PMID:2008433

Citation	Bauer, AJ, Rayment, I, Frey, PA and Holden, HM (1991) The isolation, purification, and preliminary crystallographic characterization of UDP-galactose-4-epimerase from Escherichia coli. Proteins 9:135-42
Abstract	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.
Links	PubMed Online version:10.1002/prot.340090207
Keywords	Crystallization; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression; UDPglucose 4-Epimerase/chemistry; UDPglucose 4-Epimerase/genetics; UDPglucose 4-Epimerase/isolation & purification; X-Ray Diffraction
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.