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- W2001786953 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." @default.
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- W2001786953 date "2001-06-21" @default.
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- W2001786953 title "Crystallization and preliminary X-ray analysis of UDP-<i>N</i>-acetylenolpyruvylglucosamine reductase (MurB) from<i>Staphylococcus aureus</i>" @default.
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- W2001786953 doi "https://doi.org/10.1107/s0907444901006552" @default.
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