Open AccessCrystallization and preliminary X‐ray crystallographic analysis of free methionine‐( R )‐sulfoxide reductase from Staphylococcus aureus
Author(s) -
Bong Seoung Min,
Moon Jin Ho,
Kim Hwa Young,
Kim Hong Seok,
Chi Young Min,
Kim Augustine Yonghwi
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109037105
Subject(s) - ammonium sulfate , crystallization , methionine , crystallography , chemistry , crystal structure , escherichia coli , x ray crystallography , methionine sulfoxide , sulfoxide , solvent , stereochemistry , diffraction , biochemistry , organic chemistry , amino acid , physics , optics , gene
Free methionine‐( R )‐sulfoxide reductase (fRMsr) catalyzes the reduction of the free form of methionine‐( R )‐sulfoxide back to free methionine. The fRMsr protein from Staphylococcus aureus was overexpressed in Escherichia coli , purified and crystallized at 295 K using ammonium sulfate as a precipitant. Diffraction data were collected to 1.7 Å resolution from a native crystal using synchrotron radiation. The crystal belonged to the hexagonal space group P 6 1 22, with unit‐cell parameters a = b = 89.84, c = 88.75 Å, α = β = 90, γ = 120°. Assuming the presence of one molecule in the asymmetric unit, the calculated Matthews coefficient value was 2.21 Å 3 Da −1 , with a solvent content of 57.1%.