issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

December 2014 issue

Highlighted illustration

Cover illustration: Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor (Thompson et al., p. 1584).

editorial


Acta Cryst. (2014). F70, 1575
doi: 10.1107/S2053230X14024789

IYCr crystallization series


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In the last three decades, membrane-protein crystallization has changed from overwhelmingly difficult to nearly routine. This review offers a snapshot of the current state of the art, focusing particularly on the role of detergents in this process.

structural communications


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The Eut microcompartment is a protein-based organelle that carries out B12-dependent degradation of ethanolamine in diverse bacteria. This work characterizes a binding interaction between cobalamin (B12) and the inward-facing surface of EutL, a shell protein proposed to be involved in cofactor transport in the Eut microcompartment.

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A strategy for the purification of forced POZ-domain heterodimers is described, and crystal structures of the heterodimeric POZ domains of Miz1/BCL6 and Miz1/NAC1 are reported.

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The highly conserved domain of unknown function in the cyanobactin superfamily has a novel fold. The protein does not appear to bind the most plausible substrates, leaving questions as to its role.

crystallization communications


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Here, the expression, purification and crystallization of the phosphate-binding protein PhoX from Xanthomonas axonopodis pv. citri and X-ray data collection at 3.0 Å resolution are described.

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This article describes the preliminary crystallographic data for a complex consisting of Porcine epidemic diarrhea virus main protease and its inhibitor N3.

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This article describes the preliminary crystallographic data of a complex of Feline infectious peritonitis virus main protease with its inhibitor N3.

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Biosynthetic alanine racemase from P. aeruginosa PAO1 was expressed in E. coli and purified. The purified enzyme was crystallized and preliminary X-ray crystallographic analysis was performed.

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This article describes the preliminary crystallographic data of a functional mutant (N60K) of nonstructural protein 9 from Human coronavirus HKU1.

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The central SLR (Sel1-like repeat) domain of mouse SEL1L was cloned, expressed, purified and crystallized. X-ray diffraction data were collected to 3.3 Å resolution.

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The full-length B. halodurans trimodular endo-β-1,4-glucanase has been crystallized and data were processed to 1.64 Å resolution in the orthorhombic space group P21212. A molecular-replacement solution has been found.

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Recombinant expression and nanobody-aided crystallization of a soluble BabA truncation (BabA25–460) corresponding to the predicted adhesin domain are reported.

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The tetradomain bacteriophytochrome protein XccBphP from Xanthomonas campestris pv. campestris was overexpressed, purified and crystallized in complex with its cofactor biliverdin. A complete data set was collected to 3.25 Å resolution from a crystal belonging to space group P43212 at the SOLEIL synchrotron.

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To contribute to the molecular understanding of the function of a tandem-type universal stress protein, UspE from E. coli was overexpressed and crystals of the recombinant protein were obtained using sitting-drop vapour diffusion. A diffraction data set was collected to a resolution of 3.2 Å.

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The expression, purification, crystallization and preliminary X-ray diffraction analysis of KstR2, a TetR-family transcriptional regulator of cholesterol metabolism from M. tuberculosis, is described.

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The overproduction, purification, crystallization and preliminary X-ray analysis of wild-type Hikeshi and its Phe97Ala mutant are described.

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The core domain of the eukaryotic ribosome assembly factor complex Rpf2–Rrs1 from A. nidulans was crystallized.

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A novel carbohydrate-binding module from an R. flavefaciens glycoside hydrolase family 5 modular enzyme was purified and crystallized and data were collected from crystals of the native protein and a selenomethionine derivative to 2.0 and 2.28 Å resolution, respectively.


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A feruloyl esterase from T. cellulolyticus containing a carbohydrate-binding module was prepared, purified and crystallized. The crystal diffracted to 2.60 Å resolution using synchrotron radiation.

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Acetylxylan esterase from T. cellulolyticus expressed as a truncated form without the cellulose-binding module 1 domain was purified and crystallized. The crystal diffracted to 1.50 Å resolution using synchrotron radiation.

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The dual-domain β-propeller phytases (PhyHT) from Bacillus sp. HJB17, which had the secreted signal peptide of the first 40 amino acids deleted and had a typical BPP domain (PhyH-DII; residues 319–644) at the C-terminus and an incomplete N-terminal BPP domain (PhyH-DI; residues 41–318) that was found to act synergistically (with a 1.2–2.5-fold increase in phosphate release) with PhyH-DII, other BPPs (PhyP and 168PhyA) and a histidine acid phosphatase, was prepared, purified, crystallized and preliminary crystallographic analysis was undertaken. The structure of PhyHT will be therefore studied with the aim of explaining these functions.

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A GH52 β-D-xylosidase from G. stearothermophilus T6 (Xyn52B2) has been crystallized in a new orthorhombic P212121 crystal form. Full X-ray diffraction data sets were measured for the wild-type enzyme (3.70 Å resolution), the E335G catalytic mutant (2.95 Å resolution), a potential Hg derivative (2.15 Å resolution) and a selenomethionine derivative (3.90 Å resolution) for use in a detailed three-dimensional structural analysis of the Xyn52B2 protein.

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Crystals of the N-M domain of human Trap1 in complex with ATPase inhibitors (PU-H71 and BIIB-021) were obtained and diffraction data were collected to 2.7 Å (Trap1–PU-H71) and 3.1 Å (Trap1–BIIB-021) resolution.

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Two endonuclease III enzymes from the extreme radiation-resistant and desiccation-resistant bacterium D. radiodurans have been expressed, purified and crystallized. Diffraction data have been collected to resolutions of 2.15 Å (EndoIII-1) and 1.31 Å (EndoIII-3).

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The tyrosine phosphatase AmsI from E. amylovora was cloned, overexpressed in E. coli, purified and crystallized. X-ray diffraction data were collected to a resolution of 1.57 Å.

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Recombinant BPSL1038 from B. pseudomallei was overexpressed, purified to homogeneity and crystallized in a form suitable for X-ray analysis.

laboratory communications


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A combination of size-exclusion chromatography, Thermofluor assay and dynamic light scattering was used to find conditions optimal for the stability and oligomeric homogeneity of a single-chain variable antibody fragment, which resulted in significantly improved protein crystallizability.

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This article describes the use of evaporation control lids that are fitted to crystallization plates to improve the reproducibility of trials using as little as 5 nl. The plate lids contain apertures which are large enough for the transfer of protein containing droplets, but small enough to greatly reduce the rate of evaporation during the time needed to prepare the plate.
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