19923731 |
Bong SM, Moon JH, Kim HY, Kim HS, Chi YM, Kim AY: Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1120-2. Epub 2009 Oct 30. 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%. |
82(1,1,1,2) |