issue contents

ISSN: 2053-230X

February 2008 issue

Highlighted illustration

Cover illustration: Structure of human serum albumin with S-naproxen and the GA module (Lejon, Cramer & Nordberg, p. 64).


Acta Cryst. (2008). F64, 63
doi: 10.1107/S1744309108000134

protein structure communications

Acta Cryst. (2008). F64, 64-69
doi: 10.1107/S174430910706770X
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The crystal structure of the complex formed by human serum albumin and a bacterial albumin-binding domain with the drug compound naproxen and fatty acid decanoate bound to albumin is described.

Acta Cryst. (2008). F64, 70-76
doi: 10.1107/S1744309107068236

crystallization communications

Acta Cryst. (2008). F64, 77-80
doi: 10.1107/S1744309107067437
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The cloning, expression, purification, crystallization and preliminary X-ray characterization of a novel class of cohesin module (type III) from the R. flavefaciens ScaE anchoring scaffoldin are described.

Acta Cryst. (2008). F64, 81-84
doi: 10.1107/S1744309107067930
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The cloning, expression, purification, crystallization and preliminary X-ray crystallographic studies of mannose 6-phosphate isomerase from S. typhimurium are reported.

Acta Cryst. (2008). F64, 85-87
doi: 10.1107/S174430910706825X
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Glutathione S-transferase from X. fastidiosa (xfGST) has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.23 Å.

Acta Cryst. (2008). F64, 88-90
doi: 10.1107/S1744309107068522
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A 2.8 Å resolution data set was collected from a crystal of a recombinant plant aminoaldehyde dehydrogenase from P. sativum. This enzyme oxidizes ω-aminoaldehydes arising from polyamine degradation.

Acta Cryst. (2008). F64, 91-93
doi: 10.1107/S1744309107068649

Acta Cryst. (2008). F64, 94-97
doi: 10.1107/S1744309108000055
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The first crystallization of a W. pipientis protein, α-DsbA1, was achieved using hanging-drop and sitting-drop vapour diffusion.

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Selenomethionine-substituted IDH was crystallized using the microbatch method. The crystals diffracted to beyond 2.0 Å resolution using synchrotron radiation.

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The ribosomal protein (L30e) from M. jannaschii was cloned from the gene MJ1044, expressed, purified and crystallized. The crystal belongs to the primitive tetragonal space group P43 and diffracted to 1.9 Å resolution.

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The 6-pyruvoyltetrahydropterin synthase from E. coli has been crystallized in two crystal forms. Diffraction data were collected from hexagonal- and rectangular-shaped crystals to 3.0 and 2.3 Å, respectively.

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To investigate the mechanism by which P58(IPK) functions to promote protein folding within the ER, a P58(IPK) TPR fragment without the C-terminal J-domain has been crystallized.

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The Neisseria meningitidis genome possesses three genes encoding active DsbAs. To throw light on the reason for this genetic multiplicity, the three enzymes have been purified and crystallized.

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Crystals of the carbohydrate-recognition domain of human langerin were obtained that diffracted synchrotron radiation to 1.5 Å resolution.

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B. subtilis queD was overexpressed, purified and crystallized. A diffraction data set was collected to a resolution of 3.6 Å.

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The extracellular rubber-degrading enzyme rubber oxygenase A (RoxA) from Xanthomonas sp. strain 35Y has been crystallized and diffraction data have been collected to high resolution.

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APH(2′′)-Ic is an enzyme that is responsible for high-level gentamicin resistance in E. gallinarum isolates. Crystals of the wild-type enzyme and three mutants have been prepared and a complete X-ray diffraction data set was collected to 2.15 Å resolution from an F108L crystal.

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A nickel uptake regulator (Nur) from Streptomyces coelicolor has been crystallized. A 2.4 Å native data set and a 3.0 Å Ni-MAD data set were collected using synchrotron radiation.

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Human calbindin-D28k has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.4 Å resolution.

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Three mutants of the haloalkane dehalogenase DhaA derived from R. rhodochrous NCIMB 13064 were crystallized and diffracted to ultrahigh resolution.

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The S. pyogenes laminin-binding protein Lbp, which is essential for adhesion to human laminin, has been expressed, purified and crystallized.

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The overproduction, purification, crystallization and preliminary crystallographic studies of the native and selenomethionine-labelled P1 domain are reported here as a first step towards the elucidation of the molecular mechanism of YidC as a membrane-protein insertase.

international union of crystallography

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