Crystallization and preliminary crystallographic analysis of the major NAD(P)H: FMN oxidoreductase of Vibrio fischeri ATCC 7744

J Struct Biol. 1996 Jul-Aug;117(1):70-2. doi: 10.1006/jsbi.1996.0070.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • FMN Reductase
  • Flavin Mononucleotide
  • NADH, NADPH Oxidoreductases / chemistry*
  • Polyethylene Glycols
  • Protein Conformation
  • Vibrio / enzymology*

Substances

  • Polyethylene Glycols
  • Flavin Mononucleotide
  • FMN Reductase
  • NADH, NADPH Oxidoreductases