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Preliminary crystallographic analysis of a complex between tetracycline and the trypsin-modified form of Escherichia coli elongation factor Tu.

作者信息

Mui S, Delaria K, Jurnak F

机构信息

Department of Biochemistry, University of California, Riverside 92521.

出版信息

J Mol Biol. 1990 Apr 5;212(3):445-7. doi: 10.1016/0022-2836(90)90322-D.

DOI:10.1016/0022-2836(90)90322-D
PMID:2182884
Abstract

Crystals of a complex between the antibiotic tetracycline and the trypsin-modified form of the Escherichia coli protein elongation factor Tu have been grown in a form suitable for high-resolution X-ray diffraction analysis. The crystals belong to space group P2(1), with cell dimensions a = 69.7 A, b = 156.4 A, c = 135.4 A and beta = 95.3 degrees, and contain six molecules of the complex per asymmetric unit. The crystals are well ordered and diffract to a resolution of 2.3 A.

摘要

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