Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume 65, Part 12 (December 2009)
Copyright (c) International Union of Crystallography 2009


[Issue Author Index][Volume Author Index]

RIKEN-UK structural genomics


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Acta Cryst. (2009). F65, 1200-1203
[ doi:10.1107/S1744309109043772 ]

Structure of hypothetical Mo-cofactor biosynthesis protein B (ST2315) from Sulfolobus tokodaii

S. V. Antonyuk, R. W. Strange, M. J. Ellis, Y. Bessho, S. Kuramitsu, A. Shinkai, S. Yokoyama and S. S. Hasnain

Synopsis: The structure of a protein involved in the molybdopterin and molybdenum co-factor biosynthesis pathways of Sulfolobus tokodaii has been solved to a resolution of 1.9 Å.

PDB reference: 3iwt

Online 27 November 2009


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Acta Cryst. (2009). F65, 1204-1208
[ doi:10.1107/S1744309109043814 ]

Structure of SurE protein from Aquifex aeolicus VF5 at 1.5 Å resolution

S. V. Antonyuk, M. J. Ellis, R. W. Strange, Y. Bessho, S. Kuramitsu, A. Shinkai, S. Yokoyama and S. S. Hasnain

Synopsis: The structure of the stationary phase survival protein SurE protein from the hyperthermophile Aquifex aeolicus has been solved to 1.5 Å resolution. The divalent-metal-ion-dependent phosphatase active-site pocket is occupied by sulfate ions from the crystallization medium.

PDB reference: 2wqk

Online 27 November 2009


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Acta Cryst. (2009). F65, 1209-1213
[ doi:10.1107/S1744309109044935 ]

Structure of D-lactate dehydrogenase from Aquifex aeolicus complexed with NAD+ and lactic acid (or pyruvate)

S. V. Antonyuk, R. W. Strange, M. J. Ellis, Y. Bessho, S. Kuramitsu, Y. Inoue, S. Yokoyama and S. S. Hasnain

Synopsis: The structure of D-lactate dehydrogenase from Aquifex aeolicus has been determined with each subunit of the homodimer in a `closed' conformation and with the NAD+ cofactor and lactate (or pyruvate) bound at the inter-domain active-site cleft.

PDB reference: 3kb6

Online 27 November 2009


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Acta Cryst. (2009). F65, 1214-1217
[ doi:10.1107/S1744309109044923 ]

The structure of an archaeal ribose-5-phosphate isomerase from Methanocaldococcus jannaschii (MJ1603)

R. W. Strange, S. V. Antonyuk, M. J. Ellis, Y. Bessho, S. Kuramitsu, S. Yokoyama and S. S. Hasnain

Synopsis: The structure of ribose-5-phosphate isomerase from Methanocaldococcus jannaschii has been solved to 1.78 Å resolution, with the active site occupied by two molecules of propylene glycol mimicking the binding of a known arabinose-5-phosphate inhibitor.

PDB reference: 3ixq

Online 27 November 2009


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Acta Cryst. (2009). F65, 1218-1221
[ doi:10.1107/S1744309109046302 ]

Structure of a putative [beta]-phosphoglucomutase (TM1254) from Thermotoga maritima

R. W. Strange, S. V. Antonyuk, M. J. Ellis, Y. Bessho, S. Kuramitsu, A. Shinkai, S. Yokoyama and S. S. Hasnain

Synopsis: The structure of a putative [beta]-phosphoglucomutase from Thermotoga maritima belonging to the haloacid dehalogenase (HAD) hydrolase family has been determined to 1.74 Å resolution.

PDB reference: 3kbb

Online 27 November 2009


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Acta Cryst. (2009). F65, 1222-1226
[ doi:10.1107/S174430910904651X ]

Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii

B. Padmanabhan, R. W. Strange, S. V. Antonyuk, M. J. Ellis, S. S. Hasnain, H. Iino, Y. Agari, Y. Bessho and S. Yokoyama

Synopsis: The crystal structure of dihydrodipicolinate synthase from the (S)-lysine synthesis pathway of Methanocaldococcus jannaschii has been solved to 2.2 Å resolution, revealing a functional homotetramer.

