Crystallization and preliminary crystallographic analysis of the major NAD(P)H: FMN oxidoreductase of Vibrio fischeri ATCC 7744.
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.
Koike
H
H
Biotechnology Research Center, University of Tokyo, Japan.
Sasaki
H
H
Tanokura
M
M
Zenno
S
S
Saigo
K
K
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*
D011092:Polyethylene Glycols; D005486:Flavin Mononucleotide; D038181:FMN Reductase; D009247:NADH, NADPH Oxidoreductases