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The structure of 3-methyladenine DNA glycosylase I in complex with 3-methyladenine is reported.
The catalytic domain of human ADAM-8 was expressed, purified and crystallized in complex with a hydroxamic acid inhibitor, batimastat. The crystal structure of the enzyme–inhibitor complex was refined to 2.1 Å resolution.
The structure of the L166K variant of G protein-coupled receptor kinase 1 has been determined at 2.5 Å resolution in order to determine how a dimer interface observed in prior crystal structures influences the conformation of the enzyme and how the C-terminal amino acids are configured while in a monomeric state.
The structure of the Rem2 G domain bound to GDP is reported in a monoclinic crystal form at 2.66 Å resolution.
The crystal structure of a short-chain dehydrogenase/reductase from B. anthracis strain ‘Ames Ancestor’ is reported.
MatP is a small DNA-binding protein of about 18 kDa. In order to understand the DNA-compaction mechanism of MatP at an atomic level, the structures of apo MatP and of the nucleoprotein complex MatP–matS have been studied.
d-Aspartate oxidase from porcine kidney was crystallized by the sitting-drop vapour-diffusion method. The crystal diffracted to 1.80 Å resolution.
The amino-terminal domain of the Hsp70 co-chaperone Bag2 from M. musculus has been crystallized in native and selenomethionyl forms diffracting to 2.27 and 3.1 Å resolution, respectively.
The haloalkane dehalogenase DatA from A. tumefaciens C58 was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to 1.70 Å resolution.
The ATPase domain of human TAP in nucleotide free, ADP, vanadate and azide complexed forms were purified and crystallized. The X-ray diffraction data sets were collected for all crystals in the resolution range of 2.8–3.0 Å.
The collection of X-ray diffraction data from malate dehydrogenase from P. falciparum to a resolution of 2.2 Å is reported.
The expression, purification and crystallization of the soluble forms of LukE and LukD, which together constitute the LukE–LukD staphylococcal leukotoxin, are described.
Human peptidylarginine deiminase type III was crystallized using polyethylene glycol monomethylether or polyethylene glycol as a precipitant. The crystals belonged to space group R3, with unit-cell parameters a = b = 114.97, c = 332.49 Å (hexagonal axes), and contained two molecules in an asymmetric unit.
P. falciparum GTP:AMP phosphotransferase was expressed in E. coli, purified and crystallized. An X-ray diffraction data set was collected to a resolution of 2.90 Å.
Human histidine decarboxylase was crystallized by the sitting-drop vapour-diffusion method. Diffraction data were collected to 1.8 Å resolution.
Bacterial selenocysteine tRNA was crystallized as the heterologous complex with archaeal seryl-tRNA synthetase. X-ray diffraction was improved by introducing point mutations and heavy-atom labeling, and a 3.2 Å diffraction data set for phase determination was obtained from a platinum-labeled crystal.
The purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of CCM2, which is part of a signalling complex, are reported.
Rv0864, an enzyme of the Moco biosynthesis pathway from M. tuberculosis, has been overexpressed, purified and crystallized. Diffraction data to 2.5 Å were collected and the structure solved by molecular replacement.
Here, the expression, purification, crystallization and preliminary crystallographic analysis of human α1m are reported.
MvfRC87, a 242-residue C-terminal segment of the LysR-type transcriptional regulator MvfR, was produced in Escherichia coli, purified and crystallized.
Recombinant Q9F8T9 protein from Streptomyces rishiriensis (CouO), an S-adenosyl-l-methionine-dependent C-methyltransferase, has been successfully cloned, expressed and purified.
A mutated version of InsP5 2-K allows the production of crystals of the apo form and structure determination using X-ray crystallography.
The cloning, overexpression, purification, crystallization and preliminary X-ray diffraction data are described for UDP-galactopyranose mutase, an enzyme involved in cell-wall synthesis in A. fumigatus.
Cyclophin A like protein from Piriformospora indica involved in salt-stress tolerance was cloned, overexpressed, purified and crystallized. The crystals obtained diffracted X-rays to 2 Å resolution and belonged to space group C2221.
T. maritima CheA P3-P4-P5 domains were crystallized in complex with CheW. Low-resolution diffraction data were collected to ~8 Å using synchrotron X-ray radiation.
Nonstructural protein 2 from avian infectious bronchitis virus has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.8 Å resolution.
The reductase component of p-hydroxyphenylacetate 3-hydroxylase from A. baumannii was overexpressed, purified and crystallized. X-ray diffraction data were collected and processed to 2.3 Å resolution.
Crystals of the complex of E. coli O157 ParE2 and PaaA2 belong to space group P3121 or P3221 and diffract to 3.8 Å resolution.