issue contents

ISSN: 2053-230X

January 2013 issue

Highlighted illustration

Cover illustration: A selection of crystals from articles published in 2012.


Acta Cryst. (2013). F69, 1
doi: 10.1107/S1744309112051950

structural communications

Acta Cryst. (2013). F69, 2-5
doi: 10.1107/S1744309112047422
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The structure of the near germline antibody S25-2 in complex with an unnatural Kdo disaccharide highlights the remarkable plasticity in antigen recognition of germline antibodies.

Acta Cryst. (2013). F69, 6-9
doi: 10.1107/S1744309112048890
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Crystal structures of the protein LpxD from A. baumannii were solved in apo forms that are suitable for structure-based antibacterial drug discovery.

Acta Cryst. (2013). F69, 10-14
doi: 10.1107/S1744309112047549
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The crystallization and structure determination to 2.2 Å resolution is reported for a ribulose 1,5-bisphosphate-bound non-activated form of garden pea ribulose-1,5-bisphosphate carboxylase/oxygenase.

Acta Cryst. (2013). F69, 15-19
doi: 10.1107/S1744309112047276
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Alanine racemase from O. oeni exists as a dimer in the crystal structure. Both monomers contribute to the two active sites present, one for each monomer.

Acta Cryst. (2013). F69, 20-24
doi: 10.1107/S1744309112047562
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Europium(III) ions bound to the surface of hen egg-white lysozyme were found to exhibit good anomalous signal facilitating SAD phasing using laboratory-source data and automated model building. The europium ion-binding sites were observed up to the 15σ level.

Acta Cryst. (2013). F69, 25-34
doi: 10.1107/S1744309112044739
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A focused strategy has been directed towards the structural characterization of selected proteins from the bacterial pathogen P. aeruginosa. The objective is to exploit the resulting structural data, in combination with ligand-binding studies, and to assess the potential of these proteins for early-stage antimicrobial drug discovery.

crystallization communications

Acta Cryst. (2013). F69, 35-38
doi: 10.1107/S1744309112049184

Acta Cryst. (2013). F69, 39-41
doi: 10.1107/S1744309112045484

Acta Cryst. (2013). F69, 42-44
doi: 10.1107/S1744309112048506
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The crystallization and preliminary X-ray crystallographic analysis of diaminopimelate epimerase from A. baumannii are reported.

Acta Cryst. (2013). F69, 45-48
doi: 10.1107/S1744309112048002
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A mutant human MTH1 protein [hMTH1(G2K)] with a homogeneous N-terminus produced high-quality crystals which diffracted to near 1.1 Å resolution using synchrotron radiation.

Acta Cryst. (2013). F69, 49-52
doi: 10.1107/S1744309112047124
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The expression, purification, crystallization and preliminary crystallographic characterization of the extracellular serine protease Esp from S. epidermidis are reported.

Acta Cryst. (2013). F69, 53-56
doi: 10.1107/S1744309112048257
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The preliminary crystallographic analysis of Megavirus chilensis Mg561, which has a predicted polyadenylate synthase function, is reported. The crystals belonged to space group P212121, with two monomers per asymmetric unit.

Acta Cryst. (2013). F69, 57-60
doi: 10.1107/S1744309112049032
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Crystals of the phosphotriesterase from M. tuberculosis were obtained and diffraction data were collected and processed to 2.27 Å resolution. An analytical ultracentrifugation experiment suggested that mPHP exists as dimers in solution.

Acta Cryst. (2013). F69, 61-64
doi: 10.1107/S174430911204804X
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D. melanogaster Gαo-subunit and the RGS domain of its interacting partner CG5036 have been overproduced and purified; the crystallization and preliminary X-ray crystallographic analysis of the complex of the two proteins are reported.

Acta Cryst. (2013). F69, 65-68
doi: 10.1107/S1744309112045095
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The UDP-glucuronic acid:flavonol-3-O-glucuronosyltransferase (VvGT5) from the grapevine V. vinifera was purified and crystallized. The best crystal diffracted X-rays to 2.2 Å resolution and belonged to space group P6122.

Acta Cryst. (2013). F69, 69-72
doi: 10.1107/S1744309112048774
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Crystals of Deg8, an ATP-independent serine endopeptidase from A. thaliana, were monoclinic, belonging to space group C2 with unit-cell parameters a = 129.5, b = 124.2, c = 93.3 Å, β = 132.4°, and diffracted to 2.0 Å resolution.

Acta Cryst. (2013). F69, 73-76
doi: 10.1107/S174430911205049X
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An organophosphorus hydrolase from P. pseudoalcaligenes named OPHC2 has been crystallized. Combined with biochemical characterization, it is expected that the structure of this protein will provide insight into the catalytic mechanism of organophosphorus hydrolysis and will highlight the role of key residues involved in substrate specificity.

Acta Cryst. (2013). F69, 77-79
doi: 10.1107/S1744309112049330
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A bacteria biofilm formation involved enzyme, BsYisP, from Bacillus subtilis subsp. subtilis strain 168, was crystallized and diffracted to 1.92 Å.

Acta Cryst. (2013). F69, 80-82
doi: 10.1107/S1744309112049408
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The hypothetical protein MJ0927 of the Nif3 family has been crystallized and X-ray diffraction data have been collected to a resolution of 2.47 Å.
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