Crystallization and preliminary crystallographic analysis of major nitroreductase from Escherichia coli.
NADPH:nitrocompound oxidoreductase from Escherichia coli, NfsA, has been crystallized in the presence of FMN by the vapor-diffusion method using polyethylene glycol 6000 as a precipitant. The crystals belonged to the triclinic space group P1 with cell dimensions, a = 52.2, b = 52.7, c = 53.3 A, alpha = 75.1, beta = 60.1, gamma = 60.5 degrees. The crystals are expected to contain two NfsA molecules per asymmetric unit. The crystals diffracted X-rays to at least 2.3 A resolution and are appropriate for structural analysis at high resolution.
Kobori
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Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Lee
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WC
Akagi
T
T
Sasaki
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H
Zenno
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S
Saigo
K
K
Tanokura
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M
D003460:Crystallization; D018360:Crystallography, X-Ray; D019008:Drug Resistance, Neoplasm; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D005486:Flavin Mononucleotide / Q000737:chemistry; D009249:NADP / Q000737:chemistry; D009601:Nitroreductases / Q000737:chemistry*; D011092:Polyethylene Glycols; D012984:Software
D029968:Escherichia coli Proteins; D011092:Polyethylene Glycols; D009249:NADP; D005486:Flavin Mononucleotide; C116053:NfsA protein, E coli; D009601:Nitroreductases