crystallization communications
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.
IYCr crystallization series
Recombinant XynAS9, a thermophilic GH10 xylanase from Streptomyces sp. S9, was crystallized and X-ray diffraction data were collected to 2.08 Å resolution.