issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

July 2007 issue

Highlighted illustration

Cover illustration: The hypothetical protein PF0899 from Pyrococcus furiosus [Clancy Kelley et al. (2007), Acta Cryst. F63, 549-552].

protein structure communications


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The X-ray crystal structure of the ThDP-dependent enzyme benzaldehyde lyase has been refined to 1.65 Å.

structural genomics communications


crystallization communications


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A phosphotriesterase (PTE) from the hyperthermophilic archaeon S. solfataricus has been crystallized. Combined with biochemical and bioengineering studies, it is expected that the structure of this protein will provide insight into the natural function of the PTE family and provide important data for achieving an efficient organophosphate biodecontaminant.

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Crystals of the oxygenase component (HpaB) of 4-hydroxyphenylacetate 3-monooxygenase from T. thermophilus HB8 were obtained which diffracted synchrotron X-rays to a resolution of 1.6 Å.

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To clarify the structural basis of sugar binding by BxlE at the atomic level, recombinant BxlE was crystallized using the hanging-drop vapour-diffusion method at 290 K.

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The catabolic ornithine transcarbamylase (cOTC) from L. hilgardii has been overexpressed in E. coli, purified and crystallized under two different experimental conditions. The structure has been solved by the molecular-replacement method using the atomic coordinates of catabolic ornithine transcarbamylase from P. aeruginosa as the search model.

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Recombinant SOS3 and SOS2 regulatory domain from A. thaliana have been coexpressed in E. coli, purified and crystallized by the hanging-drop vapour-diffusion method. An X-ray data set has been collected at 2.0 Å resolution.

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E. coli WrbA, the founding member of a novel flavoprotein family, was crystallized in complex with its physiological cofactor. Preliminary diffraction analysis is reported.

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An acridone-producing novel type III polyketide synthase from H. serrata has been overexpressed in E. coli, purified and crystallized. Diffraction data have been collected to 2.0 Å.

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Est25, a ketoprofen-specific hormone-sensitive lipase from a metagenomic library, was crystallized and diffraction data were collected to 1.49 Å resolution.

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The purification, crystallization and preliminary diffraction analysis of the HsdR subunit of the EcoR124I endonuclease are described.

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A recombinant form of DL-2-haloacid dehalogenase from Methylobacterium sp. CPA1 has been expressed in E. coli, purified and crystallized. The crystal belongs to space group P63. Diffraction data have been collected to 1.75 Å resolution.

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Crystallization of DING protein from P. fluorescens is reported. A complete data set was collected to 1.43 Å resolution.

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P30, the transmembrane C-terminal domain of pertactin from B. pertussis has been crystallized after refolding in vitro. Preliminary X-ray crystallographic data are reported.

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In order to gain new insights into the protein structure and its possible interaction with a metal ion or effector ligand, BigR from X. fastidiosa was crystallized in native and selenomethionine (SeMet) labelled forms using the hanging-drop vapour-diffusion method.


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The kinase domain (residues 1–331) of human tau-tubulin kinase 2 was expressed in insect cells, purified and crystallized. Diffraction data have been collected to 2.9 Å resolution.

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A single crystal of zhaoermiatoxin with maximum dimensions of 0.2 × 0.2 × 0.5 mm was used for X-ray diffraction data collection to a resolution of 2.05 Å using synchrotron radiation and the diffraction pattern was indexed in the hexagonal space group P64, with unit-cell parameters a = 72.9, b = 72.9, c = 93.9 Å.

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A putative nondiscriminating aspartyl-tRNA synthetase from the crenarchaeon S. tokodaii strain 7 has been recombinantly expressed, purified and crystallized. The crystal structure has been preliminarily solved at 2.3 Å resolution by the molecular-replacement method.

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The C-terminal bromodomain of human BRD2 was cloned, expressed, purified and crystallized. A complete diffraction data set has been collected to 1.80 Å resolution.

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Crystal structure of a triple mutant (M115L, K121M, T142M) of SeMet-labelled Sec2p, a GEF for Rab GTPase, has been solved by SAD. Control of the selenium sites by mutagenesis much improved the resolution of the SeMet-labelled crystals.

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The isolation and preliminary X-ray analysis of crystals of phage Mu activator protein C bound to promoter DNA are reported.

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The crystallization of the N-terminal transmembrane region-truncated VP26 and VP28 of white spot syndrome virus is described.

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The ligand-binding domain of metabotropic glutamate receptor 7 has been overexpressed, purified, and crystallized by the hanging-drop vapour-diffusion method. A complete data set has been collected to 3.30 Å.

book reviews


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