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FEBS Lett. 1992 Mar 9;299(2):135-42.

Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolution.

Author information

1
Laboratoire de Cristallographie Biologique, IBMC du CNRS, Strasbourg, France.

Abstract

The crystal structure of beta-lactamase TEM1 from E. coli has been solved to 2.5 A resolution by X-ray diffraction methods and refined to a crystallographic R-factor of 22.7%. The structure was determined by multiple isomorphous replacement using four heavy atom derivatives. The solution from molecular replacement, using a polyalanine model constructed from the C alpha coordinates of S. Aureus PCl enzyme, provided a set of phases used for heavy atom derivatives analysis. The E. coli beta-lactamase TEM1 is made up of two domains whose topology is similar to that of the PCl enzyme. However, global superposition of the two proteins shows significant differences.

PMID:
1544485
DOI:
10.1016/0014-5793(92)80232-6
[Indexed for MEDLINE]
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