemistry2
www.theochem .uwa.edu.au/tonto/index.html.

347

348

Saturday August 16

Sagamore XIV

ABSTRACTS
ORAL SESSIONS

349

SSa1-1
POSITION AND MOMENTUM DENSITIES COMPLEMENTARITY AT
WORK, REFINING A QUANTUM MODEL FROM DIFFERENT DATA SETS

J. -M . Gillet, S. Ragot, and P. J . Becker
Laboratoire Structures , Proprieties et Modelisation des Solides .
CNRS/UMR8580 , Ecole Centrale Paris, Grande Voie des Vignes 92295
Chaten ay-Malabry Cedex , France (gillet@spms .ecp.fr)

Although Bragg and Compton scattering are well-established techniques,very few attempts to combine information orig inating from those experiments
have been made so fa r. Thi s remark also holds for Bragg magnetic scattering.
We propose a qu ite general procedure to refine a quantum model fromdifferent data sets using basic Bayesian statistics . As an illustration , different
results for extracting chemica l information such as charge transfer in ioniccovalent compounds will be given .
Influence of correlation in data , as introduced in momentum density
reconstructio n, will be explored and extens ion to other combina tio ns ofexperiments will be suggested .
At a different leve l of interpretation and accuracy , a simultan eous
app roa ch of position and momentum representations of the One electron
Density Matrix (1OM) requires , at least , a possibility of working beyond thestra ight path of "independent electrons" scheme in a perfect 3D lattice. We wi ll
describe an ab-in itio computationa l strategy to the ca lculation of the 1DM that
reproduces infinite lattices results with a good accu racy but that enables for theof defects in the structure as well as a fa ir accou nt for electron co rrelationenergy . This Cluster Partition ing Method (CPM) will be shown to be efficient forstudies ranging from intra-atomic correlation mechanisms in ionic soli d toanalysis of hydrogen bond in ice and , with few compromises , an extension tomore complicated structu res.

350

SSa1-2
ELF: FOR THE GOOD AND FOR THE BAD

Andreas Savin
Laboratoire de Chimie Theorique, CNRS et Universite Pierre et Marie Curie ,Paris , France (andreas.savin@lct.jussieu.fr)

The electron localization function (ELF) of Becke and Edgecombe [1] is atool to analyze chemical bonding in molecules and solids. After a decade ofapplications , this talk is a view back , about the soundness of its definition, its
advantages and limitations, its perspectives , but also about some of its
competitors.
ReferenceI
Becke , A. D. and Edgecombe , K. E. (1990) J. Chem. Phys. 92, 5397.

351

SSa1-3
SINGLE-PARTICLE ORBITALS AND MANY-BODY COMPTON SCATTERING
Bernardo Barbiellini
Department of Physics , Northeastern University, Boston , MA 02115 , USA(bba@neu .edu)

Single particle orbitals continue to play a useful role even when one
considers properties of correlated electron systems. The natural orbitals
introduced by Lowdin , which form an orthonormal basis set, are a particularly
suitable set of one-particle functions to use for ground-state electron
momentum density (EMD) computation [1) . In the independent particle model(I PM) , the occupancy of a natural orbital can only be 1 or 0. The introduction ofcorrelations then yields occupation numbers with values which differ from 0 or
1, with most high energy states being nearly unoccupied. We also discuss theso-called Dyson orbitals , which are a different set of one-particle orbitals
associated with many-body states and related spectral functions . These
orbitals however are in general not normalized and can be linearly dependent.
We show how Dyson orbitals can be used to express the Compton scatteringcross-section beyond the constraints of the commonly invoked framework of theimpulse approximation (lA) [2). Our goal is to develop computationally tractable
schemes for obtaining Compton scattering cross-section beyond the IPM and
lA. Illustrative results on Li , AI , Be and Cr are presented .
References
I
Barbiellini , B. and Bansil , A. (2001) J. Phys. Chem. Solids 62, 2181 .
2
Kaplan , I.G., Barbiellini , B. and Bansil , A., preprint cond-mat/0304294 .

352

SSa1-4
CHEMICAL INFORMATION FROM THE SOURCE FUNCTION
C. Gatti , F. Cargnoni , and L. Bertini
CNR-ISTM , lstituto di Scienze e Tecnologie Molecolari, via Golgi 19, 20133
Milano, Italy (c.gatti@istm.cnr.it)
Recently it was shown [1] that one may view the electron density at any pointr within a molecule to consist of contributions from a source G(r, r') operating at allother points r' . By evaluating the source over regions bounded by surfaces thatsatisfy the topological definition of an atom[2], the density at r may be equated to asum of atomic source contributions S(r,Q)'11' fi (r' )i7( r ) = -(1/ 4n)J dt·'
- -r- r' 1=-( l/ 4n) 2; 0 J ., G( r , r' )dr'

= 2; 0 S(r , Q)

1

Such a decomposition enables one to view the properties of the density froma new perspective and establishes the source function (SF) as a potentiallyinteresting tool to provide chemical information.
This study [3] is aimed at widening up the limited spectrum of applications of
the SF [1 ,4] so as to increase the knowledge of properties and usefulness of theSF. We examine a number of cases, including (a) the effect of the X substitution
on the source contribution from A to the electron density at bond critical point(BCP) in AX diatomics and the extent to which the near transferability of theintegral properties of A , when present, is reflected in the source contribution from A
to the BCP density; (b) the relative weight of the internal and external contribution
to the density at a (3,-3) critical point when this is a non-nuclear maximum, rather
than a maximum associated to a nuclear-cusp; (c) the relative weight of source
contributions from the atoms of H-bond complex to the density at the H-bond CP,
in a series of complexes of increasing strength . The correspondence between the
H-bond classification provided by the ELF topological approach and by the SF is
also highlighted .
The figure on the right, where circles areproportional to the S(r,Q) from different atoms Q
tF·- H·-FJ'
and with negative sources in light grey, clearlyshows how the SF discriminates among very•strong , intermediate
andweak
H-bondFH - NH.
complexes.
e-lt is concluded that the SF appears as apractical tool to unravel the local and non local
character of the electron density distributions andto quantify such a locality and non locality in termsof a physically sound and appealing chemical partitioning .

•--e--e----·---.

References
1
Bader, R. F. W. and Gatti , C. (1998), Chern. Phys. Lett. 287 , 233-238.
2
Bader, R. F. W. in Atoms in Molecules: A Quantum Theory, International
Series of Monographs on Chemistry, Oxford , University Press, (1990), 22.
3
Gatti, C. , Cargnoni, F. and Bertini, L. (2003), J. Comput. Chern. 24, 422-436.
4Overgaard , J., Schi0tt, B., Larsen , F. K. and Iversen, B. B. (2001) Chern.
Eur. J. 7, 56-3767.

353

SSa2-1
THERMAL MOTION ANALYSIS, A MOLECULAR MEAN FIELD MODEL
Hans-Beat Burgi
Laboratory of Crystallography, University of Berne, Freiestr. 3, CH-3012 Bern ,Switzerland (hans-beat.buergi@krist.unibe.ch)Atomic displacement parameters (ADPs) are a by-product of crystal structure
analysis that is largely ignored although they encompass about two thirds of thenumerical information from such an analysis. Reasons for this include: (1) poor
quality of ADPs due to systematic errors arising from the diffraction experimentsand (2) no information on the correlation of motion between different atoms. The
quality of ADPs has improved significantly due largely to the availability ofsynchrotron radiation and CCD area detectors [1] . Due to the low dispersion ofsynchrotron radiation , the magnitude of ADPs is largely independent of the detailsof data processing , contrary to what is found for sealed tube data , and with Heand N2-cooling devices it is relatively easy to collect data from -10 to 300 K within
2-3 days of beam time.
The rigid body model of Schomaker and Trueblood is the most popular way
of interpreting ADPs [2] . It has been extended to include soft intramolecularmotion, albeit at a penalty: the distinction between internal and external motions ispartially lost [3] . Both approaches assume correlations implicit in a rigid or semirigid body. If a structure is determined at several temperatures, each set of ADPs isanalysed seperately, thus ignoring the information contained in the temperaturedependence of the ADPs.
We have developed a physical model that improves several of theseshortcomings: ( 1) the model explicitly accounts for the temperature dependence of
the ADPs and provides for temperature independent contributions to the ADPs; (2)the correlation of atomic motion is obtainable from the model provided ADPs areavailable over a sufficient range of T, preferably from -10 K to the melting
temperature of the substance; (3) the ADPs from all experiments are analysed
simultaneously; (4) the model is expressed and programmed in terms of chemical
coordinates to facilitate comparison with results from vibrational spectroscopy andab initio calculations [4] . Multi-temperature analysis of ADPs gives access toseveral new types of information. For rigid molecules the amplitudes of
intramolecular zero-point motions are determined simultaneously with those oflibration and translation. The T,L,S matrices are thus improved compared to theclassical analyses. A Grueneisen parameter may be introduced to account for the
lowering of vibration frequencies due to thermal expansion of the crystal(anharmonicity). The specific heat cv is obtainable from the vibration frequencies(cp if combined with measurements of dV/dP). Multi-temperature analysis is a
powerful way to distinguish between motion and positional disorder of atoms that is
too small to be resolved by most structure analysis(-< 0.7 A) [5] .
References
I
A.T .H. Lenstra , J.F.J. Van Loock, B. Rousseau , S.T. Maes, Acta Cryst. ,2001, A57 , 629.
2
V. Schomaker, K. N. Trueblood ,. Acta Cryst. , 1968, B24, 63 .
3
V. Schomaker, K. N. Trueblood,. Acta Cryst., 1998, B54, 507
4H.-B. Burgi , S. C. Capelli , Acta Cryst. , 2000, A56, 403. H. B. Burgi, M.
Fi:irtsch , J . Mol. Struct. , 1999, 485-486, 457 .
5
H.-B. Burgi , Annu. Rev . Phys. Chem ., 2000 , 51 , 275. H.-B. Burgi, Faraday
Discussion , 122 (2002) 41 .

354

SSa2-2
PSEUDOATOM RADIAL FUNCTIONS FROM THEORETICAL MOLECULARDENSITIES

T. Koritsanszky," and A. Volkovb
8
Department of Chemistry, Middle Tennessee State University, TN , USA;bDepartment of Chemistry, State University of New York at Buffalo , NY, USA(tkoritsa@mtsu .edu)

Recent experimental and model electron density (ED) studies[1) havepresented convincing evidences for the limited adequacy of the deformation
radial functions (RF) applied in popular pseudoatom models. These functions
are routinely taken as Slater-type functions whose parameters are deduced
from ground-state atomic Hartree-Fock calculations utilizing single-zeta basissets[2) .
In this contribution we present a simple method for deriving pseudoatomic
RF's for chemically bonded atoms. The approach , following Stewart's
suggestion[2] , is based on the least-squares projection technique , however,instead of the total molecular ED , we use its component stockholder- atoms[4)(ps) as individual target functions in the fit. ps represents the most localized
bonded atom , satisfies the nuclear cusp cond ition and exhibits the proper longrange behavior.
The least-squares conditions lead to stockholder-atom RF's (YimJ defined
asa1'", (r) = r,;,~.Jn 5 ( r)d ,"" (f}, cp)d u,r,"" = Jn 5 (r )d ,'", (f},cp)dru

where , d1m; s are density normalized re al spherical harmonics , P1m,'s are
multipole populations and the integration , taken over the angular variables({)·,cp ), is performed numerically. The multicenter three-dimensional problem of
projecting the molecul ar ED into its constituent pseudoatoms can thus be
reduced to a one-center one-dimensional problem of projecting normalized
stockholder-atom RF's to linear combinations of primitive basis functions.
Preliminary results for H-, C- and 0 -atoms show that the molecular ED
can be reconstructed with an accuracy of 0.05 eA- 3 if the RF's are represented
in terms of two Slater functions , at least. While the x-refinement works well forthe monopole RF's, it fails for the higher order functions , just as it often does inexperimental studies . The method has th e potential not only for redu cing th ebias in parameter estimates of the multipole model and thus providing reliable
topologi cal details of the static experimental ED , but also in density constructionof large molecules .
References
I
Koritsanszky, T. and Coppens , P. (2001) Chern. Rev. 101 , 1583 andreferences therein .
2
Clementi , E. and Raimondi , D. L. (1963) J. Chern. Phys. 38 , 2686.
3
Stewart, R. F. (1977) lsr. J. Chern. 16, 12.
4Hirshfed , F. L. (1977) Theoret. Chim. Acta 44, 129.

