Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional
L R Olsen1, Y Tian, S L Roderick
1Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Acta Crystallographica. Section D, Biological Crystallography
|February 15, 2001
Abstract:
Crystals of Escherichia coli GlmU, a bifunctional enzyme catalyzing the acetylation of glucosamine-1-phosphate and uridylylation of N-acetylglucosamine-1-phosphate to produce UDP-GlcNAc, have been prepared in complex with coenzyme A and UDP-GlcNAc. These crystals belong to space group R32, with unit-cell parameters a = 104.5, c = 648.2 A, diffract to at least 2.1 A resolution and may contain two subunits of the trimeric enzyme per asymmetric unit.