PDB reference: 2yxg

Online 27 November 2009


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Acta Cryst. (2009). F65, 1227-1233
[ doi:10.1107/S1744309109047046 ]

Structure of glyceraldehyde-3-phosphate dehydrogenase from the archaeal hyperthermophile Methanocaldococcus jannaschii

A. D. Malay, Y. Bessho, M. J. Ellis, S. V. Antonyuk, R. W. Strange, S. S. Hasnain, A. Shinkai, B. Padmanabhan and S. Yokoyama

Synopsis: The structure of glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanocaldococcus jannaschii was determined to 1.81 Å resolution with the NADP+ cofactor at the nucleotide binding site.

PDB reference: 2yyy

Online 27 November 2009


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Acta Cryst. (2009). F65, 1234-1239
[ doi:10.1107/S1744309109050052 ]

Structure of putative 4-amino-4-deoxychorismate lyase from Thermus thermophilus HB8

B. Padmanabhan, Y. Bessho, A. Ebihara, S. V. Antonyuk, M. J. Ellis, R. W. Strange, S. Kuramitsu, N. Watanabe, S. S. Hasnain and S. Yokoyama

Synopsis: The putative 4-amino-4-deoxychorismate lyase (TTHA0621) from T. thermophilus HB8 was cloned, overexpressed, purified and crystallized. Its crystal structure was determined by a combination of SAD and molecular-replacement methods and was refined to 1.93 Å resolution.

PDB reference: 2zgi

Online 27 November 2009


structural communications


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Acta Cryst. (2009). F65, 1240-1245
[ doi:10.1107/S1744309109033788 ]

Crystallization and X-ray structure of cold-shock protein E from Salmonella typhimurium

H. P. Morgan, M. A. Wear, I. McNae, M. P. Gallagher and M. D. Walkinshaw

Synopsis: The crystal structure of cold-shock protein E from S. typhimurium (StCspE) has been determined at 1.1 Å resolution.

PDB reference: 3i2z

Online 27 November 2009


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Acta Cryst. (2009). F65, 1246-1253
[ doi:10.1107/S1744309109041670 ]

Structure of human glycolate oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole

J.-M. Bourhis, C. Vignaud, N. Pietrancosta, F. Guéritte, D. Guénard, F. Lederer and Y. Lindqvist

Synopsis: The crystal structure of human glycolate oxidase in complex with an inhibitor is described. A comparison with complexes with other inhibitors and with structures of homologous enzymes is given.

PDB reference: 2w0u

Online 27 November 2009


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Acta Cryst. (2009). F65, 1254-1257
[ doi:10.1107/S1744309109043267 ]

Structure of the first PDZ domain of human PSD-93

M. Fiorentini, A. K. Nielsen, O. Kristensen, J. S. Kastrup and M. Gajhede

Synopsis: This article describes the trimeric structure of the first PDZ domain of human PSD-93 at 2 Å resolution.

PDB reference: 2wl7

Online 27 November 2009


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Acta Cryst. (2009). F65, 1258-1260
[ doi:10.1107/S1744309109043152 ]

The high-resolution structure of the extracellular domain of human CD69 using a novel polymer

P. Kolenko, T. Skálová, O. Vanek, A. Stepánková, J. Dusková, J. Hasek, K. Bezouska and J. Dohnálek

Synopsis: The structure of the extracellular domain of human CD69 was crystallized using a novel polymer precipitant: di[poly(ethylene glycol)] adipate. The structure was refined at 1.37 Å resolution.

