Crystallization and preliminary X-ray analysis of gamma-glutamyltranspeptidase from Escherichia coli K-12.
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.
Kumagai
H
H
Department of Food Science and Technology, Faculty of Agriculture Kyoto University, Japan.
Nohara
S
S
Suzuki
H
H
Hashimoto
W
W
Yamamoto
K
K
Sakai
H
H
Sakabe
K
K
Fukuyama
K
K
Sakabe
N
N
D001426:Bacterial Proteins; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology; D011994:Recombinant Proteins; D005723:gamma-Glutamyltransferase / Q000648:ultrastructure*
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D005723:gamma-Glutamyltransferase