title: Crystallization and preliminary X-ray crystallographic analysis of the putative NADP(H)-dependent oxidoreductase YncB from Vibrio vulnificus.
abstract: The yncB gene product from Vibrio vulnificus, which belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily, was crystallized using the microbatch crystallization method at 295 K. Diffraction data sets were collected using synchrotron radiation. Crystals of selenomethionine-substituted YncB protein belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 90.52, b = 91.56, c = 104.79 Å. Assuming the presence of two molecules in the asymmetric unit, the solvent content was estimated to be about 57%. Crystals of the YncB-NADP(H) complex belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 90.14, c = 105.61 Å. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 56.42%.
authors.affiliation: Marine Biotechnology Research Division, Korea Institute of Ocean Science and Technology, Ansan, Republic of Korea.
authors.forename: Min-Kyu
authors.initials: MK
authors.lastname: Kim
authors.forename: Young Jun
authors.initials: YJ
authors.lastname: An
authors.forename: Chang-Sook
authors.initials: CS
authors.lastname: Jeong
authors.forename: Sun-Shin
authors.initials: SS
authors.lastname: Cha
mesh_terms: D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D041261:Vibrio vulnificus / Q000201:enzymology*
chemical_list: D010088:Oxidoreductases