issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

August 2013 issue

Highlighted illustration

Cover illustration: RBcel1, a metagenome-derived psychrotolerant family GH5 endoglucanase (Delsaute et al., p. 828).

editorial


Acta Cryst. (2013). F69, 827
doi: 10.1107/S1744309113020873

structural communications


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The crystal structure of the psychrotolerant endoclucanase RBcel1, an enzyme implicated in bacterial cellulose synthesis, has been determined to 1.4 Å resolution.

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The crystal structure of DusC from E. coli was determined at 2.1 Å resolution.

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The crystal structure of Na-GST-3 from the human hookworm parasite N. americanus is reported.

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The crystal structure of 1,5-anhydro-D-fructose reductase from S. meliloti has been determined to 1.93 Å resolution. It is compared with that of 1,5-anhydro-D-fructose reductase from S. morelense and the significance of the observed open conformation of the active site is discussed.

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Endo-β-1,4-galactanase from E. nidulans crystallized in the presence of 0.2 M zinc acetate contains 15 zinc ions.

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The crystal structure of the first zebrafish caspase-recruitment domain at 1.47 Å resolution illustrates a six-helix bundle fold similar to that of the human NLRP1 CARD.

crystallization communications


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The preliminary crystallographic analysis of neuraminidase N2 from influenza virus A/Myanmar/M187/2007 is reported. The crystals belonged to space group P212121, with four monomers per asymmetric unit.

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Selenophosphate synthetases from L. major and T. brucei were crystallized for the first time using limited proteolysis and microbatch techniques and suitable crystals for X-ray diffraction experiments were obtained.

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The staphylococcal α-haemolysin H35A mutant has been cloned, expressed and crystallized. The crystals belonged to space group P61, with unit-cell parameters a = b = 151.3, c = 145.0 Å.

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P. cuspidatum bifunctional chalcone synthase/benzalacetone synthase was crystallized in the presence of the product and diffraction data were collected to 2.0 Å resolution.

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The putative small terminase protein from the thermostable bacteriophage G20C has been produced, purified and crystallized.

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Cyanuric acid hydrolase has been crystallized with the bound inhibitor barbituric acid and diffraction data were collected to 2.7 Å resolution.

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Spermidine acetyltransferase (SAT) from E. coli catalyses the transfer of acetyl groups from acetyl-CoA to spermidine. SAT was crystallized and the crystals contained four molecules in the asymmetric unit.

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Nitroalkane oxidase from P. aeruginosa was purified and crystallized. A complete data set was collected to 1.9 Å resolution.

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Two crystal forms of β-carbonic anhydrase psCA3 from P. aeruginosa were grown. Crystal form A belonged to space group P212121, with unit-cell parameters a = 81.9, b = 84.9, c = 124.2 Å, and diffracted X-rays to 2.9 Å resolution; crystal form B belonged to space group P21212, with unit-cell parameters a = 69.9, b = 77.7, c = 88.5 Å, and diffracted X-rays to 3.0 Å resolution.

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The bacterial cell-division protein FtsA from methicillin-resistant S. aureus was crystallized and X-ray diffraction data were collected to a resolution of 2.3 Å.

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The α subdomain of Lon protease from B. thermoruber WR-249 has been expressed, purified and crystallized. Preliminary X-ray diffraction experiments have been undertaken.

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The crystallization and preliminary X-ray crystallographic analysis of the MxaJ protein of the mox operon from the marine bacterium M. aminisulfidivorans MPT is reported.

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The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 2.5.1.61) catalyses a key early step in the biosynthesis of tetrapyrroles in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole. PBGD from B. megaterium was expressed and the enzyme was crystallized in a form which diffracts synchrotron radiation to high resolution.


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The cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of a novel AB5 toxin EcxAB are described.

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The human TRAF4 TRAF domain was crystallized. The crystals were found to belong to the hexagonal space group P32, with unit-cell parameters a = b = 147.17, c = 202.69 Å. The crystals were obtained at 293 K and diffracted to a resolution of 4.2 Å.

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A putative lipase (CpsLip) from C. psychrerythraea strain 34H was expressed, purified and characterized. Crystallization and preliminary X-ray crystallographic analysis of CpsLip were performed.

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The pac gene encoding penicillin G acylase from K. citrophila was cloned and a slow-processing site-directed mutant was prepared, expressed, purified and crystallized. Triclinic and monoclinic crystal forms were obtained which diffracted to 2.5 and 3.5 Å resolution, respectively.

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Crystals of the β-pore-forming toxin monalysin from the Drosophila pathogen P. entomophila grown from PEG solutions were monoclinic (space group C2) and diffracted to 2.85 Å resolution.

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An alanine dehydrogenase from B. megaterium WSH-002 was expressed in E. coli and purified. Crystallization and preliminary X-ray crystallographic analysis of the recombinant enzyme were performed.

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Soybean mature glycinin was purified and crystallized and its preliminary crystallographic analysis is also reported.

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Hepatitis B virus-like particles consisting of core protein dimers fused to EGFP were expressed, purified and crystallized. The crystals diffracted to 2.8 Å resolution.

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B. circulans T-3040 cycloisomaltooligosaccharide glucanotransferase was overexpressed in E. coli in two forms and crystallized by the sitting-drop vapour-diffusion method.
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