Open AccessCrystallization and preliminary X‐ray diffraction analysis of a novel type of phosphoserine phosphatase from Hydrogenobacter thermophilus TK‐6
Author(s) -
Chiba Yoko,
Horita Shoichiro,
Ohtsuka Jun,
Arai Hiroyuki,
Nagata Koji,
Igarashi Yasuo,
Tanokura Masaru,
Ishii Masaharu
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112025213
Subject(s) - crystallization , phosphoserine , crystallography , materials science , chemistry , biochemistry , serine , enzyme , organic chemistry
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 P 2 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.