The isolation, purification, and preliminary crystallographic characterization of UDP-galactose-4-epimerase from Escherichia coli.
Uridine diphosphogalactose-4-epimerase from E. coli has been crystallized in a form suitable for a high-resolution X-ray crystallographic structural analysis. The enzyme complexed with a substrate analogue, uridine diphosphobenzene (UDP-benzene), crystallizes readily using polyethylene glycol 8000 as the precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions, a = 76.3 A, b = 83.1 A, and c = 132.1 A. Based on still setting photographs, the crystals diffract to a nominal resolution of 2.3 A and are stable in the X-ray beam. The enzyme used in these experiments was produced by a new expression system and a modified purification scheme.
Bauer
A J
AJ
Institute for Enzyme Research, Graduate School, University of Wisconsin-Madison 53705.
Rayment
I
I
Frey
P A
PA
Holden
H M
HM
D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D015870:Gene Expression; D014534:UDPglucose 4-Epimerase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction
D014534:UDPglucose 4-Epimerase