PDB reference: 3hup

Online 27 November 2009


crystallization communications


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Acta Cryst. (2009). F65, 1261-1263
[ doi:10.1107/S1744309109038007 ]

Preliminary crystallographic analysis of mouse Elf3 C-terminal DNA-binding domain in complex with type II TGF-[beta] receptor promoter DNA

V. B. Agarkar, N. D. Babayeva, A. Rizzino and T. H. Tahirov

Synopsis: The cloning, expression, purification and crystallization of the mouse Elf3 C-terminal DNA-binding domain in complex with mouse type II TGF-[beta] receptor promoter DNA are reported. The crystals were characterized and an X-ray diffraction data set was collected to a resolution of 2.2 Å.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1264-1266
[ doi:10.1107/S1744309109041992 ]

Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophages

N. Silva-Martin, J. D. Schauer, C. G. Park and J. A. Hermoso

Synopsis: The carbohydrate-recognition domain of the SIGN-R1 receptor from M. musculus has been crystallized by the hanging-drop vapour-diffusion method. A native data set has been collected to 1.87 Å resolution.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1267-1270
[ doi:10.1107/S1744309109043127 ]

Purification, crystallization and preliminary X-ray analysis of a deletion mutant of a major buckwheat allergen

Y. Kezuka, T. Itagaki, R. Satoh, R. Teshima and T. Nonaka

Synopsis: A 16 kDa buckwheat protein (BWp16) is a major allergen responsible for immediate hypersensitivity reactions including anaphylaxis. An immunologically active mutant of BWp16 was prepared and a three-wavelength MAD data set was collected from a crystal of selenomethionine-labelled mutant protein.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1271-1273
[ doi:10.1107/S1744309109043115 ]

Expression, crystallization and preliminary X-ray diffraction analysis of a modification subunit of a putative type I restriction enzyme from Vibrio vulnificus YJ016

H.-J. Lee, K. Nishi, J.-M. Song and J.-S. Kim

Synopsis: The crystallization of an HsdM subunit, a component of the methyltransferase of a putative type I restriction enzyme, from V. vulnificus YJ016 and the collection of diffraction data to 1.86 Å resolution are reported.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1274-1276
[ doi:10.1107/S1744309109043395 ]

Crystallization of selenomethionyl exo-[beta]-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium

T. Ishida, Z. Fujimoto, H. Ichinose, K. Igarashi, S. Kaneko and M. Samejima

Synopsis: Selenomethionyl exo-[beta]-1,3-galactanase from P. chrysosporium K-3 produced in Pichia pastoris was crystallized. The crystals diffracted to a resolution of 1.8 Å and belonged to space group P21.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1277-1281
[ doi:10.1107/S1744309109044571 ]

The taming of small heat-shock proteins: crystallization of the [alpha]-crystallin domain from human Hsp27

E. V. Baranova, S. Beelen, N. B. Gusev and S. V. Strelkov

Synopsis: A procedure for obtaining diffraction-quality crystals of the [alpha]-crystallin domain from human small heat-shock protein 27 with the help of limited proteolysis and rational surface mutagenesis is described.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1282-1284
[ doi:10.1107/S1744309109044479 ]

Purification, crystallization and preliminary X-ray analysis of the PCNA2-PCNA3 complex from Sulfolobus tokodaii strain 7

A. Kawai, S. Higuchi, M. Tsunoda, K. T. Nakamura and S. Miyamoto

Synopsis: A PCNA2-PCNA3 complex which has recently been identified from S. tokodaii strain 7 was overexpressed, purified and crystallized in two crystal forms.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1285-1288
[ doi:10.1107/S1744309109044789 ]

Crystallization and preliminary X-ray diffraction studies of FAD synthetase from Corynebacterium ammoniagenes

B. Herguedas, M. Martínez-Júlvez, S. Frago, M. Medina and J. A. Hermoso

Synopsis: Native and selenomethionine-labelled FAD synthetase from C. ammoniagenes have been crystallized by the hanging-drop vapour-diffusion method. A MAD data set for SeMet-labelled FAD synthetase was collected to 2.42 Å resolution, while data sets were collected to 1.95 Å resolution for the native crystals.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1289-1291
[ doi:10.1107/S1744309109045059 ]

Preliminary crystallographic studies of purine nucleoside phosphorylase from the cariogenic pathogen Streptococcus mutans