355

SSa2-3
MULTIPOLAR REFINEMENT OF PROTEINS : SUCCESS AND PITFALLS

B. Guillot." C. Jelsch ," A. Podjarny,b and C. Lecomte 8
LCM 3B, Faculte des Sciences , BP239 , 54506 Vandoeuvre-les-Nancy, France;bLGBS , IGBMC, 1, rue Laurent Fries, BP10142, 67404111kirch , France(bguillot@lcm3b.uhp-nancy.fr)

8

The constant advances in synchrotron radiation and crystallogenesis
methods , and the impulse of structural genomics projects have bought biocrystallography in a context favorable to subatomic resolution protein or nucleic
acid structures. Thus , as soon as such precision can be frequently obtained , theamount of information available in the precise electron density should also beeasily and naturally exploited , similarly to the field of small molecules charge
density studies.
Indeed , in addition of a better modeling of thermal motion andstereochemistry , allowing a deeper understanding of the structure - function
relationship, subatomic resolution leads to a parameterized description of thedeformation density, if an adequate atomic model like the multipole formalism ,is used during the refinement[1). From this description , it becomes possible toderive experimental atomic charges and more generally experimental
electrostatic properties: in other words a new point of view to chemical
reactivity, molecular recognition processes and host-guest mechanism .
However, proteins are not small molecules. There are specific methods forboth fields and prior to get valuable information from a charge density study of abiological macromolecule, we have to extend multipolar refinement methods toproteins and in parallel adapt some bio-crystallography techniques to the small
molecules world!
This is the topic of the present talk . We will present, on one hand themethods implemented in our program MoPro[2], designed to allow non
spherical (multipolar) electron density refinement of all sized molecules , inreasonable amounts of CPU time , and , on the other hand, some applications ,especially based on the 0.66A structure of Human Aldose Reductase[3], toshow both successes and limits of these methods.
References
I
Jelsch , C., Teeter, M. M., Lamzin , V. , Pichon-Pesme , V. , Blessing , R. H.
and Lecomte, C. (2000). Proc. Nat!. Acad. Sci. (USA). 97 , 3171-3176.
2
Guillot, B., Viry, L. , Guillot, R., Lecomte , C. and Jelsch , C. (2001 ). J. Appl.
Cryst. 34, 214-223.
3
Muzet, N., Guillot, B., Jelsch , C., Pichon-Pesme, V. and Lecomte, C.
(2003) submitted.

356

SSa2-4
CHARGE DENSITY STUDIES OF Z' = 2 MOLECULES. POSSIBILITIES AND
LIMITATIONS

Dai Hibbs, Mark P. Waller, and Jacob Overgaard
School of Chemistry, University of Sydney, NSW 2006 , Australia(hibbs_d@chem.usyd.edu.au)
Experimental X-ray charge density (CD) studies of molecules with morethan one molecule in the asymmetric unit are relatively rare [1]. On the contrary,such occurrences are abundant in structural chemistry, evidenced by the 22015
hits of Z' 2 in CCDC , corresponding to 8% of all published structures [2] . Thus ,it is apparent that such compounds have been avoided by the CD community.
This is due to several factors. Firstly , the increase in the number of parameters
is a significant drawback, since a successful multipole model in most cases
requires more than 300 reflections per non-hydrogen atom . Secondly, one of
the molecules often experiences a rather weak crystal field ; hence the thermal
motion of this molecule can be severe and the molecule may even bedisordered . Thirdly , there can exist significant correlations between multipole
parameters from different molecules. All in all , CD studies of this type of crystal
structures offer a range of problems that need to be addressed .
There are , however, large potential benefits of studying the CD in suchmolecules. In the case of rigid molecules , it allows the determination ofmultipole parameters of identical atoms in slightly different environments
without the presence of systematic errors intrinsic in a comparison of different
experiments. Hence, it is important in the evaluation of transferability of atomic
multipole parameters [3].
This presentation will outline the details of experimental and theoreticalcharge density studies of three organic molecules all having two molecules in
the asymmetric unit (see Figure) . Besides a discussion of the prospects ofgiving an independent description of the two molecules in the same study, eachof the three systems represents interesting chemical and theoretical issues thatwill be addressed .

-- J_ .
~M--M

FLAVONEFLUOR ENOL

TFIPN

ReferencesI

2
3

Gatti , C., May, E., Destro , R. and Cargnoni , F. (2002) J. Phys. Chem. A.
106 , 2707; van Reeuwijk , S. J., van Beek , K. G. and Feil , D. (2000) J.
Phys. Chem. A. 104, 10901.
eeoc search 13/3/03 gave 22015 hits equalling Z' 2 out of 272066.
Pichon-Pesme , V., Lecomte , C. and Lachekar, H. (1995) J. Phys. Chem.
99 , 6242.

357

SSa3-1
SPIN DENSITIES IN MOLECULE-BASED MAGNETIC COMPOUNDS: FIRSTSTUDY OF A PHOTO-INDUCED MAGNETIC STATE

B. Gillon
Laboratoire Leon Brillouin (CEA-CNRS), C.E. Saclay, 91191 Gif-sur-Yvette,
France (gillon@llb.saclay.cea.fr)

Molecule-based magnets attract growing attention because of their
specific optical and mechanical properties , which do not present classicalmagnets. Photo-switchable molecule-based magnetic materials , like spincrossover compounds , are of particular interest for future data storage at themolecular level.
The understanding of the mechanisms which are involved in magnetism ofmolecule-based compounds is essential for the design of new systems . The
spin density determination by polarized neutron diffraction (PND) provides
direct information on the nature and the origin of the intra- and inter-molecularmagnetic interactions. A short review of spin density studies in different types ofmolecule-based magnetic compounds will be given: a molecule-based magnet,
with an ordering temperature of 39K , in which Mn 11 and Mo 111 transition metal
ions interact through cyano bridges[1], a paramagnetic Ti 1v complex in which
two semiquinonato radicals interact ferromagnetically via the non magnetictransition metal ion [2] and a high spin cyano-bridged molecular cluster Ni11 9W V6(S =12).
In a second part, the determination of the photo-induced magnetisation
density and high spin Fe 11 magnetic form factor in a spin crossover Fe 11 complex
will be reported[3]. A new experimental set-up on the polarised neutron
diffractometer 5C1 at the LLB allows in situ light illumination of the crystal. A
complete photo-process was achieved for the Fe 11 complex . Large possibilities
of PND in providing information on the magnetic coupling scheme , the spin
density distribution and spin delocalisation effects could be useful for otherphoto-magnetic crystals.
References
I
Stride , J. A. , Gillon , B. , Gukasov , A., Larionova , J. , Clerac , R. and Kahn ,0 . (2001) C. R. Acad. Sci. Paris, Chern. 4, 105-112.
2
Pontillon , Y., Bencini, A., Caneschi , A., Dei, A., Gattteschi, D., Gillon , B.,
Sangregorio , C. , Stride , J. A. and Totti , F. (2000) Angew. Chem. Int. Eng.
Ed. 39 , 1786-1788.
3
Jeftic, J., Gillon , B., Goujon , A. , Nau , Q ., Gukasov , A., Codjovi , E. andVarret, F. Polyhedron, in press .

358

SSa3-2
ENSEMBLE REPRESENTABLE DENSITIES FOR ATOMS AND MOLECULES:ANALYSIS OF POLARISED NEUTRON EXPERIMENTS WHEN SEVERALZEEMAN LEVELS ARE POPULATED

P. Cassam-ChenaYa.b
8
LETMEX , Physique Recherche, Faculte des Sciences , Universite de NiceSophia Antipolis , Pare Val rose , Nice, F-061 00 , France; bDepartment ofChemistry , University of Western Australia , Nedlands, WA 6009 , Australia(cassam@unice.fr)

Polarised neutron diffraction experiments conducted at 4.2 K on Cs3CoCI 5
crystals are analysed by using a 4-dimensional model Hilbert space made of abinitio n-electron wave functions of the CoCI/· molecular ion. The magnetic
structure factors given by the best ensemble density operator that isrepresentable in our model space are fitted to the experimental ones by
optimizing two spin-orbit mixing coefficients of the embedded CoCI/- ions andseveral configuration interaction coefficients . The optimized density operator
can in turn be used to calculate any observable. Here we present density mapsof the spin density, and the orbital current density. The method , which is
general , gives a goodness of fit,less then 1 with fewer parameters optimised
than other methods employed so far. It provides a new way of gaining
information about spin-orbit coupling and the relative contributions of spin andorbital motion to the magnetic properties of an atomic or molecular system .
Another interesting finding is that a l less then 1, can be obtained with a spin
density of the same sign everywhere in space , leading to the conclusion thatspin polarisation is within the experimental error. The so-called "collinear
approximation" has been avoided in this work although it has been found to bejustified for this system. A direct comparison is made between calculated andexperimental flipping ratios [1] .

l.

References
I
Cassam-ChenaY, P. (2002) J. Chem. Phys. 116, 8677-8690 .

359

SSa3-3
OBSERVATION OF ORDERED ORBITAL OF YTi03 BY THE X-RAY
MAGNETIC DIFFRACTION EXPERIMENTS
Masahisa Ito,a Naruki Tuji ,8 Fumitake ltoh ,8 Hiromichi Adachi ,b Etsuo Arakawa ,cKazumichi Namikawa ,c Hironori Nakao ,d Youichi Murakami ,d Yasujiro Taguchi ,".
and Yoshinori Tokura•
8

Faculty of Engineering, Gunma University , Aramaki-machi 4-2, Maebashi ,Gunma 371-8510, Japan ; bMaterials Research Institute, KEK , Oho 1-1 ,Tukuba , lbaraki 305-0801 , Japan ; cTokyo Gakugei University, Nukuikita-machi
4-1-1 , Koganei , Tokyo 184-8501 , Japan ; dGraduate School of Science , Tohoku
University , Aramaki , Aoba-ku , Sendai 980-8578, Japan ; • oepartment ofApplied Physics , The University of Tokyo , Hongo 7-3-1 , Bunkyo-ku , Tokyo 1130033 , Japan ; ·present address, Institute for Materials Research , Tohoku
University , Katahira 2-1-1 , Aoba-ku , Sendai 980-8577 , Japan(itom@fs.aramaki.gunma-u .ac.jp)

The orbital degree of freedom is recognized to be an important factor that
determine the solid state properties of some perovskite compounds such as
YTi0 3 together with the charge degree and the spin degree of freedom. Orbital
ordering of YTi0 3 has been intensively researched both theoretically[1 ,2] andexperimentally[3-6]. The 3d electrons of Ti atoms in a t29 orbital are thought tobe ordered. Ordered orbitals of YTi0 3 have been observed by NMR[3], neutron
diffraction[4], and the resonant X-ray scattering[5] . The model wave functions of
the ordered orbitals were based on the assumption that the orbital moments arequenched. In the present study we made the X-ray magnetic diffraction (XMD)
measurement of ferromagneti c YTi0 3 in order to measure the orbital (L) and thespin(S) magnetic form factors utilizing the ability of LS separation of the XMD.
The experiment is divided into two part ; (1) the measurement of the orbital
magnetic form factor to check the orbital moments is quenched or not , and (2)the measurement of the spin magnetic form factor to observe the orderedorbital directly. XMD could be a tool to observe directly the orbitals of the orbital
ordering systems.
References
I
Mizokawa , T. and Fujimori , A. (1996) Phys. Rev. 8 54, 5368-5380.
Sawada, H. and Terakura , K. (1998) Phys. Rev. 8 58 , 6831-6836.
2
3ltoh , M ., Tsuchiya , M. , Tanaka , H. and Mataya , K. (1999) J. Phys. Soc.
Jpn. 68 , 2783-2789.
4
Ichikawa , H., Akimitsu , J. , Nishi, M. and Kakurai , K. (2000) Physica 8
281 &282 482-484.
5
Nakao , H ., Wakabayashi, Y. , Kiyama , T., Murakami , Y., Zimmenrmann , M.
V. , Hill , J . P., Gibbs, D., Ishihara , S. , Taniguchi , Y. and Tokura , Y. (2002)
Phys. Rev. B 66 , 184419 1-7.
6
Ulrich , C ., Khaliullin , G., Okamoto , S., Reehuis , M. , Ivanov , A. , He, H.,
Tagu chi , Y. , Tokura , Y. and Keimer, B. (2002) Phys. Rev. Lett. 89 167202
1-4.

