title: Crystallization and preliminary analysis of xenobiotic reductase B from Pseudomonas fluorescens I-C.
abstract: Single crystals have been obtained of xenobiotic reductase B (XenB), a flavoenzyme isolated and cloned from Pseudomonas fluorescens I-C. The enzyme catalyzes the NADPH-dependent elimination of nitrite from nitroglycerin with an approximately fivefold kinetic preference for the middle nitro group, primarily yielding 1,3-dinitroglycerol. X-ray diffraction data sets have been collected from native crystals to 2.3 A resolution. The space group is P4(1)2(1)2, with unit-cell parameters a = b = 140, c = 95.6 A. The asymmetric unit is likely to contain at least two XenB molecules (V(M) = 3.1 A(3) Da(-1), 60% solvent) and a molecular-replacement solution has been determined in order to solve the structure.
authors.affiliation: School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0400, USA. allen.orville@chemistry.gatech.edu
authors.forename: Allen M
authors.initials: AM
authors.lastname: Orville
authors.forename: Linda
authors.initials: L
authors.lastname: Manning
authors.forename: David S
authors.initials: DS
authors.lastname: Blehert
authors.forename: Brian G
authors.initials: BG
authors.lastname: Fox
authors.forename: Glenn H
authors.initials: GH
authors.lastname: Chambliss
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D011551:Pseudomonas fluorescens / Q000201:enzymology*; D015262:Xenobiotics / Q000378:metabolism*
chemical_list: D015262:Xenobiotics; D010088:Oxidoreductases