Open AccessCloning, overexpression, purification, crystallization and preliminary X‐ray diffraction analysis of an atypical two‐cysteine peroxiredoxin (SAOUHSC_01822) from Staphylococcus aureus NCTC 8325
Author(s) -
Bhattacharyya Sudipta,
Dutta Debajyoti,
Ghosh Ananta Kumar,
Das Amit Kumar
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109037580
Subject(s) - crystallization , ammonium sulfate , cysteine , staphylococcus aureus , plasmid , chemistry , crystallography , microbiology and biotechnology , biology , bacteria , biochemistry , gene , chromatography , enzyme , organic chemistry , genetics
An atypical two‐cysteine peroxidase, SAOUHSC_01822, from the virulent Staphylococcus aureus strain NCTC 8325 plays a major role in the reponse of the bacterium to oxidative stress. The protein was cloned, expressed, purified to homogeneity and crystallized. The protein was crystallized from 2 M ammonium sulfate, 0.1 M Na HEPES pH 7, 2%( v / v ) PEG 400. A complete diffraction data set was collected to 2.3 Å resolution using a Rigaku MicroMax HF007 Cu K α X‐ray generator and a Rigaku R‐AXIS IV ++ detector. The crystals belonged to space group P 2 1 , with unit‐cell parameters a = 43.50, b = 149.35, c = 73.73 Å, β = 104.4°, and contained four molecules in the asymmetric unit.