| Literature DB >> 11418774 |
M S Harris1, J T Herberg, J I Cialdella, J P Martin, T E Benson, G H Choi, 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 I2(1)3, with unit-cell parameters a = b = c = 178.99 A. 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 A resolution.Entities:
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Year: 2001 PMID： 11418774 DOI： 10.1107/s0907444901006552
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN： 0907-4449