360

Sunday August 17

Sagamore XIV

ABSTRACTS
ORAL SESSIONS

361

SSu1-1
ELECTRON MOMENTUM SPECTROSCOPY OF SINGLE CRYSTAL SILICON
AND NICKEL TARGETS

M. Vas , C. Bowles , C. Chen , A. S. Kheifets , V. A. Sashin , and E. Weigold
Research School of Physical Sciences and Engineering , Australian National
University, Canberra 0200 ACT, Australia (maarten .vos@anu .edu .au)
In Electron Momentum Spectroscopy (EMS) an incoming electron ionizes
a target and the scattered and ejected electrons are measured in coincidence.
By comparing the energies and momenta of both outgoing electrons with that of
the incoming electron , we can determine the energy and momentum transferredto the target , i.e. we measure the energy-resol ved momentum densities
including lifetime broadening and other correlation effects. Here we present
data for single crystal silicon and nickel along high-symmetry directions. Clear
anisotropies in the electronic structure were found for both materials. For an
infinitely thin crystal one can determine directly the magnitude of thecontribution of different plane waves to the Bloch function at a given binding
energy. However, for a crystal of finite thickness diffraction may occur for theincoming and /or outgoing electron beams and this complicates theinterpretation. By varying measurement geometry one can vary the diffraction
conditions , and hence extract valuable information on the contribution ofdifferent plane waves to the Bloch function .
<110>

K X

K

r

<100>

K X K

'---'--'

1

lvfomeull ull (:1.u.)

Fig.1 Measured spectral momentum density of Si along <11 0> and <100>directions. The dotted line is the calculated band stru cture . The top halfshows the high momentum part on an expanded grey scale . The anisotropy
is clearly resolved , and the influence of diffraction is evident as well.

362

SSu1-2
ORBITAL MOMENTUM DENSITIES OF CHEMICALLY SIMILAR
MOLECULES USING HREMS AND OFT

M. J . Brunger," K. L. Nixon ," L. Campbell ," F. Wang ,b B.Appelbe ,b M. Hamilton ,cand D. A. Winklerd"School of Chemistry, Physics and Earth Sciences , Flinders University, GPO
Box 2100, Adelaide, SA 5001 , Australia; bVictorian Partnership for Advanced
Computing, PO Box 201, Carlton South , Vic 3053, Australia ; cSchool ofComputer Science and Information Technology , RMIT, Melbourne, Vic 3000 ,Australia ; dDivision of Molecular Sciences , CSIRO, Private Bag 10, Clayton
South MDC, Vic 3169, Australia (Michaei.Brunger@flinders.edu.au)

We repo rt on results from our High-Resolution Electron Momentum
Spectrosco py (HREMS) studies[1) and Density Functional Theory (OFT)
calculations[2) into the complete valence electronic structures of the chemicallysimilar molecules norbornadiene (C?Hs), norbornene (C7H,o) and norbornane(C7H12). Representative examples of our measured and calculated orbital
momentum densities for each of these molecules are presented andsystematically discussed. In addition some of their important physico-chemical
properties (particularly their respective structures) , as derived from our studies ,are also presented. These latter results are compared against corresponding
values from independent measurements and calculations.
References
1
Brunger, M. J . and Adcock, W. (2002) J. Chern. Soc., Perkins Trans. 2, 122.
2
Wang , F., Brunger, M. J., Winkler, D. A. , Hamilton , M. and Appelbe, B.
(2003) J. Comput. Chem ., submitted .

363

SSu1-3
PROBING ELECTRON MOMENTUM DENSITIES IN MOLECULES USING A
NEW MULTICHANNEL (e,2e) SPECTROMETER
Masahiko Takahashi and Yasuo Udagawa
Institute of Multidisciplinary Research for Advanced Materials, Tohoku
University, Sendai 980-8577, Japan (masahiko@tagen.tohoku.ac.jp)

Electron momentum spectroscopy (EMS) , based on the (e ,2e) reaction
under the Bethe ridge conditions, has been developed as a powerful means forinvestigations of electronic structure of atoms and molecules [1] . Within theplane-wave impulse approximation (PW IA) , the EMS cross section for agaseous target is directly related to the spherically averaged momentum density
or momentum profile of the Dyson orbital for the ionization transition .
Furthermore , EMS can give unique and versatile information for the detailed
study of electronic structure , such as symmetries , binding energies and polestrengths of the states involved.
Nevertheless, the potential of EMS has not been fu lly achieved as yet due
mainly to the small cross sections involved , which cause large statisticaluncertainty and poor energy resolution. Very recently, we have developed a
new spectrometer that employs a spherical analyzer and position sensitive
detectors [2] . By taking an advantage of simultaneous detection in energy andmomentum , collection efficiency for the two outgoing electrons has beensignificantly improved compared with our previous apparatus [3], opening up
the possibility of considerably more precise measurements.
In this contribution we report details and performan ce of the newly
developed spectrometer. Our re cen t studies of several targets will also bepresented. Applications to be discussed involve (1) electron momentum profiles
for the complete valence shell of CO and (2) simultaneous ionization excitation
processes of H2, together with comparison between expe riment and theory.
Finally, prospects for probing directional momentum densities or looking at
molecular orbitals in the three-d imensional momentum-space will be discussed
for gaseous targets.
References
I
Weigold , E. and McCarthy, I. E. Electron Momentum Spectroscopy(Kiuwer Academic/Plenum Publishers , New York , 1999).
2
Takahashi , M., Saito , T., Matsuo, M. and Udagawa, Y. (2002) Rev. Sci.
lnstrum. 73 , 2242-2248.
3
Takahashi , M., Nag asaka H. and Udagawa, Y. (1997) J. Phys. Chem. A
101 ' 528-532.

364

SSu2-1
CHARGE DENSITY MEASUREMENTS OF TRANSITION-METAL OXIDESUSING CONVERGENT -BEAM ELECTRON DIFFRACTION

K. Tsuda , Y. Ogata , and M. Tanaka
Institute of Multidisciplinary Research for Advanced Materials, Tohoku
University, Sendai 980-8577 , Japan (k_tsuda@tagen.tohoku.ac.jp)
We have developed a method to refine crystal structural parameters using
convergent-beam electron diffraction (CBED) [1], [2]. The method is applicableto nanometer-size crystal structure refinement because CBED patterns can beobtained from specimen areas of a few nm in diameter. The method is basedon the least-squares fitting between full dynamical calculations andexperimental intensities of energy-filtered two-dimensional CBED patterns ofzeroth-order Laue-zone (ZOLZ) reflections and higher-order Laue-zone (HOLZ)
reflections . For this purpose , we developed an energy-filter transmission
microscope JEM-2010FEF [3], and our own analysis program MBFIT [1] torefine structural parameters.
The method can be applied to the determination of charge-density
distribution because the low-order Fourier coefficients of the electrostatic
potential (low-order crystal structure factors for electron diffraction), which arevery sensitive to valence electrons , can be refined together with the atom
positions and Debye-Waller factors . Through Poisson's equation , the structure
factors for electron diffraction are related to those for X-ray diffraction , or the
Fourier coefficients of the charge density. According to the nature of Poisson's
equation , a small change in the low-order structure factors for X-rays causes alarge change in those for electrons . Thus , the present method has a highpotential to determine charge-density distribution more sensitively than X-ray
diffraction.
We applied the present method to the rhombohedral phase of LaCr0 3 [3] .
Clear anisotropy of thermal vibration of the oxygen atoms was successfully
determined by CBED for the first time . The deformation electrostatic potential
and deformation charge-density map were constructed from the refinedstructural parameters , revealing clear charge transfer from the metal atoms to
the oxygen atoms .
The present method can be extensively applied to the charge-density
determination of the perovskite and related transition-metal oxides revealing
charge- ordering and orbital-ordering phenomena , which are closely related tothe colossal magnetoresistance and the high-Tc superconductivity. Though thematerials are frequently composed of very small domains owing to twin
structures and/or characteristic phase separations, the CBED technique allows
us to obatain diffraction intensity data from a single domain. We have alreadyobtained a preliminary result of the anisotropic charge density of the orbitalordering phase of LaMn0 3 , for which the ordering of e 9 orbitals of the Mn 3delectrons was observed using the resonant X-ray scattering technique [4]. Moredetailed analyses using several CBED patterns with different beam incidences
are now in progress.
References
I
Tsuda , K. and Tanaka , M. (1999) Acta Cryst. , ASS , 939-954.
2
Tsuda , K., eta/. (2002) Acta Cryst., ASS , 514-525.
3
Tanaka , M., eta/. (1999) J. Microsc., 194, 219-227.
4
Murakami , Y. , eta/. (1998) Phys. Rev. Lett., 81 , 582-585.

36S

SSu2-2
CALCULATIONS OF ELECTRON ATOMIC SCATTERING FACTORS ANDTEMPERATURE DEPENDENT DEBYE-WALLER FACTORS

Lian-Mao Peng
Department of Electronics, Peking University, Beijing 100871 , China(plm@ele.pku.edu.cn)

Electron atomic scattering factors and Debye-Waller factors are two typesof important parameters that an electron crystallographer must have before
conducting any quantitative electron crystallography work. While numericalvalues of electron atomic scattering factors are available for all free neutral
atoms and most commonly occurring ions[1). Oebye-Waller factors are moredifficult to find and most of the time the existing Debye-Waller factors are given
only at few fixed temperatures and it is not always clear as to how to interpolatethese values to other temperatures. In this lecture we will be concerned with theadvantages of using an alternative analytical expression [2] for the electron
atomic scattering factors , especially those for ions and for reflection high-energy
electron diffraction (HREED) and surface calculations [3-5] . We will also present
results on lattice dynamics calculations on a range of compounds, especiallyoxides, and the evaluation of temperature dependent Oebye-Waller factors fromthese calculations , their parameterization [6-8] and computation of absorptive
scattering factors of electrons [9] .
References
J.M. Cowley (1999) International Tables for Crystallography, Volume C,I
p259 , Kluwer Academic Publishers
J.M. Cowley, L.-M . Peng , G. Ren , S.L. Dudarev and M.J. Whelan (1999)
2
International Tables for Crystallography, Volume C, p262 (1999) Kluwer
Academic Publishers
L.-M . Peng , G. Ren , S.L. Dudarev and M.J. Whelan (1996) Acta Cryst.
3
A52, 257
L.-M . Peng , S.L. Dudarev and M.J. Whelan (1998) Phys. Rev. 857 , 7259
4L.-M . Peng (1998) Acta Cryst. A54 , 481
5
H.X. Gao, L.-M . Peng and J.M. Zuo (1999) Acta Cryst. A55 ,1014
6
H.X. Gao and L.-M. Peng (1999) Acta Cryst. A55 , 926
7
H.X. Gao and L.-M. Peng (2000) Acta Cryst. A56, 519
8L.-M . Peng, G. Ren , S.L. Dudarev and M.J. Whelan (1996) Acta Cryst.
9
A52 , 456

