title: Crystallization and preliminary X-ray analysis of the complex of NADH and 3alpha-hydroxysteroid dehydrogenase from Pseudomonas sp. B-0831.
abstract: The NAD(P)(+)-dependent enzyme 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD) catalyzes the reversible interconversion of hydroxyl and oxo groups at position 3 of the steroid nucleus. The complex of NADH and 3alpha-HSD from Pseudomonas sp. B-0831 was crystallized by the hanging-drop vapour-diffusion method. Refinement of crystallization conditions with microseeding improved the quality of the X-ray diffraction data to a resolution of 1.8 A. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 62.46, b = 82.25, c = 86.57 A, and contained two molecules, reflecting dimer formation of 3alpha-HSD, in the asymmetric unit.
authors.affiliation: Graduate School of Agriculture, Kyoto Prefectural University, 1-5 Hangi-cho, Shimogamo, Sakyo-ku, Kyoto, Kyoto 606-8522, Japan.
authors.forename: Sachiyo
authors.initials: S
authors.lastname: Kataoka
authors.forename: Shota
authors.initials: S
authors.lastname: Nakamura
authors.forename: Tadayasu
authors.initials: T
authors.lastname: Ohkubo
authors.forename: Shigeru
authors.initials: S
authors.lastname: Ueda
authors.forename: Susumu
authors.initials: S
authors.lastname: Uchiyama
authors.forename: Yuji
authors.initials: Y
authors.lastname: Kobayashi
authors.forename: Masayuki
authors.initials: M
authors.lastname: Oda
mesh_terms: D015096:3-Hydroxysteroid Dehydrogenases / Q000737:chemistry*; D045002:3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D019281:Dimerization; D009243:NAD / Q000737:chemistry*; D011549:Pseudomonas / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D009243:NAD; D015096:3-Hydroxysteroid Dehydrogenases; D045002:3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)