title: Crystallization and preliminary crystallographic analysis of the major NAD(P)H: FMN oxidoreductase of Vibrio fischeri ATCC 7744.
abstract: The major flavin reductase from Vibrio fischeri, FRase I, has been crystallized in the presence of FMN by the vapor diffusion method using polyethylene glycol 4000 as a precipitant. The crystals belonged to the monoclinic space group C2 with unit cell dimensions, a = 101.6 A, b = 63.2 A, c = 74.4 A, and beta = 100.0 degrees. The crystals are expected to contain two FRase I molecules per asymmetric unit. The crystals diffracted X-rays to at least 2.2 A resolution and are appropriate for structural analysis at high resolution.
authors.affiliation: Biotechnology Research Center, University of Tokyo, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Koike
authors.forename: H
authors.initials: H
authors.lastname: Sasaki
authors.forename: M
authors.initials: M
authors.lastname: Tanokura
authors.forename: S
authors.initials: S
authors.lastname: Zenno
authors.forename: K
authors.initials: K
authors.lastname: Saigo
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D038181:FMN Reductase; D005486:Flavin Mononucleotide; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry*; D011092:Polyethylene Glycols; D011487:Protein Conformation; D014733:Vibrio / Q000201:enzymology*
chemical_list: D011092:Polyethylene Glycols; D005486:Flavin Mononucleotide; D038181:FMN Reductase; D009247:NADH, NADPH Oxidoreductases