366

5Su2-3
THE "COMBINATION METHOD" OF QUANTITATIVE CBED AND X-RAY
DIFFRACTION APPLIED TO CORUNDUM.
Philip N.H. Nakashima ," Victor A. Streltsov ,b and Andrew W.S. Johnsonc"School of Physics and Materials Engineering , Monash University, Clayton Vic
3800 , Australia ; bStructural Biology, CSIRO Division of Health Sciences andNutrition, Parkville Vic 3052, Australia ; ccentre for Microscopy andMicroanalysis , University of Western Australia , Crawley WA 6009 , Australia(philip .nakashima@spme.monash.edu.au)
Corundum , or a -AI20 3, has a great tendency to form perfect crystals. A lotof theoretical and experimental charge density research has been conductedwith corundum as a benchmark compound because experimental results
should , in principle , be very reproducible from this highly ideal material.
However, very high crystal perfection often leads to significant extinction in the
integrated intensity measurements of strong , lower order reflections (those mostsensitive to the bonding charge density distribution) by conventional single
crystal X-ray diffraction due to the increased likelihood of multiple scattering . In
addition , the data lacks an absolute scale, the relativity of the structure factor
measurements resulting from the application of kinematic scattering theory. The
conventional least squares methods of refining extinction and scale
simultaneously are heavily compromised in the presence of significant
extinction due to the strong correlation between the two quantities. Different
approaches to applying extinction and scale corrections can result in great
variability in the experimentally determined charge densities [1 , 2]. Suchvariability eliminates the possibility of making a reliable comparison ofexperimentally measured charge density with that computed by theoreticalmodels .
The "combination method" overcomes the problems discussed above byusing quantitative convergent beam electron diffraction (QCBED) to measure
the lower order structure factors to high precision (uncertainty of order 0.1%) on
an absolute scale . The technique fully accounts for multiple scattering andmeasures the structure factors from the angular distribution of intensity within
the corresponding reflections on or near the Laue circle. This negates theissues of scale and extinction. QCBED is less accurate in measuring higher
order structure factors and therefore , a combination of the low order QCBED
data with the higher order X-ray data is required to optimise charge density
measurements. An overlap of the QCBED data set with the valid , extinction free
portion of the X-ray data allows the latter to be scaled to the QCBED data. A
similar approach was used successfully by Zuo et al [3] to measure charge
density in Cu20.
We will present comparisons of our experimental results with OFT(GGA/FPLAPW) and PHF calculations.
References
1
Streltsov, V. A. and Maslen , E. N. (1992) Acta Cryst. A48 , 651 .
2Streltsov , V. A., Nakashima, P. N. H. and Johnson , A . W. S. (2001) J.
Phys. chem. Solids 62 , 2109 .
3
Zuo , J. M., Kim , M., O'Keeffe , M. and Spence , J. C. H. (1999) Nature 401 ,
49.

367

368

Monday August 18

Sagamore XIV

ABSTRACTS
ORAL SESSIONS

369

SMo1-1
RECENT MOMENTUM DENSITY STUDY OF NOVEL MATERIALS

Y. Sakurai , and M. ltou
Japan Synchrotron Radiation Research Institute (JASRI), SPring-S ,1-1-1 Kouto , Mikazuki , Sayo , Hyogo 679-519S , Japan (sakurai@springS.or.jp)

Recent progress of the high-resolution Compton scattering project at
SPring-S will be reported.
The Cauchois-type x-ray spectrometer[1] has been upgraded byinstallation of an x-ray image intensifier (X-II) as a position sensitive detector(PSD). The new PSD system consists of a X-II (HAMAMATSU V7339P-MOD)and a CCD camera (HAMAMATSU C4742-95-12ER) . The x-ray entrance
window has a diameter of 4 inches which covers the focal positions
corresponding to the x-ray energies between 70 and 90 keV for the incident xray energy of 115 keV and the scattering angle of 165 degrees. The X-II PSD
detects these x-rays under the photon-counting operation mode. The overall
momentum resolution is 0.12 atomic unit (a .u.) at present, and should be better
than 0.10 a.u . in future. The improvement makes it possible to measure a set ofCompton profiles within a reasonable beam-time for a tomographicalreconstruction of three- or two-dimensional momentum density or a systematicinvestigation under various sample conditions .
Currently , many research subjects are running with the spectrometer.
Among them , the followings will be presented in this conference;(1) Fermi surface topology of the spin-triplet superconductor Sr2 Ru0 4 [2],(2) Cohesion mechanism of Al-based and Cd-based quasicrystals (3],(3) Hydrogen-induced change in momentum density for metal-hydrides[4] ,(4) Charge transfer in Si clathrates.
The authors would like to express their many thanks to Y. Maeno , J.
Tamura-Okada , Y. Watanabe , S. Nanao , S. Mizusaki , I. Yamamoto , M.
Yamaguchi , H. Fukuoka , S. Yamanaka , N. Hiraoka , A. Koizumi , and N. Sakai ,whom they have been collaborating on the high-resolution Compton scattering
project at SPring-S . They also acknowledge the support by the SPring-S Joint
Research Promotion Scheme under the auspices of the Japan Science andTechnology Corporation .
References
I
Hiraoka , N., ltou, M. , Ohata , T., Mizumaki, M., Sakurai , Y. and Sakai, N.
(2001) J. Synchrotron Rad. 8, 26-32 .
2
Hiraoka, N., Deb , A. , ltou , M., Sakurai , Y., Mao, Z. Q . and Maeno ., Y.
(2003) Phys. Rev. B, in press .
3
Tamura-Okada , J. , Watanabe , Y ., Yokoyama , Y. , Hiraoka , N., ltou , M .,Sakurai , Y. and Nanao, S. (2002) J. Phys.: Condens. Matter 14, L43-L48 .
4
Mizusaki , S. , Hiraoka , N. , Yamamoto , 1. , ltou , M. , Sakurai , Y. andYamaguchi , M. (2003) J. Phys. Soc. Jpn , in press.

370

SMo1-2
SPIN DENSITIES IN MOMENTUM SPACE

J . A. Duffy
Department of Physics , University of Warwick, Coventry, CV4 7AL, United
Kingdom U.a.duffy@warwick.ac.uk)

Magnetic Compton scattering is a technique whereby the spin dependent
electron momentum density in ferromagnets can be probed. The spin-polarisedCompton profile is a 1-dimensional integral of the momentum space spin
density. The total spin moment can be directly obtained via the integrated
scattering cross section , whilst the lineshape is determined by the nature of theelectronic orbitals or bands on which the magnetism resides . Spin-polarisedCompton scattering is closely related to the magnetic form factor
measurements with the neutron and x-ray diffraction methods. The method isparticularly useful for studying both itinerant moment systems , and materials
where there is a combination of localised and itinerant moments.
A set of examples will be given , covering in particular, rare earth systems ,the hexaborides and the study of the spin density in ferromagnetic
superconductors .
Magnetic Compton scattering is particularly suited to the study of rareearth systems , since it can distinguish between the localised 4f moments andother more delocalised contributions to the spin moment. For example , in Gd ,the itinerant moment can be easily distinguished from the localised 4f
magnetism, and furthermore so can the change in itinerant moment on alloying
with yttrium. In materials such as SmMn2Ge2, it is possible to separate the 4f
and 3d contributions . It sensitivity to the spin moment only has enabled theferromagnetism in the Sm 1.xGdxAI system , where the spin and orbital moments
cancel giving little or no net moment, to be investigated.
The doped hexaboride Ca ,.xLaxB6 appears to exhibit weakferromagnetism , with a moment of 0 . 07 ~L s for x = 0.005 , with a Curie
temperature of -600K _ However, the real nature of the magnetism observed iscontroversial, and is sometimes considered to arise from Fe impurities.
Magnetic Compton scattering has revealed a very delocalised moment, notrepresentative of that found for a 3d system, providing evidence in favour of theferromagnetism being intrinsic.
Recently , the technique has been applied to the study of ferromagnetic
moments in superconducting materials. It has been used in ZrZn 2, in the normal
state , to study the 4d moment, and for comparison with electronic structure
calculations. It has also been used in ErNi2B2C, to measure the spin density inthe superconducting state, where it is not prohibited by the diamagnetism
present. ErNi 2B2C is a so-called magnetic superconductor, where magnetic
Compton scattering measurements show clear evidence for the existence of a
weak ferromagnetic state below 2.3K, within the superconducting state.
Finally, present developments of the method , including use of higher
magnetic fields , and high pressures, will be discussed.

371

SMo1-3
COMPTON-SCATTERING STUDIES ON ATOMIC AND MOLECULARSYSTEMSS. Huotari , M. Hakala, Sz . Galambosi, S. Manninen , and K. Hamalainen
Division of X-ray Physics , Department of Physical Sciences, P.O.B. 64, FlN00014 University of Helsinki, Finland (simo .huotari@helsinki.fi)

Recent advances in Compton-scattering spectroscopy have revealed arange of phenomena not yet fully understood . Systematic studies on simple
metals [1-4] have provided us with information on the final-state effects in the
scattering process and on the ground-state correlation effects in the electrongas. Separating these effects would be essential in understanding the electron gas properties. It is possible to minimize the final-state effects partly by using an
incident-photon energy high enough , but the separation of correlation and e.g.
finite-temperature effects in solids [5 ,6] is not straightforward.
To build up the understanding of these properties of electronic systems ,we have conducted high -accuracy Compton-scattering studies on simple
systems starting from noble-gas atoms and continued to simple molecules . It is
well-known that correlation effects in closed-shell atoms are small andespecially so in the helium atom. Using the Hartree-Fock approximation and byconstructing the two-electron He wave function from 1s orbitals as a Slater
determinant, it is possible to calculate the 1s momentum-space wave function
from the measured momentum density. Using this wave function , we havecomputed the charge density of He as well. Using LCAO methods andcorrelation corrections based on second-order perturbation theory , we canshow how the correlation effects increase when going from rare-gas atoms tosimple molecules.
Due to the absence of complications that arise in solid-state (thermal
disorder, high-momentum components , etc.) , the analysis of atomic andmolecular data gives important insight on the applicability of Compton scattering
as a probe for e.g . correlation and bonding.
References1
Hamalainen , K., Manninen S., Kao, C. -C ., Caliebe , W ., Hastings, J. B.,
Bansil , A. , Kaprzyk , S. and Platzman , P. M. (1996) Phys. Rev. B. 54 ,5453-5459 .
2Schulke , W., Stutz, G., Wohler!, F. and Kaprolat, A. (1996) Phys. Rev. B
54, 14381 -14395.
3
Sternemann , C. , Hamalainen , K. , Kaprolat , A., Soininen , A., DOring , G .,Kao , C. -C ., Manninen , S. and Schulke , W. (2000) Phys. Rev. B 62
R7687-R7690 .
4
Huotari, S., Hamalainen , K. , Manninen , S. , Kaprzyk, S., Bansil , A.,
Caliebe , W., Buslaps, T. , Honkimaki , V. and Suortti , P. (2000) Phys. Rev.
B 62 7956-7963.
5
Sternemann , C. , Buslaps , T. , Shukla , A. , Suortti , P., Doring , G. and
Schulke, W. (2001) Phys. Rev. B 63 , 094301 .
6
Huotari , S., Hamalainen, K., Manninen , S., Sternemann , C. , Kaprolat, A. ,Schulke, W. and Buslaps , T. (2002) Phys. Rev. B 66, 085104 .

372

SMo1-4
COMPTON SCATTERING ON ALKALI-METAL-DOPED SILICON
CLATHRATES
0

M. Volmer,• C. Sternemann ," J . S. Tse ,b D. D. Klug ,b M. Paulus," C. L. Bull ,T. Buslaps ,d N. Hiraoka ,d and M. Tolan••Institute of Physics , University of Dortmund , D-44221 Dortmund , Germany;bSteacie Institute for Molecular Sciences , National Research Council of
Canada , Ottawa, Ontario , Canada K1A OR6; 0 Davy Faraday ResearchLaboratories , Royal Institution of Great Britain , 21 Albemarle Street, London
W1S 4BS , England ; dEuropean Synchrotron Radiation Facility, B.P . 220 , F38000 Grenoble, France(schenkel@physik.uni-dortmund .de)

Silicon clathrates are guest-host materials in which a dopand is trapped in
cage-like structures built up from covalently bonded , four-coordinate Si atoms[1 ,2] . There are two structual types of the clathrates which are analogous to thewell known gas hydrate structures I and II [3] . The macroscopic physicalproperties of these semi-conductor clathrates like electrical conductivity ,glasslike thermal conductivity, or superconductivity are crucially influenced by
the different inclusion compounds. Therefore , the guest-host interactions of the
Silicon clathrates are of special importance to reach a deeper understanding of
the electronic properties of these candidates for thermoelectric applications .
Compton scattering gives a valuable tool at hand to investigate how theelectronic ground state along with the electronic wave functions of the hostlattice is changed by the different alkali-metal guests.
Compton profiles of the empty caged Si 136 structure II clathrate and of the
Na , K, Rb) structure I calthrates as well as
alkali-metal-doped M 8 Si46 (Mpolycrystalline Si have been measured at the Compton scattering beamline
ID15B of the ESRF using an incident photon energy of 56.4 keV with amomentum space resolution of 0.25 a.u. at the elastic line. The Compton profile
differences between the alkali-metal doped Si clathrates and the empty caged
structure are compared with GGA-LDA calculations [4] of these systems anddiscussed in terms of charge transfer between the guest and the host lattice .
Furthermore , small differences between the Compton profiles of the empty
caged Si clathrate and the polycrystalline Si sample are found as well for thevalence electron Compton profiles.

