Crystallization and preliminary crystallographic data for an FMN-dependent nitroreductase from Escherichia coli B

J Mol Biol. 1994 May 20;238(5):852-3. doi: 10.1006/jmbi.1994.1340.

Abstract

An FMN-dependent nitroreductase enzyme isolated from Escherichia coli B has been crystallized in a form suitable for high-resolution structural analysis. The crystals belong to the tetragonal space group P4(1)2(1)2 or its enantiomorph P4(3)2(1)2 with cell parameters a = b = 57.74 A, c = 275.51 A and two molecules per asymmetric unit. Diffraction extends to beyond 1.9 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Flavin Mononucleotide
  • Molecular Structure
  • Nitroreductases / chemistry*

Substances

  • Flavin Mononucleotide
  • Nitroreductases