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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%.

SUBMITTER: Bong SM

PROVIDER: S-EPMC2777039 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase from Staphylococcus aureus.

Bong Seoung Min SM Moon Jin Ho JH Kim Hwa Young HY Kim Hong Seok HS Chi Young Min YM Kim Augustine Yonghwi AY

Acta crystallographica. Section F, Structural biology and crystallization communications 20091030 Pt 11

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 = ...[more]

PMID: 19923731

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