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