Q.-M. Hou, X. Liu, E. Brostromer, L.-F. Li and X.-D. Su

Synopsis: Purine nucleoside phosphorylase (PNP), which is a pivotal enzyme in the nucleotide-salvage pathway, has been expressed in Escherichia coli strain BL21 (DE3) in a soluble form at a high level. After purification of the PNP enzyme, the protein was crystallized using the sitting-drop vapour-diffusion technique.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1292-1295
[ doi:10.1107/S1744309109045382 ]

Crystallization and preliminary X-ray analysis of a monomeric mutant of Azami-Green (mAG), an Aequorea victoria green fluorescent protein-like green-emitting fluorescent protein from the stony coral Galaxea fascicularis

T. Ebisawa, A. Yamamura, Y. Kameda, K. Hayakawa, K. Nagata and M. Tanokura

Synopsis: A monomeric mutant of Azami-Green from G. fascicularis was expressed, purified and crystallized using the sitting-drop vapour-diffusion method. The crystal belonged to space group P1 and diffracted X-rays to 2.20 Å resolution.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1296-1298
[ doi:10.1107/S1744309109046119 ]

Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase from Nitrosomonas europaea

P. E. Cedervall, A. B. Hooper and C. M. Wilmot

Synopsis: A new crystal form of N. europaea hydroxylamine oxidoreductase (space group P21212) diffracted to 2.25 Å resolution at a third-generation synchrotron X-ray source.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1299-1301
[ doi:10.1107/S174430910904603X ]

Crystallization and preliminary X-ray analysis of neoagarobiose hydrolase from Saccharophagus degradans 2-40

S. Lee, J. Y. Lee, S. C. Ha, J. Jung, D. H. Shin, K.-H. Kim and I.-G. Choi

Synopsis: Neoagarobiose hydrolase from the marine bacterium Saccharophagus degradans 2-40 was overexpressed in Escherichia coli and crystallized in the monoclinic space group C2, with unit-cell parameters a = 129.83, b = 76.81, c = 90.11 Å, [beta] = 101.86°.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1302-1305
[ doi:10.1107/S1744309109046181 ]

Purification, crystallization and initial X-ray diffraction study of human REV7 in complex with a REV3 fragment

K. Hara, T. Shimizu, S. Unzai, S. Akashi, M. Sato and H. Hashimoto

Synopsis: The crystallization and initial X-ray diffraction of REV7 in complex with REV3 is reported.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1306-1308
[ doi:10.1107/S1744309109046697 ]

Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell's viper venom

D. Nakayama, Y. Ben Ammar and S. Takeda

Synopsis: The crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase are reported. The best crystal diffracted to 1.9 Å resolution.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1309-1312
[ doi:10.1107/S1744309109047381 ]

Crystallization and preliminary crystallographic characterization of glutamine synthetase from Medicago truncatula

A. R. Seabra, H. Carvalho and P. J. B. Pereira

Synopsis: The enzyme glutamine synthetase from M. truncatula has been expressed, purified and crystallized. The crystals belonged to the monoclinic space group P21 and diffracted to 2.35 Å resolution.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1313-1316
[ doi:10.1107/S1744309109047319 ]

Expression, purification, crystallization and preliminary X-ray analysis of maleylacetate reductase from Burkholderia sp. strain SJ98

A. Chauhan, Z. Islam, R. K. Jain and S. Karthikeyan

Synopsis: Purification and preliminary X-ray crystallographic analysis of maleylacetate reductase encoded by the pnpD gene is reported.

Online 27 November 2009


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Acta Cryst. (2009). F65, 1317-1319
[ doi:10.1107/S1744309109047393 ]

Purification, crystallization and preliminary crystallographic analysis of a thermostable endonuclease IV from Thermotoga maritima

R. C. Hughes, S. J. Tomanicek, J. D. Ng and L. Coates

Synopsis: The overexpression, purification and crystallization of endonuclease IV from T. maritima are reported. The crystals belonged to the hexagonal space group P61 and diffracted to 2.36 Å resolution.

Online 27 November 2009