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PMID:7903400
| Citation |
Kumagai, H, Nohara, S, Suzuki, H, Hashimoto, W, Yamamoto, K, Sakai, H, Sakabe, K, Fukuyama, K and Sakabe, N (1993) Crystallization and preliminary X-ray analysis of gamma-glutamyltranspeptidase from Escherichia coli K-12. J. Mol. Biol. 234:1259-62 |
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| 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. |
| Links |
PubMed Online version:10.1006/jmbi.1993.1677 |
| Keywords |
Bacterial Proteins; Crystallography, X-Ray; Escherichia coli/enzymology; Recombinant Proteins; gamma-Glutamyltransferase/ultrastructure |
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