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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Seoung Min BongAugustine Yonghwi Kim

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%.

References

Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Oct 3, 1998·Acta Crystallographica. Section D, Biological Crystallography·A T BrüngerG L Warren
Jan 27, 2004·Molecular Pharmacology·Roya ZoraghiSharron H Francis
Feb 1, 2005·Biochimica Et Biophysica Acta·Herbert WeissbachNathan Brot
Feb 1, 2005·Biochimica Et Biophysica Acta·Sandrine Boschi-MullerGuy Branlant
Feb 1, 2005·Biochimica Et Biophysica Acta·Brice KauffmannFrédérique Favier
May 31, 2007·Proceedings of the National Academy of Sciences of the United States of America·Zhidong LinW Todd Lowther
Feb 28, 2008·Archives of Biochemistry and Biophysics·Sandrine Boschi-MullerGuy Branlant

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