=

References
He, J., Klug , D. D. , Uehara , K., Preston , K. F., Ratcliffe , C. I. and Tse, J. S.
I(2001) J. Phys. Chem. B 105, 3475.
Moewes , A ., Kurmaev, E. Z ., Tse, J . S., Geshi , M., Ferguson , M. J.,
2
Trofimova , V. A . and Yarmoshenko , Y. M. (2002) Phys. Rev. B 65 ,
153106, and references therein .
Bowron , D. T. , Filliponi , A., Roberts , M. A. and Finney, J . L. (1999) Phys.
3
Rev. Lett. 81 , 4164.
Tse , J. S. and Klug , D. D. (2003) private communication.
4373

SMo2-1

TOPOLOGICAL ANALYSIS OF 3D GRIDDED ELECTRON DENSITIESP. Rabiller," M. Souhassou ,b C. Katan ,c S. Oahoui ,b and C. Lecomteb•Groupe Matiere Condensee et Materiaux, Universite de Rennes 1, Rennes
UMR CNRS 6626 , F35042, France; bLaboratoire de Cristallographie et deModelisation des Materiaux Mineraux et Biologiques UMR CNRS 7036 ,Universite Nancy 1, Vandoeuvre les Nancy, F54506 , France ; csyntheseelectrosynthese Organiques UMR CNRS 6510 , Universite de Rennes 1,
Rennes , F35042, France(philippe .rabiller@univ-rennes1.fr)

Obtaining topological properties of electron densities - following AIM
approach[1) -getting rid of basis set dependence is something than can be
asked for. The InteGriTy software package[2) has been developed in this spirit
and works with electron densities given on regular 30 grids corresponding toeither isolated or periodic systems . An interpolation method is used to get atany point the density, its gradient and hessian . Then critical points (CP) can belocated and characterized on one hand. On the other hand atomic basins
surfaces can be searched for and charge integration be performed over thebasins . The conditions and performances of InteGriTy will be first presented ,before discussing two applications . In the case of an inorganic compound(Ammonium Dihydrogen Phosphate) , a comparison is made between the
topological properties derived analytically from the experimental multipolar
expansion with the help of NewProp[3) and those obtained with the samedensity calculated on a 30 grid . The second application deals with organic
charge transfer complexes and neutral to ionic phase transition[5] .
References
I
Bader, R. F. W. (1995) Atoms in Molecules- A Quantum theory, Int.
Series of Monographs on Chemistry 22 , Clarendon Press - Oxford.
2
Katan , C ., Rabiller, P., Lecomte , C., Guezo , M., Oison , V., Lecomte C. andSouhassou , M. (2003) J. Appl. Cryst. 36, 65-73 .
3
Peres , N., Boukhris, A., Souhassou , M., Gavoille, G. and Lecomte , C.
(1999) Acta. Cryst. A55 , 1038-1048.
4
Souhassou , M. and Blessing , R. H. (1999) J. Appl. Cryst. 32 , 210-217 .
5
Oison , V ., Katan, C., Rabiller, P., Souhassou, M. and Koenig, C. (2003)
Phys. Rev. 867 , 035120 , 1-11 .

374

SMo2-2
CHARGE-DENSITY STUDY OF THE NON-LINEAR OPTICAL MATERIAL:
ZINC (TRIS)THIOUREA SULPHATE

Jacqueline M. Cole,8 Shamus L. G. Husheer,8 Dima S. Yufit,b Judith A. K.
Howard,6 and Garry J. Mclntyrec
8
Department of Chemistry, University of Cambridge , CB2 1EW. UK;
bDepartment of Chemistry, University of Durham , DH1 3LE , UK; clnstitut Laue
Langevin , B. P. 156, 38042 Grenoble Cedex 9, France Umc61@cam.ac.uk)

A charge-density study of the non-linear optical (NLO) material , zinc(tris)thiourea sulphate is presented . The interest lies in the efficiency of the firstorder non -linear term , second harmonic generation (SHG) , where the laser
penetration through the material affects the frequency doubling of light. This
work represents one in a series of charge-density studies that we haveundertaken in order to unravel and understand the relationships between
structure and optical properties [1 ,2]. In these studies charge-density analysis
was used to (i) conduct topologically-based bond-length-alternation typecalculations using values of ellipticity, (ii) perform polarization mapping toinvestigate the nature of intramolecular charge-transfer, and (iii) evaluate thesolid-state molecular dipole moment and relate this to the crystal field forces. Allof these features play an important role in governing the SHG activity and so
structure I property relationships have been built up from this work .
All of these previous investigations have concentrated on organic
materials. However, with the subject study, we now extend this type of analysis
our investigations to an organometallic compound , zinc (tris)thiourea sulphate ,which represents one of few examples of promising organometallic SHG-active
materials , many otherwise viable organometallic candidates suffering fromreactivity towards air. There is much impetus to study organometallic SHGactive materials since they possess both the major optical advantages oforganic materials (eg. very fast optical response and ease of molecular design)and those of inorganic materials (principally thermal stability which is the singlemost common problem with organics) . The results derive from a suitablecombination of complementary 1OOK X-ray and neutron diffraction data , thelatter being important for locating the hydrogen atoms precisely. The X-ray data
were collected in the laboratory at Durham , UK , on a Bruker SMART
diffractometer, whilst the neutron data was collected on the Laue
Diffractometer, VIVALDI , at the ILL, Grenoble, France. The results pertaining to
the aforementioned analysis methods (i)-(iii) are presented.
References
Cole , J. M. , Gaeta , A. E. , Mcintyre, G. J. and Howard , J. A. K. (2002) ActaI
Crystal/ogr. B 58, 690-700.
Cole , J. M., Copley, R. C. B., Mcintyre, G. J. , Howard , J. A. K.,
2
Szablewski , M. and Cross , G. H. (2002). Phys. Rev. B, 65, 125107(1 -11).

375

SMo2-3
TOPOLOGICAL CHARACTERIZATION OF INTERMOLECULAR
INTERACTIONS

Yu Wang ." Chi-Rung Lee,b and Chih-Chieh Wang c
aDepartment of Chemistry, National Taiwan University, Taipei , Taiwan ;bDepartment of Chemical Engineering , Ming-Hsin University of Technology,
Hsin-Fong , Taiwan ; cDepartment of Chemistry , Soochow University, Taipei,
Taiwan (wangyu@ntu.edu.tw)

Topological properties associated with bond criti cal points (BCP) areapplied to intermolecular interactions in order to analyze the role of suchinteractions in the solid state. One of the important interactions is H-bond ,where a very strong symmetric one is similar to a covalent bond , however a
very weak one for instance the di-hydrogen bond is also known. The work
presented will cover the whole spectrum of these H-bonds with comparison
between experiment and theory. In addition , directional interactions between
molecules , for example C .. .S, S... N, N ... O interactions, will also be presented .
Atomic graph of each atom will be applied to illustrate such directional weakinteractions. Packing effects on the chemical bond is investigated through asystematic computation on the designed clusters. In general , the density p b, thetotal energy density H b and the Laplacian , Y' 2 pb, at the BCP will be the mainindices for the characterization of the intermolecular interactions.

376

SMo2-4
TOPOLOGICAL FEATURES OF THE ELECTRON DENSITY AND THE BASIN
PROPERTIES IN SOLIDS

A. Martin Pendas
Departamento Quimica Fisica y Analitica , Universidad de Oviedo , 33006
Oviedo. Spain (angel@fluor.quimica .uniovi.es)

The application of the Theory of Atoms in Molecules (AIM) to condensed
phase systems (1 ,2] displays interesting peculiarities , emerging from thenecessarily finite size of atomic basins that leads to unambiguous atomic
volumes and atomic radii [3] . It also facilitates the introduction of a number ofsimple indices to characterize different chemical interactions [4] . Our ability tomanipulate interatomic distances in such systems by means of external
constraints (stress , pressure , temperature) , opens a vast field that connects
atomic properties with thermodynamic variables. In this work we will present
some of these ideas taken from our experience in solids. We will also show how
our conventional chemical intuition developed within the molecular realm may
fail far from equilibrium configurations , and how the systematic study of theelectron density in solids may help us develop new ideas (5].
References
I
Martin Pendas, A. , Costales, A. and Luana , V. (1997) Phys. Rev. B 55 ,4275.
2
Luana , V. , Costales, A. and Martin Pendas , A. (1997) Phys. Rev. B 55 ,4285.
3
Martin Pendas , A. , Costales , A. and Luana , V. (1998) J. Phys. Chem. B
102, 6937.
4
Mori Sanchez, P. , Martin Pendas, A. , and Luana , V. (2002) J. Am. Chem.
Soc. 124, 14721 .
5Mori Sanchez, P., Martin Pendas A. and Luana , V. (2001) Phys. Rev. B 63
125103-1; Martin Pendas , A., Costales , A., Blanco, M.A., Recio , J. M. andLuana , V. (2000) Phys. Rev. B 62, 13970.

377

378

AD HOCWORKSHOP

PROGRAMS

379

Australian Synchrotron Project Workshop
Monday August 11
Room A 14:00- 16:00
Convener: Richard Garrett
Australia's national 3GeV third-generation synchrotron , to becompleted in 2007, will be located at Monash University. With acircumference of 216 .0m , the storage ring will have twelve straightsections available for insertion devices. An initial suite of 9
beamlines is planned , with the facility eventually accommodatingover 30 .
Crystallographic research in the protein , powder and smallmolecule fields should be catered for at the Australian
Synchrotron . The preliminary requirements of crystallographic
beamlines were identified at a synchrotron workshop in Melbourne
earlier this year. This workshop will be used to fine-tune these
specifications and identify key scientific reasons why beamlines
supporting crystallographic applications should be part of the initialsuite .
The workshop format will be:- An overview of the status of the ASP and of thesynchrotron facilities currently available to researchers via
the ASRP .
- Presentation of the draft scientific cases for the
crystallography beamlines .
-Break-out groups will review the scientific cases andensure these are compatible with the technical features ofthe proposed beamline.

This workshop is supported by the Australian Synchrotron Program, 01/RD,
Government of Victoria.

380

Twinning Workshop
Monday August 11
Room B 14:00-16:00
Convener: Victor G Young
A 2-hour workshop will cover aspects of twinning from the basics
of identification to the advanced topics of how to handle therefinement of merohedral , pseudo-merohedral and nonmerohedral twins .
A number of short presentations will be given on the various
subtopics, and a workbook will be provided . The presentations will
be interspersed with short assignments in the workbook. Some
examples will be provided on CD-ROM for further work once theattendees return to their home laboratories.
There is no participation fee , however the number of participants
will be limited.

381

Modulated Structures Workshop
Tuesday August 12
Room A 14:00-16:00
Convener: Siegbert Schmid
Systems that form modulated structures are a fascinating class ofmaterials that lack conventional lattice periodicity but are still
perfectly long-range ordered . Such systems exist across the whole
range of chemical disciplines from organic conductors andminerals to ceramic materials like high-Tc superconductors andferroelectrics .
A workshop will investigate many of the basic features ofmodulated structures. In particular we will examine the types ofmodulated structures, how to recognise them and what to do aboutdata collection , structure solution and refinement strategies . This
introductory workshop is aimed at scientists that have limited or no
experience with modulated structures. There is no participation fee
but numbers are limited, so registration is essential.

