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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%.

The response regulator DesR, which activates the transcription of the des gene by binding to a regulatory region, is essential for controlling the fluidity of membrane phospholipids. DesR from Streptococcus pneumoniae was overexpressed in Escherichia coli. The protein was purified and crystallized for structural analysis. Diffraction data were collected to 1.7 A resolution using synchrotron radiation and the crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 46.91, b = 71.38, c = 117.73 A. Assuming the presence of a dimer in the asymmetric unit, this corresponds to a V(M) of 2.21 A(3) Da(-1).