Open AccessCrystallization and preliminary X‐ray studies of TON_1713 from Thermococcus onnurineus NA1, a putative member of the haloacid dehalogenase superfamily
Author(s) -
Le Binh Van,
Lee Hyun Sook,
Cho Yona,
Kang Sung Gyun,
Kim Dong Young,
Kim YangGyun,
Kim Kyeong Kyu
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107054747
Subject(s) - superfamily , thermococcus , crystallography , crystallization , dehalogenase , escherichia coli , enzyme , chemistry , biochemistry , biology , stereochemistry , archaea , organic chemistry , gene
The haloacid dehalogenase (HAD) protein superfamily is one of the largest enzyme families and shows hydrolytic activity towards diverse substrates. Structural analyses of enzymes belonging to the HAD family are required to elucidate the molecular basis underlying their broad substrate specificity and reaction mechanism. For this purpose, TON_1713, a hypothetical protein from Thermococcus onnurineus that is a member of the HAD superfamily, was expressed in Escherichia coli , purified and crystallized at 295 K using 1.6 M magnesium sulfate as a precipitant. X‐ray diffraction data were collected to 1.8 Å resolution using a synchrotron‐radiation source. The crystals belong to the triclinic space group P 1, with unit‐cell parameters a = 52.5, b = 65.8, c = 203.4 Å, α = 71.1, β = 79.9, γ = 74.3°.