Displacive Modulation

Schematic Diffraction Pattern
G-2q
00 .

00 •

G

G+2q

~0 ~ ~ ·•• 00 . 00
t

t

G-q

G+q

Figure 1: Schematic representation of a displacive modulation and a corresponding
diffraction pattern. The structure can either be described as an 8-times superstructureof the basic two-atom unit cell or with that basic structure and the modulation wave
parameters. The diffraction pattern indicates a clear intensity hierarchy between main382

CCP4 Workshop
Thursday August 14
Room A 14:00-18:00
14:00

Introduction and Welcome (Aiun Ashton)

14:05

CCP4 the organisation , the package (installing etc),
General Overview
CCP4i (Aiun Ashton)

14.45

Data Processing and Scaling with Mosflm and Scala .
(Harry Powell)

15.30

Overview of Molecular Replacement in CCP4
(Katherine McAuley)

16:00

Break

16.15

Advanced and Future strategies for MR
Advanced and Future strategies for Experimental Phasing(Airlie McCoy)

17.00

Refinement with CCP4/Refmac (Airlie McCoy)

17.45

CCP4 and its future projects

18.00

Close

383

384

AUTHOR

INDEX

385

386

Aagaard , Anna , 113, 142 , 179,
227 , 229 , 286
Abrahams, Brendan , 97
Acharya , N., 84
Adachi , Hiroaki , 105
Adachi , Hiromichi, 360
Adachi , N. , 241
Adachi , S., 253
Adachi , Wataru , 172, 235
Adams , Adrienne , 131
Adams , Julian J. , 171 , 219 , 230
Adams , T. E. , 274
Ahn , Hyung Jun , 170
Ahuja , B. L. , 320
Aikawa , Kyoko , 130
Akahama , Yuichi , 173
Alam , M. A. , 344
Alexa , Alexandra A. , 330
Ali , Roushown , 251
Ananthalakshmi, P. , 90Anderson , Bryan F. , 171
Andersson , C. Evalena, 169
Anikin , Michael , 80
Aoyagi , Shinobu , 145
Appelbe, B., 363
Arakawa, Etsuo, 173, 360
Araki , H. , 325
Araki , N., 109, 160
Arcus, Vickery L. , 112 , 132 , 138,
228 , 285
Artacho, Emilio , 346
Asawa! , S. S., 320
Ataka , Mitsuo , 203
Atwood , J. L., 79
Aubert, E., 313
Awana , Veer Pal Singh , 150
Azuma , Mizue, 205
Backbro, Kristina , 228 , 285
Baell , Jonathan , 139
Baker, Edward N. , 112, 132, 138,
171 , 180, 218 , 228 , 285
Baker, Heather M., 112
Baker, Matthew L. , 287
Banerjee, S. , 158
Banfield , Mark J. , 180
Banks, Jasmine , 260
Bansil, Arun, 342 , 343
Barbiellini , Bernardo , 342 , 352
Barbour, L. J., 79
Barco , Joseph , 236

Barnea , Z. , 146, 247 , 248
Barnett, Amanda C., 120
Barnham , K. J. , 219
Batchelor, Adrian H., 92
Becker, P. J., 350
Beddoe , Travis, 214 , 215
Bellin , Ch ., 339
Bencini , A. , 299
Benea , D. , 344
Benn , R. , 294
Berger, James M., 236
Berman , Helen M. , 290
Berman, L. E. , 294
Bertini , L., 353
Bhargavi , G. Ramya , 90
Blaha , Peter, 310
Blankenship , Robert E. , 127
Bowles , C. , 362
Bowman , Brian R. , 287
Breinl , Robert A. , 91
Brennessell , William , 280
Brinkworth , Ross 1. , 91
Brooks, Andrew G., 216, 261
Brooks , Neil R. , 280
Brown , Francisco, 162
Brown , P. J., 306
Brunger, M. J., 363
Bruno , E. , 344
Bull , C. L , 373
Burgess , A. W. , 274
Burgi , Hans-Beat, 182, 354
Burgner, John W. , 273
Burnet, Stephen, 152
Burrows , Scott R. , 261
Bushell , Simon , 215
Buslaps , Th ., 339 , 373
Buttery, Jarrod N. , 89
Byriel , Karl A. , 142
Bytheway, lan , 340
Cahsion , John D., 96
Campbell , L. , 363
Caneschi , A. , 299
Cappai , D., 219
Cappai , R. , 219
Carbonera , C., 299
Card , Graeme L. , 228 , 285
Cargnoni , F. , 353
Carmichael , Jennifer A. , 221
Carr, Paul D. , 118, 271
Cassam-Chenar, P. , 359

387

Cayzer, Tory N., 242
Chan , E. J. , 153
Chandler, Graham , 340
Chang , Ho-Chol , 257 , 334
Chang, Shih-Lin , 175, 312 , 321
Chantler, C. T. , 146, 247 , 248 , 300
Chao , Kuei-Jung , 88
Chapman , Karena W. , 277
Chatake, T., 204
Chaudhuri , N. Ray,94 , 103
Chen , C., 362
Chen , Chun-Jung , 212
Chen , X.-A. , 185
Chen , Yi-Ting , 212
Cheng , Hui-Chun , 135
Cheng , Sen-Yuan , 175
Chiu , Wah , 287
Choudhury, Debi , 114, 119
Christopherson , Richard 1. , 211
Chu , Woei-Chyn , 83
Church , W. Bret, 209 , 263
Claiser, N., 299
Clark, Francis, 260
Clements , Craig S. , 216 , 261
Cohen , Aina E., 128, 293
Cole , Jacqueline M., 375
Colman , Peter M., 139
Cookson , David J., 141 , 146 , 247
Courville , D. A ., 144, 233
Cousson , A., 299
Cowieson , Nathan , 113, 179, 227 ,286
Crabb , Brendan S., 121
Crichton , W., 339
Criswell , A. R., 144
Crout, David , 260
Dahoui , S. , 374
Dasgupta , Jhimli , 119
Dasgupta , Rakhi , 114
Dattagupta , J . K., 114, 119
Davaasambuu , Jav , 310
David , W. I. F., 279
de Jonge , M., 247
De Ia Mora Rey , Teresa , 126
Deane , Janet E., 125
Denny, William A., 131
Devenish , Rodney J., 214
Dey, S., 164
Dhal , B. B., 247
Diefenbach-Jagger, H., 140

Diete , W., 294
Dittrich , Birger, 314
Dong , Z. L. , 107, 276
Dooley, David M., 128, 226
Dougherty, Matthew, 287
Dove , Sophie , 214
du Boulay, Douglas, 108, 275 , 323
Du , Chao-Hong , 312 ,321
Duax , W. L., 93
Duff, Anthony P., 128, 226
Duffy, J. A., 344 , 371
Dugdale , S. B., 344
Duggleby, Ronald G ., 120
Dunstone , Michelle A. , 213
Ebert, H. , 344
Edeling , Melissa A ., 206
Effendy, 89
Ellis, Paul J , 128, 293
Ely, L. K , 216
Endo , Hirohisa , 196
Enkisch , H., 335
Enomoto , Kouichirou , 154
Epa , Vidana C., 121
Ericksson , Geoff, 260
Etheridge , J. E., 249
Faber, John , 245
Fawcett, Tim , 245
Feil , Susanne C., 230
Feng , V., 178
Ferra , J. D. , 144, 233
Figgis, Brian , 340
Fischetti , Robert F., 294
Forouhar, Farhad , 264
Fraser, John D., 112
Freeman , Hans C., 127, 128 ,
224 , 226
Fujii , Tomomi , 225
Fujii, Y. , 147
Fujishiro , Y., 327
Fujiwara , E., 327
Fukazawa , Tesuya , 172
Funahashi , S. , 301
Fushinobu , Nahomi , 130
Galambosi , Sz., 372
Gale , Julian D., 346
Gamage , Niranjali U. , 120, 142 ,229
Garcia , Alberto , 346
Garrett, T. P. J., 274
Gatteschi , D. , 299

388

Gatti , C. , 353
Gee , Christine L. , 142, 229
Gillespie, Matthew T. , 140
Gillet, J.-M ., 350
Gillon , B. , 299 , 358
Godley, Shelley, 236
Goodwin , Andrew L. , 277
Gorfman , Semen V ., 310
Gorman , Michael A ., 220
Goulon , Jose, 307
Graham , Stephen C. , 209 , 224
Grimwood , Daniel J ., 190, 336, 338
Guillot, B. , 356
Gulbis, Jacqueline M. , 220
Guss , J. Mitchell , 125, 127, 128,
131 , 211 , 224 , 226
Hamalainen , K. , 372
Hagiya, Kenji , 246
Hakala, M., 372
Halder, Gregory J. , 96
Hall , Annegret K. , 152
Hamada, Kensaku , 193
Hamilton , M., 363
Hankamer, Ben , 260
Hansen, Carl L., 236
Hansen, N. K. , 299
Harris, Mark, 289
Harrison , Anthony J., 218
Harrowfield , Jack M. , 152
Hashimoto, Hiroshi , 133
Hashizume, Daisuke , 156, 268
Hata , Yasuo , 225
Hayashida , Hirotoshi, 196
Hayden , S. M. , 344
Heaven , M. W. , 79
Hempstead , Paul D. , 171
Heras, Begofia, 206
Heron , Andrew , 260
Hester, James R. , 141
Hibbs, David E., 100, 189, 267,
322 , 357
Hibi, T., 272
Hietschold , Michael , 163
Hihara, Goro , 154, 155
Hikita , T., 149
Hirano, Keiichi , 173
Hiraoka, N., 188, 373
Hirosawa, 1. , 111
Ho, Patricia W. M., 140
Hodder, Anthony N. , 121

Hoeffner, Ed , 126
Hoegh-Guldberg, Ove , 214
Hofman , Robert M., 116
Honjo, Eijiro , 205
Honma, T. , 111
Honma, Yoshiya , 173
Horie, Akane, 205
Horne, 1. , 271
Hoshikawa, Akinori, 87 , 145
Hoshiko, Akie, 196
Hosoya , Takaaki , 87, 161
Howard , C. J., 177, 200 , 239
Howard , Judith A. K. , 375
Hsia , Kuo-Chiang , 83
Hsiao, Chwan-Deng , 264
Huang, Y.-X. , 95
Hubbard, Camden , 245
Huber, Thomas, 113, 179, 227,286
Hudson , Peter J., 221
Huether, R. , 93
Hume, David. A. , 113, 179, 227 ,
229 , 286
Hunter, Brett A., 177
Huotari, S. , 372
Husheer, Shamus L. G. , 375
Ida, Takashi , 143
limura , Yasuhiro , 156
Ikeda, K., 147
Ikeda, Susumu, 87
lkeuchi , Kazuhiro, 308
lmasaki , Tsuyoshi, 133
lmura , H., 111
lnagaki , Kenji , 116lnaka , Koji , 104, 192
Inoue, T., 208 , 231
lseki , T., 238
Ishibashi , Matsujiro, 205
lshigami , H., 149
Ishii , M. , 185
lshimatsu , Naoki, 173
lshimura , Daiju , 252
lshizawa , Nobuo, 108, 275 , 323
ltatsu , K. , 241
Ito, Masahisa , 173, 360
ltoh , Fumitake, 173, 308 , 331,
332 , 360
ltou , M., 188, 332 , 370
ltsubo, Takafumi, 324
Ivanov, Yury V. , 333

