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

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

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

doi

10.1006/jmbi.1993.1677

subject

Has Abstract

pub_date

1993-12-20 00:00:00

pages

1259-62

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(83)71677-3

journal_volume

234

pub_type

杂志文章

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