title: Crystallization and preliminary crystallographic data for an FMN-dependent nitroreductase from Escherichia coli B.
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.
authors.affiliation: CRC Biomolecular Structure Unit, Institute of Cancer Research Sutton, Surrey, U.K.
authors.forename: J V
authors.initials: JV
authors.lastname: Skelly
authors.forename: P J
authors.initials: PJ
authors.lastname: Collins
authors.forename: R J
authors.initials: RJ
authors.lastname: Knox
authors.forename: G M
authors.initials: GM
authors.lastname: Anlezark
authors.forename: R G
authors.initials: RG
authors.lastname: Melton
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D005486:Flavin Mononucleotide; D015394:Molecular Structure; D009601:Nitroreductases / Q000737:chemistry*
chemical_list: D005486:Flavin Mononucleotide; D009601:Nitroreductases