issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

February 2013 issue

Highlighted illustration

Cover illustration: Structure of an amidohydrolase, SACOL0085, from methicillin-resistant Staphylococcus aureus COL (Girish et al., p. 103).

editorial


Acta Cryst. (2013). F69, 83
doi: 10.1107/S1744309113001486

structural communications


Acta Cryst. (2013). F69, 84-89
doi: 10.1107/S1744309112050270
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The structure of AtALD1 from the flowering plant Arabidopsis thaliana was solved at a resolution of 2.3 Å. The structural analysis supports previous biochemical evidence for differential expression and distinct functions of AtALD1 and AtDAP-AT.

Acta Cryst. (2013). F69, 90-93
doi: 10.1107/S1744309112050750
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The X-ray crystal structure of a camelid VHH domain with a melting temperature of 319.9 ± 1.6 K, which is among the lowest reported for a VHH domain, is reported at 2.1 Å resolution.

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The structure of the FnI-EGF-like tandem domain was solved to 1.6 Å using data sets of native and holmium chloride bound protein. Putative biological roles of this tandem domain are discussed based on the structure.

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The crystal structure of the S. aureus amidohydrolase SACOL0085 reveals that a conserved cysteine residue at the active site serves as a bidentate ligand coordinating two Mn2+ ions.

crystallization communications


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The homotrimeric protein YhbJ from E. coli has been homologously expressed, purified and crystallized in two distinct crystal forms. The crystals diffracted to 3.26 and 3.44 Å resolution.

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β-N-Acetylglucosaminidase from T. maritima has been overexpressed and crystallized. X-ray diffraction data have been collected to 3.80 Å resolution.


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X-ray diffraction data were collected to 2.6 Å resolution from a crystal of the chicken MHC class I molecule BF2*1501. The crystal belonged to space group P3121, with unit-cell parameters a = 125.1, b = 125.1, c = 80.9 Å, and contained two molecules in the asymmetric unit. The Matthews coefficient and solvent content were calculated to be 2.08 Å3 Da−1 and 40.78%, respectively.

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Preliminary crystallographic study of low-oxygen affinity haemoglobin from mongoose; the first structural study of haemoglobin from a member of the Herpestidae family.

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Fructosyl peptide oxidases from Coniochaeta sp. and E. terrenum were crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to 1.8 and 1.6 Å resolution, respectively.


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Major endoglucanase was purified from the extracellular extract of X. campestris pv. campestris and crystals of the catalytic domain were obtained. X-ray diffraction data were collected to 2.7 Å resolution.

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In this work, the crystallization of a self-assembling three-dimensional B-DNA nanostructure is described.

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In this study, the C-terminal regulatory domain of Upc2 from Saccharomyces cerevisiae was purified and crystallized by the vapour-diffusion method.

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The purification and crystallization of UbcA1, a novel ubiquitin-conjugating enzyme identified from the medicinal mushroom A. aegerita, are described.


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The expression, purification, characterization and crystallization of GK2848, a carbonic anhydrase from G. kaustophilus, are described. The crystals diffracted to a resolution of 2.70 Å.

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Novel hepatitis B virus-like particles of recombinant dimeric core–GFP fusion protein were expressed, purified and crystallized. The crystals diffracted to 2.15 Å resolution and belonged to space group F432, with unit-cell parameters a = b = c = 219.7 Å.

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The BinB subunit of mosquito-larvicidal binary toxin from B. sphaericus has been crystallized. The crystal could diffract to a resolution of 1.75 Å and belongs to space group P6222.

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Backtracked bacterial RNA polymerase (RNAP) complexes were reconstituted by assembling Thermus thermophilus RNAP with nucleic acid scaffolds. The complexes were crystallized, and their X-ray diffraction data were collected and analyzed.

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This paper reports the successful purification, crystallization and preliminary structure solution of the transfer protein TraM from the Gram-positive conjugative plasmid pIP501.

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ADH2, an NAD(P)-dependent butanol dehydrogenase A, is part of the terminal oxidation pathway in the long-chain alkane-degrading G. thermodenitrificans NG80-2. The expression, purification, crystallization and preliminary crystallographic analysis of ADH2 are reported.

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The expression, purification, crystallization and diffraction of the acyl-CoA thioesterase TesB from Y. pestis are reported. X-ray crystallographic diffraction data to 2.0 Å resolution were collected at the Australian Synchrotron.

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The C-terminal carbohydrate-binding module (CBM65B) of family 5 glycoside hydrolase endoglucanase 5A (Cel5A) of E. cellulosolvens has been co-crystallized with cellohexaose and xyloglucan heptasaccharide and various data collected to 1.42–3.5 Å resolution.

laboratory communications


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A software script is presented for facilitating the analysis and visual inspection of ligand molecules in the context of the electron-density maps calculated from experimental data associated with protein structures determined by X-ray crystallography.

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The use of UV imaging as a means of locating protein crystals is a fairly new tool, however not suitable for all protein crystallization trials. Practical examples of the strengths and some of the pitfalls of the technology are presented.

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The Thermofluor assay constitutes a quick and easy-to-perform high-throughput method with which it is possible to identify protein-stabilizing buffer compositions or small-molecule additives.
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