title: Crystallization and preliminary analysis of xenobiotic reductase A and ligand complexes from Pseudomonas putida II-B.
abstract: Diffraction-quality crystals have been obtained of the xenobiotic reductase A (XenA) from Pseudomonas II-B, which was originally cultured from the contaminated soil of a World War II era munitions-manufacturing plant. Several complete X-ray diffraction data sets have been collected and analyzed. The native XenA data set includes reflections between 35 and 1.65 A. Four-wavelength MAD data sets from selenomethionine-enriched XenA and from three different ligand complexes are also reported. The XenA crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 84, b = 158, c = 57 A. Experimental phasing from analysis of the MAD data from selenomethionine-enriched XenA reveals the presence of two molecules in the asymmetric unit. They are related by a non-crystallographic 2(1) screw axis nearly parallel to the c axis, but offset by a quarter unit-cell translation. Thus, the local symmetry produces approximate systematic absences along the (00l) principal axis and complicates the space-group determination.
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: Joey M
authors.initials: JM
authors.lastname: Studts
authors.forename: Brian G
authors.initials: BG
authors.lastname: Fox
authors.forename: Glenn H
authors.initials: GH
authors.lastname: Chambliss
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray; D005420:Flavoproteins / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D008795:Metronidazole / Q000737:chemistry / Q000378:metabolism; D005996:Nitroglycerin / Q000737:chemistry / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000201:enzymology*; D015203:Reproducibility of Results; D012645:Selenomethionine / Q000737:chemistry / Q000378:metabolism; D014303:Trinitrotoluene / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D005420:Flavoproteins; D008024:Ligands; C122134:XenA protein, Pseudomonas putida; D014303:Trinitrotoluene; D008795:Metronidazole; D012645:Selenomethionine; D010088:Oxidoreductases; D005996:Nitroglycerin