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Crystallization and preliminary X-ray analysis of gamma-glutamyltranspeptidase from Escherichia coli K-12.
J Mol Biol. 1993 Dec 20; 234(4):1259-62.JM

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.

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Authors+Show Affiliations

Kumagai H
Department of Food Science and Technology, Faculty of Agriculture Kyoto University, Japan.
Nohara S
No affiliation info available
Suzuki H
No affiliation info available
Hashimoto W
No affiliation info available
Yamamoto K
No affiliation info available
Sakai H
No affiliation info available
Sakabe K
No affiliation info available
Fukuyama K
No affiliation info available
Sakabe N
No affiliation info available

MeSH

Bacterial ProteinsCrystallography, X-RayEscherichia coliRecombinant Proteinsgamma-Glutamyltransferase

Pub Type(s)

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

Language

eng

PubMed ID

7903400

Citation

Kumagai, H, et al. "Crystallization and Preliminary X-ray Analysis of Gamma-glutamyltranspeptidase From Escherichia Coli K-12." Journal of Molecular Biology, vol. 234, no. 4, 1993, pp. 1259-62.
Kumagai H, Nohara S, Suzuki H, et al. Crystallization and preliminary X-ray analysis of gamma-glutamyltranspeptidase from Escherichia coli K-12. J Mol Biol. 1993;234(4):1259-62.
Kumagai, H., Nohara, S., Suzuki, H., Hashimoto, W., Yamamoto, K., Sakai, H., Sakabe, K., Fukuyama, K., & Sakabe, N. (1993). Crystallization and preliminary X-ray analysis of gamma-glutamyltranspeptidase from Escherichia coli K-12. Journal of Molecular Biology, 234(4), 1259-62.
Kumagai H, et al. Crystallization and Preliminary X-ray Analysis of Gamma-glutamyltranspeptidase From Escherichia Coli K-12. J Mol Biol. 1993 Dec 20;234(4):1259-62. PubMed PMID: 7903400.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray analysis of gamma-glutamyltranspeptidase from Escherichia coli K-12. AU - Kumagai,H, AU - Nohara,S, AU - Suzuki,H, AU - Hashimoto,W, AU - Yamamoto,K, AU - Sakai,H, AU - Sakabe,K, AU - Fukuyama,K, AU - Sakabe,N, PY - 1993/12/20/pubmed PY - 1993/12/20/medline PY - 1993/12/20/entrez SP - 1259 EP - 62 JF - Journal of molecular biology JO - J Mol Biol VL - 234 IS - 4 N2 - 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. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/7903400/Crystallization_and_preliminary_X_ray_analysis_of_gamma_glutamyltranspeptidase_from_Escherichia_coli_K_12_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(83)71677-3 DB - PRIME DP - Unbound Medicine ER -