title: Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureus.
abstract: 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 angstrom resolution from a native crystal using synchrotron radiation. The crystal belonged to the hexagonal space group P6(1)22, with unit-cell parameters a = b = 89.84, c = 88.75 angstrom, alpha = beta = 90, gamma = 120 degrees. Assuming the presence of one molecule in the asymmetric unit, the calculated Matthews coefficient value was 2.21 angstrom(3) Da(-1), with a solvent content of 57.1%.
authors.affiliation: Korea University, Seoul, Republic of Korea.
authors.forename: Seoung Min
authors.initials: SM
authors.lastname: Bong
authors.forename: Jin Ho
authors.initials: JH
authors.lastname: Moon
authors.forename: Hwa Young
authors.initials: HY
authors.lastname: Kim
authors.forename: Hong Seok
authors.initials: HS
authors.lastname: Kim
authors.forename: Young Min
authors.initials: YM
authors.lastname: Chi
authors.forename: Augustine Yonghwi
authors.initials: AY
authors.lastname: Kim
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D051150:Methionine Sulfoxide Reductases / Q000737:chemistry*; D008969:Molecular Sequence Data; D050862:Oxidoreductases Acting on Sulfur Group Donors; D011487:Protein Conformation; D013211:Staphylococcus aureus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D050862:Oxidoreductases Acting on Sulfur Group Donors; C030542:sulfoxide reductase; D051150:Methionine Sulfoxide Reductases