Acta Crystallographica Section D

Biological Crystallography

Volume 57, Part 7 (July 2001)

crystallization papers

Acta Cryst. (2001). D57, 1032-1035 [ doi:10.1107/S0907444901006552 ]

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

M. S. Harris, J. T. Herberg, J. I. Cialdella, J. P. Martin Jr, T. E. Benson, G. H. Choi and E. T. Baldwin

Abstract: UDP-N-acetylenolpyruvylglucosamine reductase (MurB) is an essential enzyme in the bacterial cell-wall biosynthetic pathway, making it a potential therapeutic 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 polyethylene glycol (PEG) 8000, ammonium sulfate, sodium cacodylate pH 6.5 and dimethyl sulfoxide (DMSO). Crystals belong to the cubic space group I2₁3, with unit-cell parameters a = b = c = 178.99 Å. 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 Å resolution.

Keywords: UDP-N-acetylenolpyruvylglucosamine reductase; oxidoreductases.