title: Crystallization and preliminary X-ray diffraction studies of a mammalian steroid dehydrogenase.
abstract: 20 beta-Hydroxysteroid dehydrogenase from the cytosolic fraction of neonatal pig testis is a NADPH-dependent enzyme that catalyzes the reduction of the C-20 ketone of C21-steroids. It is 85% homologous in amino acid sequence to the human enzyme, carbonyl reductase. The enzyme has been crystallized from 36% saturated ammonium sulfate in 10 mM 2-[N-Morpholino]ethanesulfonic acid buffer. The size and the quality of nicely formed square bi-pyramidal crystals were improved by using a "seeding" technique. The crystals diffract X-rays to at least 2.5 A resolution. The space group is P4(1)2(1)2 (or P4(3)2(1)2) and the unit-cell dimensions are a = b = 58.53 A, c = 165.64 A. There is one molecule (M(r) = 30.5 kDa; 289 amino acid residues) in the asymmetric unit. An intensity data set to 2.5 A has been collected with an overall Rmerge of 6.6% for all reflections.
authors.affiliation: Medical Foundation of Buffalo, Inc., NY 14203.
authors.forename: D
authors.initials: D
authors.lastname: Ghosh
authors.forename: M
authors.initials: M
authors.lastname: Erman
authors.forename: W
authors.initials: W
authors.lastname: Pangborn
authors.forename: W L
authors.initials: WL
authors.lastname: Duax
authors.forename: S
authors.initials: S
authors.lastname: Nakajin
authors.forename: S
authors.initials: S
authors.lastname: Ohno
authors.forename: M
authors.initials: M
authors.lastname: Shinoda
mesh_terms: D000818:Animals; D003349:Cortisone Reductase / Q000737:chemistry*; D003460:Crystallization; D013552:Swine; D014961:X-Ray Diffraction
chemical_list: D003349:Cortisone Reductase