title: Crystallization and preliminary X-ray diffraction analysis of a novel type of phosphoserine phosphatase from Hydrogenobacter thermophilus TK-6.
abstract: Two novel-type phosphoserine phosphatases (PSPs) with unique substrate specificity from the thermophilic and hydrogen-oxidizing bacterium Hydrogenobacter thermophilus TK-6 have previously been identified. Here, one of the PSPs (iPSP1) was heterologously expressed in Escherichia coli, purified and crystallized. Diffraction-quality crystals were obtained by the sitting-drop vapour-diffusion method using PEG 4000 as the precipitant. Two diffraction data sets with resolution ranges of 45.0-2.50 and 45.0-1.50 Å were collected from a single crystal and were merged to give a highly complete data set. The space group of the crystal was identified as primitive orthorhombic P2(1)2(1)2(1), with unit-cell parameters a = 49.8, b = 73.6, c = 124.3 Å. The calculated Matthews coefficient (V(M) = 2.32 Å(3) Da(-1)) indicated that the crystal contained one iPSP1 complex per asymmetric unit.
authors.affiliation: Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
authors.forename: Yoko
authors.initials: Y
authors.lastname: Chiba
authors.forename: Shoichiro
authors.initials: S
authors.lastname: Horita
authors.forename: Jun
authors.initials: J
authors.lastname: Ohtsuka
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Arai
authors.forename: Koji
authors.initials: K
authors.lastname: Nagata
authors.forename: Yasuo
authors.initials: Y
authors.lastname: Igarashi
authors.forename: Masaru
authors.initials: M
authors.lastname: Tanokura
authors.forename: Masaharu
authors.initials: M
authors.lastname: Ishii
mesh_terms: D001419:Bacteria / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry*
chemical_list: D010744:Phosphoric Monoester Hydrolases; C022394:phosphoserine phosphatase