issue contents
January 2013 issue
Cover illustration: A selection of crystals from articles published in 2012.
editorial
Free
structural communications
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.
PDB reference: S25-2 in complex with a 5,6-dehydro-Kdo disaccharide, 4hgw
Crystal structures of the protein LpxD from A. baumannii were solved in apo forms that are suitable for structure-based antibacterial drug discovery.
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.
PDB reference: Rubisco, 4hhh
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.
PDB reference: alanine racemase, 3co8
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.
PDB reference: lysozyme, europium derivative, 4h1p
Open access
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
The cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the ectodomain of BVDV E2 are described.
The VLR2913 ectodomain fused with internalin B was crystallized and diffraction data were collected to a maximum resolution of 2.04 Å.
The crystallization and preliminary X-ray crystallographic analysis of diaminopimelate epimerase from A. baumannii are reported.
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.
The expression, purification, crystallization and preliminary crystallographic characterization of the extracellular serine protease Esp from S. epidermidis are reported.
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.
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.
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.
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.
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.
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.
A bacteria biofilm formation involved enzyme, BsYisP, from Bacillus subtilis subsp. subtilis strain 168, was crystallized and diffracted to 1.92 Å.
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.