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