title: Crystallization and preliminary X-ray analysis of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from Staphylococcus aureus.
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.
authors: Pharmacia, 301 Henrietta Street, Kalamazoo, MI 49007, USA. melissa.s.harris@pharmacia.com
authors: M S
authors: MS
authors: Harris
authors: J T
authors: JT
authors: Herberg
authors: J I
authors: JI
authors: Cialdella
authors: J P
authors: JP
authors: Martin
authors: T E
authors: TE
authors: Benson
authors: G H
authors: GH
authors: Choi
authors: E T
authors: ET
authors: Baldwin
mesh_terms: D002237:Carbohydrate Dehydrogenases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D013211:Staphylococcus aureus / Q000201:enzymology*
chemical_list: D002237:Carbohydrate Dehydrogenases; C023215:UDP-N-acetylmuramate dehydrogenase