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The crystal structure of cytochrome c 6 from the brown alga H. fusiformis has been determined at 1.6 Å resolution. The amino-acid sequence and tertiary structure of H. fusiformis cytochrome c 6 were very similar to those of red algal cytochrome c 6 rather than those of green algal cytochrome c 6.
A combination of spectroscopic and crystallographic data have been used to identify the native metal-ion preference of GpdQ. These data suggest that GpdQ is a homobinuclear non-haem iron enzyme.
A crystal structure of zebrafish Plk1 reveals the binding of an extended ATP-competitive inhibitor that targets the adaptive pocket and helps to order the activation segment of the kinase. The conformation of the segment resembles that observed in a nonphosphorylated ligand-free wild-type kinase domain.
The gene-regulation factor PyrR from B. halodurans has been crystallized in two crystal forms. Preliminary crystallographic analysis showed that the protein forms tetramers in both space groups.
l-Methionine γ-lyase 1, a key enzyme in sulfur-containing amino-acid degradation, from the protozoan parasite E. histolytica was crystallized in a form suitable for X-ray structure analysis.
The structure of the decameric inducible lysine decarboxylase from E. coli was determined by SIRAS using a hexatantalum dodecabromide (Ta6Br12 2+) derivative. Model building and refinement are under way.
Crystallization of the cystine-knot protein Spätzle occurred following serendipitous limited degradation of the pro-Spätzle propeptide during the crystallization experiment.
Crystals of the soluble ternary GM-CSF receptor complex were obtained which diffracted to a resolution of 3.3 Å.
The N-terminal moiety of C. thermocellum endo-1,4-β-d-xylanase 10B, comprising a carbohydrate-binding module (CBM22-1) and a GH10 E337A mutant domain, has been crystallized in complex with xylohexaose. The crystals belong to the trigonal space group P3221, contain a dimer in the asymmetric unit and diffract to beyond 2.0 Å resolution.
This article describes the first successful crystallization of a membrane-bound [NiFe] hydrogenase isolated from a photosynthetic organism (A. vinosum). The crystals obtained produced diffraction patterns up to 2.5 Å resolution.
Glyceraldehyde-3-phosphate dehydrogenase A has been cloned, expressed and purified. Apoprotein crystals have been grown which diffracted to 1.75 Å resolution and belonged to space group P21; holo crystals were grown in the presence of NADP, diffracted to 2.6 Å resolution and belonged to space group P32.
Glyceraldehyde-3-phosphate dehydrogenase B from H. pylori has been cloned, expressed, purified and crystallized in the presence of NAD. Crystals of GAPDHB diffracted to 2.8 Å resolution and belonged to space group P6522, with unit-cell parameters a = b = 166.1, c = 253.1 Å.
Preliminary X-ray data collection and analysis for crystals of chlorite dismutase, a haem-based enzyme that very effectively reduces chlorite to chloride while producing molecular oxygen, is reported to 2.1 Å resolution.
A 2S albumin from L. culinaris was purified and crystallized and preliminary crystallographic studies were carried out.
Maleylacetate reductase from Rhizobium sp. strain MTP-10005 has been crystallized using the sitting-drop vapour-diffusion method and microseeding. The crystals contained one dimeric molecule per asymmetric unit and diffracted to 1.79 Å resolution.
l-Asparaginase from H. pylori was overexpressed in E. coli, purified and crystallized. The crystals belonged to space group I222, with unit-cell parameters a = 63.6, b = 94.9, c = 100.2 Å and one molecule in the asymmetric unit. A complete data set to 1.6 Å resolution was collected using synchrotron radiation.
tRNA (m7G46) methyltransferase from E. coli was overexpressed, purified and crystallized. Diffraction data were collected to 2.04 Å resolution.
The ribonuclease HI domain of a bifunctional protein Rv2228c-CobC from M. tuberculosis has been crystallized as a fusion protein with maltose-binding protein in a form suitable for high-resolution crystallographic analysis.
XometC, a cystathionine γ-lyase-like protein from X. oryzae pv. oryzae and an antibacterial drug-target protein against bacterial blight, was cloned, purified and crystallized. Preliminary X-ray crystallographic analysis of XometC crystals was carried out.
The crystal of a 1,3-1,4-β-glucanase produced by Paecilomyces thermophila belongs to the hexagonal space group P6322, with unit-cell parameters a = b = 154.54, c = 87.62 Å.
Crystallization of recombinant IgG-binding protein expressed in Escherichia coli using the hanging-drop vapour-diffusion method is described. The crystals belonged to space group P212121, with unit-cell parameters a = 38.98, b = 43.94, c = 78.17 Å.
The enzyme mannosyl-3-phosphoglycerate synthase from R. xylanophilus has been expressed, purified and crystallized. The crystals belong to the hexagonal space group P6522 and diffract to 2.2 Å resolution.
The full-length LysR transcriptional regulator TsaR from C. testosteroni T-2 has been crystallized in two crystal forms and several native and derivative data sets have been collected using synchrotron and in-house X-ray sources.
A corrigendum to the paper by Lafaye et al. [Acta Cryst. (2008). F64, 111–114].
A corrigendum to the article by Ito et al. [Acta Cryst. (2008). F64, 531–532].