Expression, purification, crystallization and preliminary X-ray diffraction analysis of a type II NADH:quinone oxidoreductase from the human pathogen Staphylococcus aureus

In recent years, type II NADH dehydrogenases (NDH-IIs) have emerged as potential drug targets for a wide range of human disease causative agents. In this work, the NDH-II enzyme from the Gram-positive human pathogen Staphylococcus aureus was recombinantly expressed in Escherichia coli, purified, crystallized and a crystallographic data set was collected at a wavelength of 0.873 angstrom. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 81.8, b = 86.0, c = 269.9 angstrom, contained four monomers per asymmetric unit and diffracted to a resolution of 3.32 angstrom. A molecular-replacement solution was obtained and model building and refinement are currently under way.