ISSN:
0887-3585
Keywords:
X-ray crystallography
;
galactose metabolism
;
nucleotide binding
;
nonstereospecific hydride transfer
;
protein structure
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
Notes:
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 P212121 with unit cell dimensions, a = 76.3 Å, b = 83.1 Å, and c = 132.1 Å. Based on still setting photographs, the crystals diffract to a nominal resolution of 2.3 Å 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.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/prot.340090207
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