issue contents
February 2013 issue
Cover illustration: Structure of an amidohydrolase, SACOL0085, from methicillin-resistant Staphylococcus aureus COL (Girish et al., p. 103).
editorial
Free
structural communications
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.
PDB reference: AtALD1, 4fl0
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.
PDB reference: llama VHH domain, 4idl
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.
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.
PDB reference: S. aureus amidohydrolase SACOL0085, 4ewt
crystallization communications
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.
β-N-Acetylglucosaminidase from T. maritima has been overexpressed and crystallized. X-ray diffraction data have been collected to 3.80 Å resolution.
Thymidylate kinase from T. thermophilus HB8 has been cloned, expressed, purified and crystallized.
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.
Preliminary crystallographic study of low-oxygen affinity haemoglobin from mongoose; the first structural study of haemoglobin from a member of the Herpestidae family.
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.
An NAD(P)+-dependent L-serine 3-dehydrogenase from a hyperthermophilic archaeon was successfully isolated and crystallized.
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.
In this work, the crystallization of a self-assembling three-dimensional B-DNA nanostructure is described.
In this study, the C-terminal regulatory domain of Upc2 from Saccharomyces cerevisiae was purified and crystallized by the vapour-diffusion method.
The purification and crystallization of UbcA1, a novel ubiquitin-conjugating enzyme identified from the medicinal mushroom A. aegerita, are described.
AHP2 from A. thaliana was cloned, expressed, purified and crystallized.
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.
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.
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.
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.
Open access
This paper reports the successful purification, crystallization and preliminary structure solution of the transfer protein TraM from the Gram-positive conjugative plasmid pIP501.
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.
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.
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
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.
Open access
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.
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.