Crystallization and preliminary X-ray analysis of gamma-glutamyltranspeptidase from Escherichia coli K-12

H Kumagai; S Nohara; H Suzuki; W Hashimoto; K Yamamoto; H Sakai; K Sakabe; K Fukuyama; N Sakabe

doi:10.1006/jmbi.1993.1677

Crystallization and preliminary X-ray analysis of gamma-glutamyltranspeptidase from Escherichia coli K-12

J Mol Biol. 1993 Dec 20;234(4):1259-62. doi: 10.1006/jmbi.1993.1677.

Authors

H Kumagai¹, S Nohara, H Suzuki, W Hashimoto, K Yamamoto, H Sakai, K Sakabe, K Fukuyama, N Sakabe

Affiliation

¹ Department of Food Science and Technology, Faculty of Agriculture Kyoto University, Japan.

PMID: 7903400
DOI: 10.1006/jmbi.1993.1677

Abstract

gamma-Glutamyltranspeptidase (EC 2.3.2.2) from Escherichia coli K-12 has been purified and crystallized by means of vapor diffusion in hanging drops. Two kinds of crystals on cell dimensions were found for X-ray diffraction analysis, one from ammonium sulfate and the other from polyethylene glycol 6000 as precipitants. The crystals of the orthorhombic form grown in the presence of 15% polyethylene glycol and 20 mM sodium acetate buffer were chosen for further analysis. The crystals belonged to space group P2(1)2(1)2(1), with cell dimensions of a = 128.1, b = 129.9 and c = 79.2 A, and two molecules constitute an asymmetric unit. These crystals diffracted to 2.0 A resolution and were suitable for X-ray crystallographic studies.

Publication types

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

MeSH terms

Bacterial Proteins
Crystallography, X-Ray
Escherichia coli / enzymology
Recombinant Proteins
gamma-Glutamyltransferase / ultrastructure*

Substances

Bacterial Proteins
Recombinant Proteins
gamma-Glutamyltransferase