389

Iwasaki, Fujiko, 156, 268
Iwasaki, Hiroshi, 151
lwataki, T. , 109
Izumi , M. , 240
Jabeen, T. , 164
Jakana, Joanita , 287
Jameson , Geoffrey B. , 171
Jarlborg, T., 344
Jayatilaka, Dylan , 101 , 190, 314 ,
319, 337 , 338 , 340
Jelsch, C., 356
Jeyakanthan, J. , 84
Jeyaprakash , A. A. , 122, 201
Jiang , L. , 144
Jiang , Wen , 287
Johnson, Andrew W. S. , 367
Johnston, Jodie M. , 132, 228 , 285
Jones, D. A. , 129
Jones, T.Aiwyn , 169, 289
Jorissen , R. N. , 274
Judge, Roopwant K. , 234
Junquera, Javier, 346
Kai , Y., 208 , 231
Kakimoto , K. , 109, 160, 199
Kakutani, Yukinobu , 311 , 320
Kamiyama, Takashi , 87 , 145
Kanaya , S., 208
Kanzaki, Yae, 130
Kaprzyk , S. , 342
Karppinen , Maarit, 150
Kalan , C. , 374
Katiyar, S. , 201
Kato , Ken-ichi , 145, 326
Kato , Matsuri , 133
Kato , T. , 258
Katsube , Yukiteru , 202

Kheifets , A. S. , 362
Kidd , Richard D., 229
Kigawa , Takanori, 284
Kijima, N., 111
Kim , Youn Joong , 250
Kimizuka , Noboru , 162
Kimoto, Koji, 150
Kimura , Hiroyuki, 17 4
Kimura , Yoshisato , 278
Kindo , Kouichi , 257 , 334
Kishimoto , Shunji , 173
Kisi , Erich H., 166
Kita , Keiko , 133
Kitagawa , Susumu , 257 , 334
Kitamura , Masaya , 124
Kitaura , Ryo , 257 , 334
Kiyanagi , Ryoji, 174
Kjer-Nielsen, Lars , 216 , 261
Kleywegt, Gerard J. , 289
Klooster, Wim T., 176, 269 ,
315 , 318
Klug , D. D., 373
Kniep, R. , 95
Kobayashi , A ., 327
Kobayashi , H. , 327
Kobayashi , Kimiko , 197
Kobayashi , Michihiro, 257 , 334
Kobayashi , Shigenobu , 207
Kobayashi , Tatsuo , 257 , 334
Kobayasi , Teiji , 316
Kobe , Bostjan, 91 , 113, 129, 179,
227 , 286
Kochin , Vasili , 310
Kohori , Yoh , 173
Koizumi , Akihisa , 311 , 320
Koizumi , Nozomu, 123
Kojima , Akiko , 174
Kojima, Akira , 151
Kojima , Norimichi, 324
Komai , T. , 147
Komatsu , Hiroshi , 192
Komen , Moyra M. , 138, 228 , 285
Kondo , Jiro, 82
Kong , G. K. W., 219
Konno , Michiko, 130
Koon , Nayden, 228 , 285
Koritsanszky , T. , 328 , 355
Koshiba , Takumi , 205
Koutsantonis , George A. , 89 , 152
Kubo, Yasunori , 317

Ka~uya , Yosh~.202

Katsuyama , J ., 325
Katsuyama , N. , 231
Kaur, P., 164
Kaushik , Jai K., 137
Kawaminami , Masaru, 110, 196
Kawamura , Naomi, 173
Kawamura , Y. , 195
Kawano , Masaki , 85
Kawata , Hiroshi , 325 , 331
Kawata , Yasushi, 225
Kelly, J., 232
Kennedy, Brendan J., 177, 200
Kepert, Cameron J. , 96, 277390

Kubota, Yoshiki , 257 , 334
Kuchar, Jason A. , 128
Kudoh,Ka~uya , 155
Kudoh , Y. , 109
Kuribayashi , M. , 144
Kuribayashi , T. , 109
Kurisu , Genji, 223
Kuroki , Ryota , 191 , 205
Kurosawa , Keiko, 191
Kusaba , Hajime, 198
Kusaka , Katsuhiro , 246
Kusunoki , Masami , 223
Kuwaki , Tomoaki , 191
Lang , S., 129
Langley, David B., 128, 226
Larsen , Sine , 168
Latham , Catherine F. , 120
Le Gall , Jean, 212
Lecomte , C., 299 , 313 , 356 , 374
Lee, Byung II , 170
Lee, Chi-Rung , 376
Lee, H.W., 209
Lee, Jey-Jau , 88, 265, 321
Lee, Lawrence K. , 209, 263
Lee , Mihwa H. , 127,211 , 224
Lee , Sujeong , 250
Lee , Tet Verne , 138
Lee , Yen-Ru, 175, 312 , 321
Leedman , PeterJ ., 115
Lelievre-Bema , E., 299
Lewis , R. A. , 256
Li , Chia Lung , 83
Li, Genpei , 117
Li , Hsou-min , 264
Li , Leqing , 177
Li , M.-R. , 95
Li , Simon , 228 , 285
Li , Y ., 342
Lii , Kwang-Hwa , 86
Liljas , Anders , 270 , 292
Lin , Guin-Gi , 175
Lin , Tsong-Tze , 312
Ling , Michael, 214
Listwan , Pawel , 113, 179, 227 , 286
Lithgow, Trevor, 215
Liu , J. W. , 271
Liu , Ming-Yih , 212
Liu , Xioxi , 331
Liyou , Nancy E., 120

Lott, J. Shaun , 138, 180, 218 ,
228, 285
Lou , M-Z , 274
Loupias , Genevieve , 339
Lovrecz, G. 0 ., 274
Lu , Tian-Huey, 94, 103
Luger, Peter, 305
Luu , Tien Hung , 163
Lyu , Ping-Chiang , 135
Macasev , Diana , 215
Macchi , Piero , 298
MacDonald , W. A., 216
Maeda, M ., 204
Maeda , Yoshitake, 205
Maher, Megan J., 125, 127,
211 , 224
Major, Zs ., 344
Makarov , 0 ., 294
Makker, J., 164
Malby, Robyn L. , 121
Mandagie , M. , 255
Manninen , S., 372
Mao , S.-Y., 95
Marangolo , M. , 339
Marto-Owusu , E., 258
Martin , Jennifer L. , 113, 120, 142,
179, 206 , 227 , 229 , 286
Martin , T . John, 140
Maruyama , Hiroshi , 173
Maruyama , Youhei, 154
Masuda , Jun , 273
Matsuda , Kazuyuki , 173
Matsuda , Ryotaro , 257 , 334
Matsuda, T. , 208
Matsui, Yoshio , 150
Matsukura , Yasuko , 205
Matsumoto , 1. , 325
Matsumoto, lsamu , 130
Matsumoto, Shinya, 197
Matsumura , H. , 208 , 231
Matsuo, Akira , 257 , 334
Matthews , Jacqueline M., 125
Maunders , C. J., 249
Mauri , F., 339
McAllister , William T., 80
McCarthy , Andrew A., 228 , 285
McCluskey, James , 216,261
McDowall , Alasdair, 260
Mcintyre , Garry J., 375
McKay, Joel , 138391

McKern, N. M. , 274
McKinnon, Joshua, 102, 319
McKinstry, William J. , 140, 219
Mcloughlin , S .Yu. , 271
McManus , Michael E. , 120
McMillan , Fiona M., 229
Meng, S., 319
Messerschmidt, Marc, 305
Mezouar, M., 339
Mi , J.-X. , 95
Michiue, Yuichi , 162
Mijnarends, P. E., 342
Mine , Shouhei , 205
Misaki , Shintaro , 116, 202
Mishima , Yoshinao , 278
Mita, Yoshimi , 257 , 334
Mitchell, J. F., 342
Mitsumori , Takahiro , 85
Miyabe , Yumiko, 203
Miyake , H. , 223
Miyamae, Hiroshi, 154, 155
Miyano, K., 240
Miyata, Yoshikazu , 246
Mizuno , Hiroshi, 124
Mizuno , M. , 325
Mochida , Tomoyuki , 174
Mochizuki , Kayoko , 130
Montano, P. A., 342
Moon , Hi-Soo , 250
Morgenstern-Badarau , Irene, 171
Mori , Mizuki , 145, 251
Mori,Takeharu, 145, 251 , 252 , 278
Mori, Yusuke, 105
Morikawa , M. , 208
Morikoshi , H., 109
Morimoto, Yukio, 273
Moritomo, Yutakata, 324
Morth, J.P., 178
Morton, Craig J., 140
Mostafa, G. , 94 , 103
Moubaraki , Boujemaa , 96
Mowbray , Sherry L., 169
Moylan , Michael , 97
Mukherjee, A. K. , 158
Murakami , Youichi , 240 , 360
Muramoto, Koji , 203
Murray, Keith S., 96
Mutrofin, Siti , 89
Nagae, Masamichi , 123
Nagasawa, H., 335

Nakagawa, Atsushi, 254 , 326
Nakagawa, Takeshi , 246
Nakamura , M., 240
Nakamura , N. , 106, 194, 195
Nakamura, Satoshi , 172
Nakaniwa, Tetsuko , 134
Nakao , Hironori, 360
Nakashima, Philip N. H. , 367
Nakayama , M. , 272
Namba, Keiichi , 281
Namikawa, Kazumichi, 173, 360
Nanao, S. , 188
Nara , Hisashi , 316
Ng , Susanna , 236
Nice, E. C., 274
Nicholson, Melissa , 112
Nii , H. , 272
Niimura, Nobuo, 161, 204 , 210
Nishi , Y ., 253
Nishibori, Eiji , 145, 156, 266 ,
324 , 327
Nishijima, C. , 238
Nishijima, Kazumi , 202
Nishikubo, Keiko, 198
Nishimura , Keiichiro , 134
Nishimura , Sigenori , 223
Nishiyama , Uichi, 191
Nitta, Katsutoshi , 205
Nitta, Yasunori , 223
Niwa, Yuusuke , 203
Nixon, K. L. , 363
Noda, Yukio , 174
Noguchi , K. , 136
Nozawa , Akira , 123
Nugent, K. A. , 256
Nygaard , Frank B., 168
O'Connor, Brian , 245
Oakeshott, J. G. , 271
Oakley, Aaron J. , 214, 217
Ochiai , Akira , 173
Oda, J , 272
Odo, Y., 110
Ogasahara , Kyoko , 137
Ogata , Y. , 365
Ogawa , Masaru , 156
Ogawa , Tomohisa , 203
Ogawa , Y., 106, 194
Ohashi , Yuji , 85 , 87 , 157, 161 , 253
Ohhara , Takashi , 87 , 161
Ohishi , Yasuo , 324

392

Pontillon , Y., 299
Porcher, F., 313
Porter, Corrine J., 81 , 115
Power, Barbara , 221
Pratap, J. V ., 122
Prescott, Mark, 214
Proft, Thomas, 112
Pucher, Andreas , 310
Purcell , Anthony W. , 21 3, 216 , 261
Purvia , V. , 320
Qiu , X. , 271
Quake , Stephen R. , 236
Quiocho , Florante A. , 287
Raabe , Gerhard , 244
Rabii, S., 339
Rabiller, P., 374
Radford , C., 319
Rae, A. David, 148, 242
Ragot, S., 350
Raina , Salish , 206
Ramsay, Rochelle J., 218,
228 , 285
Rani , P. G., 201
Raston , C. L. , 79
Ravasi , Timothy, 11 3, 179,
227,286
Reed , Lester J., 235
Riley, Daniel P., 166
Rixon , Frazer J., 287
Robinson , lan , 78
Robinson , R. A., 302
Robson , Richard , 97
Rodwell , Victor W., 273
Rogalev, Andrei , 307
Roos, Annette , 169
Rossjohn , Jamie , 213-216 , 261
Rossouw, C. J. , 249
Rothnagel , Rosalba , 260
Russell , R. J. , 271
Ryan , Michael T ., 220
Sanchez-Portal , Daniel , 346
Sabouri-Dodaran , A. A., 339
Saikrishnan , K., 84
Saitoh, Koh , 145
Sakai , Atsushi , 278
Sakai , Hisanobu, 225
Sakai , Hitomi , 266
Sakai , Masato, 155
Sakai , Nobuhiko , 311 , 320
Sakai , Takuo , 134

