Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 11 (November 2005)



[Issue Author Index][Volume Author Index]
[Cover illustration] Cover illustration: The ybeY protein from Escherichia coli (p. 959).

structural genomics communications


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Acta Cryst. (2005). F61, 959-963  [ doi:10.1107/S1744309105031131 ]

The ybeY protein from Escherichia coli is a metalloprotein

C. Zhan, E. V. Fedorov, W. Shi, U. A. Ramagopal, R. Thirumuruhan, B. A. Manjasetty, S. C. Almo, A. Fiser, M. R. Chance and A. A. Fedorov

Synopsis: The ybeY protein from E. coli is reported at a 2.7  Å resolution with a metal ion.

PDB reference: 1xm5

Online 20 October 2005


protein structure communications


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Acta Cryst. (2005). F61, 964-966  [ doi:10.1107/S1744309105033257 ]

Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer

T. Xu, A. Ooi, H. C. Lee, R. Wilmouth, D. X. Liu and J. Lescar

Synopsis: An orthorhombic crystal form of the SARS CoV main proteinase diffracting to a resolution of 1.9  Å is reported. The conformation of residues in the catalytic site indicates an active enzyme.

PDB reference: 2c3s

Online 20 October 2005


crystallization communications


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Acta Cryst. (2005). F61, 967-970  [ doi:10.1107/S174430910502885X ]

Superoxide reductase from the syphilis spirochete Treponema pallidum: crystallization and structure determination using soft X-rays

T. Santos-Silva, J. Trincão, A. L. Carvalho, C. Bonifácio, F. Auchère, I. Moura, J. J. G. Moura and M. J. Romão

Synopsis: Superoxide reductase is a non-haem iron-containing protein involved in resistance to oxidative stress. The oxidized form of the protein has been crystallized and its three-dimensional structure solved. A highly redundant X-ray diffraction data set was collected on a rotating-anode generator using Cu  K[alpha] X-ray radiation. Four Fe atoms were located in the asymmetric unit corresponding to four protein molecules arranged as a dimer of homodimers.

Online 20 October 2005


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Acta Cryst. (2005). F61, 971-973  [ doi:10.1107/S1744309105030927 ]

Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast

T. Umehara, Y. Otta, K. Tsuganezawa, T. Matsumoto, A. Tanaka, M. Horikoshi, B. Padmanabhan and S. Yokoyama

Synopsis: The histone chaperone cia1 from fission yeast has been overexpressed in E. coli, purified and crystallized using the vapour-diffusion method.

Online 20 October 2005


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Acta Cryst. (2005). F61, 974-977  [ doi:10.1107/S1744309105030939 ]

Cloning, purification, crystallization and preliminary X-ray diffraction analysis of nitrile hydratase from the themophilic Bacillus smithii SC-J05-1

S. Hourai, T. Ishii, M. Miki, Y. Takashima, S. Mitsuda and K. Yanagi

Synopsis: The nitrile hydratase from the themophilic B. smithii SC-J05-1 (Bs NHase) has been purified, cloned and crystallized.

Online 20 October 2005


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Acta Cryst. (2005). F61, 978-980  [ doi:10.1107/S1744309105031982 ]

Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase

A. Yanuar, S. Sakurai, K. Kitano and T. Hakoshima

Synopsis: Human Rad has been crystallized. A diffraction data set was collected to a resolution of 1.8  Å.

Online 20 October 2005


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Acta Cryst. (2005). F61, 981-984  [ doi:10.1107/S1744309105032410 ]

Crystallization and preliminary X-ray diffraction analysis of apolipoprotein E-containing lipoprotein particles

Y. Newhouse, C. Peters-Libeu and K. H. Weisgraber

Synopsis: Further understanding of the structure and function of plasma apolipoproteins requires the determination of their high-resolution structures when complexed with lipids. In these studies, the production of homogeneous, biologically active lipoprotein particles of apolipoprotein E complexed with dipalmitoylphosphatidylcholine and their crystallization and X-ray diffraction are demonstrated.

Online 20 October 2005


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Acta Cryst. (2005). F61, 985-988  [ doi:10.1107/S1744309105032148 ]

Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of Ss-LrpB, a transcription regulator from Sulfolobus solfataricus

E. Peeters, B. T. M. Hoa, I. Zegers, D. Charlier and D. Maes

Synopsis: The C-terminal domain of the transcriptional regulator Ss-LrpB from S. solfataricus was purified by affinity chromatography and crystallized. Crystals belong to space group P21212. A complete data set was collected to a resolution of 2  Å.

Online 20 October 2005


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Acta Cryst. (2005). F61, 989-993  [ doi:10.1107/S1744309105032999 ]

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the VP8* carbohydrate-binding protein of the human rotavirus strain Wa

M. J. Kraschnefski, S. A. Scott, G. Holloway, B. S. Coulson, M. von Itzstein and H. Blanchard

Synopsis: The carbohydrate-binding component (VP8*64-223) of the human Wa rotavirus spike protein has been overexpressed in E. coli, purified and crystallized in two different crystal forms. X-ray diffraction data have been collected that have enabled determination of the Wa VP8*64-223 structure by molecular replacement.

Online 20 October 2005


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Acta Cryst. (2005). F61, 994-996  [ doi:10.1107/S174430910503318X ]

Crystallization and preliminary X-ray analysis of the isomerase domain of glucosamine-6-phosphate synthase from Candida albicans

J. Olchowy, R. Jedrzejczak, S. Milewski and W. Rypniewski

Synopsis: The isomerase domain of glucosamine-6-phosphate synthase from C. albicans has been crystallized and X-ray diffraction data have been collected. Preliminary analysis of the data reveals the oligomeric structure of the eukaryotic synthase to be a `dimer' of prokaryotic-like dimers.

