Crystallization and preliminary X-ray analysis of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from Staphylococcus aureus

UDP-N-acetylenolpyruvylglucosamine reductase (MurB) is an essential enzyme in the bacterial cell-wall biosynthetic pathway, making it a potential ther apeutic target for novel antibiotics. Diffraction-quality crystals of both the native and Se-methionine-expressed MurB from Staphylococcus aureus have been prepared by sitting-drop vapour diffusion from solutions containing p olyethylene glycol (PEG) 8000, ammonium sulfate, sodium cacodylate pH 6.5 a nd dimethyl sulfoxide (DMSO). Crystals belong to the cubic space group I2(1 )3, with unit-cell parameters a = b = c = 178.99 Angstrom. X-ray data from these crystals were collected at the Advanced Photon Source 17-ID beamline and were used to solve the MurB structure to 2.3 Angstrom resolution.