Ohmasa , Yoshinori , 196
Ohouchi , Kenjiro, 252
Ohoyama , Kenji , 278
Ohsato , H., 109, 160, 199
Ohsumi , Kazumasa , 246
Oikawa , Kenichi , 87 , 145
Oike, Hiromi , 308
Okabe , H. , 199
Okada , J. T. , 188
Okada , Y. , 195
Okamoto, Tomoyuki , 205
Okano, Y., 231
Okawa , T ., 199
Okazaki , N., 231
Okuda , T ., 241
Okuyama, K., 136
Ollis, David L. , 118, 271
Onoda , Mitsuko , 162, 185
Onuma , Etsuro , 140
Orchard , Simon , 97
Ordej6n , Pablo, 346
Ostermann, A. , 204
Oszawa , Tadashi , 257, 334
Ota , Minoru , 331 , 332
Overgaard , Jacob, 100, 189, 267 ,
322 , 357
Ozerov, Ruslan P., 329 , 330
Pailthorpe , Bernard, 260
Paramsivam , M ., 164
Parker, Emily, 218
Parker, Michael W., 140, 219 , 230 ,262
Parry, D. J., 256
Patlan , Vsevolod , 80
Paulus, M. , 335 , 373
Pearson , Arwen R., 126, 288
Pei-Tsung , Cheng , 135
Pendas , A. Martin , 377
Peng , Lian-Mao, 366
Peng, Peiyu , 135
Perry, L. J., 178
Pflugrath , J. W ., 233
Phyu , Khin Win , 88
Pietsch , Ullrich , 310
Piltz, Ross 0 ., 100, 269 , 318
Pink , Maren , 280
Placket!, Neil C. , 89
Pletnev, V ., 93
Podjarny, A., 356
Polekhina , Galina , 140, 219, 262

393

Sakashita , H., 160
Sakata , Makoto, 257 , 266 , 324 ,
326, 327, 334
Sakurai , Hiroshi, 173, 308, 331,
332
Sakurai , Y. , 188, 332, 370
Sanford , Vanessa , 152
Sanishvili , R. , 294
Sano , Hiroshi, 123
Sa no , Satoshi , 104, 192
Santi, G., 344
Sasaki, Takatomo , 105
Sashin , V. A., 362
Sasou , Hiroshi, 151
Satchell , Jacqueline F., 139
Sato , A. , 185
Sato , Ayano , 130
Sato , Koh , 140
Sato , Mamoru , 123, 133
Sato , Masaru , 104, 192, 193
Sato , Miharu , 205
Sato , S. , 149
Sauter, Daan , 152
Savin , Andreas, 351
Sawa , H., 240
Schulke , W., 335
Schmid , Siegbert, 184
Schmidberger, Jason W., 217
Schmidt , G., 335
Schmidt, Tim , 273
Schulze , Steffen , 163
Scobie , Judy, 215
Scott, Clare, 138
Seddon , John , 260
Sekar, K. , 84, 90 , 122, 201
Sekiguchi , Takeshi , 235
Self, Kyle, 236
Sen , Udayaditya, 119
Sennoga , Charles, 260
Seo , Won-Seon , 250
Serek, Robert, 227 , 286
Shankland , K. , 279
Sharma , B. K., 320
Sharma , S., 164
Sharpe , Miriam L. , 228 , 285
Sheik, S. S., 90
Shepard , Eric M., 226
Sherburn , MichaelS. , 242
Sherman , Mark, 221
Sheu , Hwo-Shuenn, 88

Shi , Weng-Shen , 198
Shibata , Naoki, 273
Shimizu , H. , 194
Shimizu , Shinji, 172
Shimizu , Toshiyuki , 123
Shimo , T., 110
Shimomura , Osamu , 173
Shimomura , Y. , 111
Shimuzu , Toshiyuki , 133
Shionyu-Mitsuyama , Clara , 203
Shiotani , N. , 325
Shirai , Kazuko , 197
Shirai , Y. , 325
Shiro , Motoo, 149, 197
Shishitani , H., 231
Shui, William M., 209
Shukla , Alok, 345
Sidiqi , Mahjooba , 222
Signorato , R. , 294
Sigrell, Jill, 180
Simmons , W. H., 224
Singh , R. K. , 164Singh , T. P. , 164
Sironi , Angelo , 298
Siu , K. K-W., 256
Skelton , Brian W., 89 , 152, 153
Smith , Brian J. , 139
Smith , Janet L. , 294
Smith , W. W. , 294
Sobolev, Alexandre N., 243 , 329
Soejima , Yuji , 196
Soininen , J. A. , 335
Soler, Jose M., 346
Somekawa , K. , 110
Souhassou , M. , 299 , 313, 374
Spackman , Mark, 102, 269 , 318,
319
Srinivasan , A. , 164
Stauffacher, Cynthia V. , 273
Stence , C. N., 233
Stepanov , S., 294
Sternemann , C., 335 , 373
Stetsko , Yuri P., 175, 312 , 32 1
Steussy, Nicklaus , 273
Stevenson , A. W., 256
Stojanovski , Diana , 220
Streltsov , Victor A. , 323 , 329 , 330 ,367
Suda , Katsumi , 275
Sugawara , Tadashi , 174394

Tang , Mau-Tsu , 3 12, 321
Tao , A ., 147
Tassel, Francis, 303
Tateishi , Kenji , 108
Taylor, J. W. , 344
Teh , T., 129
Temiakov , Dmitry, 80
Templer, Richard , 260
Tesh , K. F., 144, 233
Thakurta , Piyali Guha , 114
Thang , Ng . Q ., 237
Theodossiou , G. , 255
Thompson , Colin A. , 217
Tohdo , Y ., 199
Tokunaga , Masao , 205
Tokunaga , Naotoshi , 151
Tokura , Yoshinori , 360
Tolan , M ., 335 , 373
Toraya , Hideo , 143
Toraya , Tetsuo , 273
Torii , Shuki , 145
Tozaki , Ken-ichi , 151
Tran , C. Q ., 146, 247 , 248
Tresillian , Michael , 120
Tse , J. S. , 373
Tsirelson , Vladimir G. , 310
Tsuda , Kenji , 145, 365
Tsuji , Y ., 253
Tsukihara , Tomitake, 254
Tsunashima , Y ., 149
Tsunoda , Masaru , 235
Tucker, P. A ., 178
Tuji , Naruki , 360
Turner, Peter, 269 , 318
Tweten , Rodney K. , 230, 262
Udagawa , Yasuo , 364
Uekusa , Hidehiro , 85 , 157, 161 ,253
Umeda , Shun-ichi , 82
Unge, Torsten , 169
Uno, K., 106, 194, 195
Urade, Y., 231
Urakhchin , A. , 294
van Donkelaar, Albert, 221
Varghese , Jose, 295
Varshney, U., 84
Vassylyev, Dmitry G. , 80
Vasudevan , Subhash G ., 118
Venkatesh , J. , 84
Verman , B., 144

Suh , Se Won , 170
Sumi , T., 238
Sumita, M. , 149
Sun , Wen-Shien , 175, 312
Sun , Yuh-Ju, 135, 264
Sunami , Tomoko, 82 , 172
Surolia , A. , 122, 201
Suto , Kyoko , 124
Suzuki , Atsuo , 203
Suzuki , Kaoru , 235
Suzuki , Kenji , 275
Suzuki , Kenji , 202
Suzuki , Mamie , 172
Suzuki , Megumi , 257 , 334
Suzuki, Motohiro , 173
Suzuki , W. , 327
Tachibana , Masaru, 269 , 318
Tada, Toshiji , 134
Taguc.hi , Yasujiro, 360
Tahirov , Tahir H. , 80
Tajima , T ., 253
Takagi , S., 301
Takahashi , Masahiko , 364
Takahashi, Osamu , 207
Takahashi, Sachiko , 104, 192, 193
Takakura , Tomoaki , 116
Takano , Katsuyoshi , 308 , 331
Takano, Kazufumi , 105
Takao, Makoto , 134
Takata , Masaki, 145, 156, 257 ,
266 , 324,326,327 , 334
Takayama , Terufumi , 85
Takayama-Muromachi , Eiji, 150
Takenaka , Akio , 82, 172 , 235
Takeuchi , H ., 238
Takeuchi , S. , 188
Takimoto , Akio , 116
Tamada , Taro , 191, 205
Tamakawa , Kou~ . 268
Tamura , Norihiro , 155
Tamura , R., 188
Tanaka , H. , 327
Tanaka , Hiroaki , 104 , 192, 193
Tanaka , Hiroshi , 326
Tanaka , 1. , 238
Tanaka , lchiro , 161 , 204
Tanaka , Kiyoaki , 241 , 301 , 333
Tanaka , Masahiko , 145, 251 , 252 ,278
Tanaka , Michiyosh i, 167, 365

395

Vijayan , M., 84 , 122, 201
Vikram , P., 164
Vivian , Julian P. , 81 , 222
Volkov , A. , 355
Volmer, M., 335 , 373
Vong, Vo, 163, 237
Vas, M. , 362
Wada , H., 185
Wada , Tatsuo , 197
Wakabayashi, Y. , 240
Wakelin, Laurence P. G., 131
Waller, Mark P. , 189, 267 , 322 , 357
Walsh , Carmel , 227 , 286
Wang , Chih-Chieh , 376
Wang , Dacheng , 117
Wang , F., 363
Wang , Sheng , 117
Wang , Sue-Lein , 159
Wang, Yu , 265, 376
Ward , C. W. , 274
Watanabe , Mamoru , 162
Watanabe , Masashi , 174
Watanabe , N. , 238
Watanabe , Y. , 188
Watts , Kevin T. , 126
Watts , R. , 344
Webb , Andrew Z., 21 3Weber, T , 182
Weigold , E. , 362
Welberry, T. R. , 183
Wells , Christine , 113, 179, 227 ,286
Whisstock, James C. , 261
Whitaker, Claire R., 89
White , Allan H., 89 , 152, 153, 243
White, T. J. , 107, 276
Whitfield , H. J., 249
Whittaker, James W., 171
Whitten , Andrew, 269 , 318, 31 9
Wilce, Jacqueline A. , 81 , 115, 222 ,234
Wilce, Matthew C. J., 81 , 115, 217 ,
222 , 232 , 234
Wilkins, S. W. , 256 , 304
Williams, E. A ., 232
Williams , Peter, 100
Williamson , N . A. , 219
Willis , Anthony. C. , 242
Wilmann , Pascal G. , 214 , 215
Wilmot, Carrie M., 126, 288

Winkler, D. A. , 363
Withers , R. L. , 183
Wolff, Stephen , 190, 338
Wong , Raymond K., 209
Wong , Shih-Chang , 175, 312
Wright, Natasha, 255
Wu , Anna M., 221
Xiang , Ye, 117
Xu, Chao-Nan , 198
Xu , S., 294
Xu , X., 136
Xu, Yibin , 118
Yagi , Shigeo , 116
Yamada , Hiroshi, 198
Yamagata , Yuriko , 137
Yamaguchi , Asako , 134
Yamaguchi , Yasuo , 278
Yamamoto, Keisuke, 278
Yamamoto, Masaki , 254
Yamamoto, T., 208
Yamane , Takashi , 203
Yamashita , Eiki , 254
Yamauchi , Hisao, 150
Yang, C. , 144, 233
Yang , H., 271
Yang , Jin Kuk , 170
Yashima , Masatomo, 145, 251 ,
252 , 278
Yasuda , Nobuhiro, 157
Yasui , Masanori , 156, 268
Yasuoka , Noritake, 124
Yatsunami , Rie , 172
Yazaki , Paul , 221
Yokosawa , Tadahiro , 150
Yokoyama , Shigeyuki , 80 , 181 , 284
Yokoyama , Y. , 188
Yoon , Hye-Jin , 170
Yoshikawa , Shinya , 254
Yoshimine, Takashi , 193
Yoshimura , Masashi , 105
Yoshimura , Masato, 254
Yoshimura , Yukio , 151
Yoshioka , Takayuki , 116
Yoshitomi , Susumu , 104, 192, 193
Young , Jr. , Victor G., 280
Young , Paul R. , 229
Yuan , Hanna S. , 83
Yufit, Dima S., 375
Yutani , Katsuhide , 137
Zhang , Rongguang , 118396

Zhang , Zhaom ing , 200 , 239
Zhao , J.-T., 95
Zhou , Z. Hong, 287

397

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