Cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of an atypical two-cysteine peroxiredoxin (SAOUHSC_01822) from Staphylococcus aureus NCTC 8325

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 Kα X-­ray generator and a Rigaku R-AXIS IV⁺⁺ detector. The crystals belonged to space group P2₁, 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.