issue contents
June 2018 issue
research communications
Carbonic anhydrase II microcrystals suitable for XFEL data collection diffracted to 1.7 Å resolution and were indexed in space group P21, with unit-cell parameters a = 42.2, b = 41.2, c = 72.0 Å, β = 104.2°.
Open access
The crystal structure of an inactive variant of the the quorum-sensing master transcription regulator HapR from Vibrio cholerae suggests that its inactivity is owing to steric clashes and charge repulsion with the phosphate backbone of DNA.
PDB reference: HapR, G39D mutant, 5l0x
The human molybdenum cofactor-dependent enzyme mARC was crystallized as a fusion protein containing an internal T4 lysozyme (T4L) moiety. The T4L fusion-protein approach is not limited to the crystallization and structure determination of GPCRs, but can also be rationally applied to soluble proteins.
A detailed analysis is presented of suspected merohedral twinning with an unusual behaviour of twin-law-independent twin indicators in crystals of the putative flavin-dependent halogenase HalX from Xanthomonas campestris.
Crystals of the GehC protein from Staphylococcus epidermidis that diffracted X-rays to a resolution of at least 1.9 Å are described.
The three-dimensional structure of Escherichia coli purine nucleoside phosphorylase in complex with the noncompetitive inhibitor 7-deazahypoxanthine has been solved. The orientation of the 7-deazahypoxanthine molecule was found to be rotated by 180° relative to bases found in other purine nucleoside phosphorylase structures.
PicW2 from Picea wilsonii: preparation, purification, crystallization and X-ray diffraction analysis
PicW2 is a dehydrin protein and its expression is associated with hardiness to cold. To understand the mechanism for the tolerance of low temperature, prokaryotically expressed PicW2 was purified using chitosan-affinity chromatography and gel filtration, crystallized using the vapour-diffusion method and crystallographic information was obtained by X-ray diffraction.
The psychrophilic esterase PsEst3 was successfully overexpressed using a psychrophilic chaperonin co-expression system, and was cystallized using the vapour-diffusion method. The X-ray diffraction data were collected to 2.1 Å resolution.
Structures of Borrelia burgdorferi nucleoside diphosphate kinase have been solved both in the native state and bound to ADP and vanadate to characterize its catalytic action. Visualization strategies and models demonstrate dynamic relationships of the enzyme and ligands, and help to define phosphate transfer by the enzyme. This reaction is important for infection within a mouse model and is a potential target for the development of therapeutics for Lyme disease.