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.

Purification, crystallization and preliminary crystallographic analysis of a ribosome-recycling factor from Thermoanaerobacter tengcongensis (TteRRF)

A reductive methylation-modified RRF from Thermoanaerobacter tengcongensis (TteRRF) has been crystallized using the vapour-diffusion method. The crystal belonged to space group P6₁22/P6₅22 with unit-cell parameters a = b = 103.26, c = 89.17 Å.