The crystal structure of the bacterial protein LpxD from P. aeruginosa was solved and refined at 1.3 Å resolution. The overall domain architecture and biological assembly are similar to those found in previously solved structures of LpxD from other species.
Cwp19 is a putatively surface-located protein from Clostridium difficile. A recombinant N-terminal protein (residues 27–401) lacking the signal peptide and the C-terminal cell-wall-binding repeats (PFam04122) was crystallized using the sitting-drop vapour-diffusion method and diffracted to 2 Å resolution.
A novel ferredoxin/thioredoxin reductase-like protein from M. acetivorans was heterologously expressed in E. coli, purified and then subjected to crystallization. Preliminary X-ray diffraction studies revealed that the crystal belonged to a primitive cubic space group, with unit-cell parameters a = b = c = 92.72 Å.
The α-mannosidase I inhibitor kifunensine inhibited N-glycan processing in long-term cultures of Chinese hamster ovary cells, allowing deglycosylation and crystallization of the homodimeric extracellular region of the inhibitory glycoprotein receptor CTLA-4 (CD152).
Recombinant GK1506 from the thermophilic bacterium Geobacillus kaustophilus has been expressed, purified and crystallized. A 2.6 Å resolution native data set was collected from a single flash-cooled crystal.
The substrate binding protein (SP_0149) of an ABC transporter from Streptococcus pneumoniae was molecularly cloned, overexpressed and purified. Diffraction quality crystals were grown using the hanging-drop vapour-diffusion technique.
The putative sensor histidine kinase domain of the cytoplasmic protein HksP4 from the hyperthermophilic bacterium A. aeolicus VF5 was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. Crystals were obtained in the presence of ATP and AMPPNP; they were found to belong to the same space group P212121 and diffracted X-rays to 3.1 and 2.9 Å resolution, respectively.
MsDpo4 from M. smegmatis, a member of the Y-family of DNA polymerases, was expressed and purified to homogeneity. Crystals of native MsDpo4 in the apo state were obtained and X-ray diffraction data were collected to a maximum resolution of 2.6 Å.
The 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (IspE) from M. tuberculosis H37Rv was overexpressed in E. coli, purified and crystallized. Diffraction data for the native enzyme were collected to 2.1 Å resolution.