Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureus.
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%.
Bong
Seoung Min
SM
Korea University, Seoul, Republic of Korea.
Moon
Jin Ho
JH
Kim
Hwa Young
HY
Kim
Hong Seok
HS
Chi
Young Min
YM
Kim
Augustine Yonghwi
AY
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*
D001426:Bacterial Proteins; D050862:Oxidoreductases Acting on Sulfur Group Donors; C030542:sulfoxide reductase; D051150:Methionine Sulfoxide Reductases