Crystallization and preliminary analysis of xenobiotic reductase A and ligand complexes from Pseudomonas putida II-B

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...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2004-05, Vol.60 (5), p.957-961
Main Authors: Orville, Allen M., Manning, Linda, Blehert, David S., Studts, Joey M., Fox, Brian G., Chambliss, Glenn H.
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Catalytic Domain
Crystallization
Crystallography, X-Ray
Flavoproteins - chemistry
Flavoproteins - metabolism
FMN
Ligands
MAD phasing
Metronidazole - chemistry
Metronidazole - metabolism
nitroester reductase
nitroglycerin
Nitroglycerin - chemistry
Nitroglycerin - metabolism
Oxidoreductases - chemistry
Oxidoreductases - metabolism
Protein Conformation
Pseudomonas putida - enzymology
Reproducibility of Results
Selenomethionine - chemistry
Selenomethionine - metabolism
Trinitrotoluene - chemistry
Trinitrotoluene - metabolism
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Summary: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 Å. 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 P21212, with unit‐cell parameters a = 84, b = 158, c = 57 Å. 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 21 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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444904006158