Crystallization and preliminary X-ray studies of T4 phage beta-glucosyltransferase

P S Freemont; W Rüger

doi:10.1016/0022-2836(88)90021-6

Crystallization and preliminary X-ray studies of T4 phage beta-glucosyltransferase

J Mol Biol. 1988 Sep 20;203(2):525-6. doi: 10.1016/0022-2836(88)90021-6.

Authors

P S Freemont¹, W Rüger

Affiliation

¹ Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.

PMID: 2974086
DOI: 10.1016/0022-2836(88)90021-6

Abstract

Crystals of the DNA glucosylating enzyme beta-glucosyltransferase from phage T4 have been grown in the presence of uridine diphosphate glucose. The crystals are orthorhombic, space group P2(1)2(1)2 with a = 148.3 A, b = 52.6 A, c = 52.6 A. The assumption of one monomer of Mr 40,000 per asymmetric unit gives rise to a Vm of 2.56 A 3/dalton. The crystals diffract to beyond 2.7 A and are suitable for X-ray structure analysis.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Glucosyltransferases*
T-Phages / enzymology*
X-Ray Diffraction

Substances

Glucosyltransferases
DNA beta-glucosyltransferase