IngentaConnect Crystallization and preliminary analysis of xenobiotic reductase ...

Authors: Orville, Allen M.; Manning, Linda; Blehert, David S.; Studts, Joey M.; Fox, Brian G.; Chambliss, Glenn H.

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 957-961(5)

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 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.

Keywords: FMN; nitroglycerin; nitroester reductase; MAD phasing

Document Type: Research article

DOI: 10.1107/S0907444904006158

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