Crystallization and preliminary X-ray study of TsiV3 from Vibrio cholerae

Immunity protein TsiV3 from Vibrio cholera has been expressed, purified and crystallized. The crystal belonged to space group P2₁2₁2₁, with unit-cell parameters a = 73.3, b = 78.12, c = 106.18 Å and diffract to 2.55 Å resolution.

Crystallization and preliminary crystallographic studies of the complement 1qA globular domain from zebrafish, Dare-C1qAgD

The crystal structure of zebrafish (D. rerio) complement 1qA globular domain (Dare-C1qAgD) was determined from X-ray diffraction data collected to 2.05 Å resolution. The crystal belonged to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 50.347, b = 85.059, c = 95.560 Å.

Crystallization and preliminary X-ray diffraction analysis of a single variable domain of the immunoglobulin superfamily in amphioxus, Amphi-IgSF-V

X-ray diffraction data for Amphi-IgSF-V (a single variable domain of the immunoglobulin superfamily from amphioxus) were collected to 1.95 Å resolution. The crystal belonged to space group P3₂21, with unit-cell parameters a = b = 53.9, c = 135.5 Å, and contained two molecules in the asymmetric unit. The Matthews coefficient and solvent content were calculated to be 2.58 Å³ Da^-1 and 52.38%, respectively.

Complex assembly, crystallization and preliminary X-ray crystallographic analysis of the chicken CD8αα–BF2*0401 complex

A crystal of the chicken MHC class I molecule BF2*0401 in complex with chicken CD8αα (CD8αα–BF2*0401) diffracted to 2.8 Å resolution and belonged to space group P2₁, with unit-cell parameters a = 90.6, b = 90.8, c = 94.9 Å, β = 98°.

Preparation, purification, crystallization and preliminary crystallographic analysis of dual-domain β-propeller phytase from Bacillus sp. HJB17

The dual-domain β-propeller phytases (PhyHT) from Bacillus sp. HJB17, which had the secreted signal peptide of the first 40 amino acids deleted and had a typical BPP domain (PhyH-DII; residues 319–644) at the C-terminus and an incomplete N-terminal BPP domain (PhyH-DI; residues 41–318) that was found to act synergistically (with a 1.2–2.5-fold increase in phosphate release) with PhyH-DII, other BPPs (PhyP and 168PhyA) and a histidine acid phosphatase, was prepared, purified, crystallized and preliminary crystallographic analysis was undertaken. The structure of PhyHT will be therefore studied with the aim of explaining these functions.