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.

Crystallization and preliminary X-ray diffraction analysis of Gos1p, a yeast SNARE protein

Gos1 protein (Golgi SNAP receptor complex member 1) is involved in the SNAREs complexes which are the core machinery driving membrane fusion between cargo-carrying vesicles and their target membranes in the secretory and endocytic pathways in yeast. In this paper, the crystallization method of truncated versions of the Gos1 protein from Saccharomyces cerevisiae is reported and preliminary data on its X-ray analysis are provided.