title: Crystallization and preliminary X-ray studies of TON_1713 from Thermococcus onnurineus NA1, a putative member of the haloacid dehalogenase superfamily.
abstract: 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 A resolution using a synchrotron-radiation source. The crystals belong to the triclinic space group P1, with unit-cell parameters a = 52.5, b = 65.8, c = 203.4 A, alpha = 71.1, beta = 79.9, gamma = 74.3 degrees.
authors: Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Republic of Korea.
authors: Binh Van
authors: BV
authors: Le
authors: Hyun Sook
authors: HS
authors: Lee
authors: Yona
authors: Y
authors: Cho
authors: Sung Gyun
authors: SG
authors: Kang
authors: Dong Young
authors: DY
authors: Kim
authors: Yang Gyun
authors: YG
authors: Kim
authors: Kyeong Kyu
authors: KK
authors: Kim
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006867:Hydrolases / Q000737:chemistry* / Q000145:classification; D019712:Thermococcus / Q000201:enzymology*
chemical_list: D006867:Hydrolases; C034507:2-haloacid dehalogenase