Online 20 October 2005


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Acta Cryst. (2005). F61, 997-999  [ doi:10.1107/S1744309105033671 ]

Crystallization and preliminary X-ray diffraction analysis of HML, a lectin from the red marine alga Hypnea musciformis

C. S. Nagano, F. Gallego del Sol, B. S. Cavada, K. S. Nascimento, E. V. Nunes, A. H. Sampaio and J. J. Calvete

Synopsis: The crystallization and preliminary X-ray diffraction analysis of a red marine alga lectin isolated from H. musciformis is reported.

Online 20 October 2005


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Acta Cryst. (2005). F61, 1000-1002  [ doi:10.1107/S1744309105033014 ]

Crystallization and preliminary X-ray crystallographic analysis of the Sulfolobus solfataricus nucleotide-exchange factor 1[beta]

A. Ruggiero, M. Masullo, P. Arcari, G. Raimo, L. Vitagliano and A. Zagari

Synopsis: Nucleotide-exchange factor from S. solfataricus (SsEF-1[beta]) has been successfully crystallized. X-ray diffraction data have been collected from the native enzyme and from the selenomethionine derivative of SsEF-1[beta] to 1.97 and 1.83  Å resolution, respectively.

Online 25 October 2005


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Acta Cryst. (2005). F61, 1003-1005  [ doi:10.1107/S1744309105033245 ]

Overexpression, purification and crystallization of tyrosyl-tRNA synthetase from the hyperthermophilic archaeon Aeropyrum pernix K1

J. Iwaki, R. Suzuki, Z. Fujimoto, M. Momma, A. Kuno and T. Hasegawa

Synopsis: Tyrosyl-tRNA synthetase from the hyperthermophilic archaeon A. pernix K1 was cloned, purified and crystallized. The crystals belonged to the tetragonal space group P43212, with unit-cell parameters a = b = 66.1, c = 196.2  Å, and diffracted to beyond 2.15  Å resolution at 100  K.

Online 25 October 2005


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Acta Cryst. (2005). F61, 1006-1008  [ doi:10.1107/S1744309105033464 ]

Cloning, purification, crystallization and preliminary crystallographic analysis of a penicillin-binding protein homologue from Pyrococcus abyssi

V. Delfosse, J.-E. Hugonnet, W. Sougakoff and C. Mayer

Synopsis: The crystallization of a hypothetical penicillin-binding protein from the archaeon P. abyssi in space group C2 by hanging-drop vapour diffusion is reported.

Online 25 October 2005


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Acta Cryst. (2005). F61, 1009-1012  [ doi:10.1107/S1744309105033506 ]

Crystallization and preliminary X-ray analysis of the Pax6 paired domain bound to the Pax6 gene enhancer

M. Ito, T. Oyama, K. Okazaki and K. Morikawa

Synopsis: The mammalian Pax6 paired domain has been cocrystallizaed with a 25  bp DNA fragment of the Pax6 gene enhancer.

Online 25 October 2005


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Acta Cryst. (2005). F61, 1013-1016  [ doi:10.1107/S1744309105033737 ]

Preparation, crystallization and X-ray diffraction analysis to 1.5  Å resolution of rat cysteine dioxygenase, a mononuclear iron enzyme responsible for cysteine thiol oxidation

C. R. Simmons, Q. Hao and M. H. Stipanuk

Synopsis: Recombinant rat cysteine dioxygenase (CDO) has been expressed, purified and crystallized and X-ray diffraction data have been collected to 1.5  Å resolution.

Online 25 October 2005


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Acta Cryst. (2005). F61, 1017-1019  [ doi:10.1107/S1744309105034330 ]

Crystallization and preliminary X-ray crystallographic studies of fatty acid-CoA racemase from Mycobacterium tuberculosis H37Rv

K.-H. Rhee, K. S. Lee, A. Priyadarshi, E. E. Kim and K. Y. Hwang

Synopsis: Fatty acid-CoA racemase from M. tuberculosis H37Rv has been overexpressed, purified and crystallized. Diffraction data have been collected to beyond 2.7  Å resolution using a synchrotron-radiation source.

Online 28 October 2005


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Acta Cryst. (2005). F61, 1020-1022  [ doi:10.1107/S1744309105034329 ]

Crystallization and preliminary X-ray crystallographic analysis of the GluR0 ligand-binding core from Nostoc punctiforme

J. H. Lee, S. J. Park, S.-H. Rho, Y. J. Im, M.-K. Kim, G. B. Kang and S. H. Eom

Synopsis: The GluR0 ligand-binding core from N. punctiforme was expressed, purified and crystallized in the presence of L-glutamate. A diffraction data set was collected to a resolution of 2.1  Å.

Online 28 October 2005


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Acta Cryst. (2005). F61, 1023-1026  [ doi:10.1107/S1744309105033221 ]

Crystallization and X-ray diffraction properties of Baeyer-Villiger monooxygenase MtmOIV from the mithramycin biosynthetic pathway in Streptomyces argillaceus

C. Wang, M. Gibson, J. Rohr and M. A. Oliveira

Synopsis: Crystals of the type I Baeyer-Villiger monooxygenase (BVMO) MtmOIV from the biosynthetic pathway of mithramycin were obtained; the crystals diffracted to 2.69  Å resolution and belong to the monoclinic space group C2 (a = 143.5, b = 114.2, c = 137.8  Å [beta] = 102.5°). Light scattering indicates that MtmOIV is a dimer of 127  kDa in solution, while in the crystalline state the data are consistent with two dimers in the asymmetric unit.

Online 28 October 2005


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