Open AccessCrystallization and preliminary X‐ray crystallographic analysis of a novel histidinol‐phosphate phosphatase from Thermococcus onnurineus NA1
Author(s) -
Jung Ha Il,
Lee Hyun Sook,
An Young Jun,
Cho Yona,
Lee JungHyun,
Kang Sung Gyun,
Cha SunShin
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109010732
Subject(s) - ton , crystallization , thermococcus , phosphate , bifunctional , crystallography , chemistry , residue (chemistry) , phosphatase , stereochemistry , gene , biochemistry , biology , organic chemistry , catalysis , enzyme , archaea , fishery
The TON_0887 gene product from Thermococcus onnurineus NA1 is a 240‐residue protein that has histidinol‐phosphate phosphatase (HolPase) activity. According to analysis of its primary structure, the TON_0887 gene product is a monofunctional HolPase that belongs to the DDDD superfamily. This contrasts with the generally accepted classification that bifunctional HolPases belong to the DDDD superfamily. The TON_0887 gene product was purified and crystallized at 295 K. A 2.2 Å resolution data set was collected using synchrotron radiation. The TON‐HolPase crystals belonged to space group P 222 1 , with unit‐cell parameters a = 40.88, b = 46.89, c = 148.03 Å. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 48.3%.