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β‐lactamase TEM1 of E. coli Crystal structure determination at 2.5 Å resolution
Author(s) -
Jelsch C.,
Lenfant F.,
Masson J.M.,
Samama J.P.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80232-6
Subject(s) - multiple isomorphous replacement , resolution (logic) , crystallography , crystal structure , molecular replacement , superposition principle , chemistry , crystal (programming language) , escherichia coli , hydrolase , atom (system on chip) , topology (electrical circuits) , diffraction , physics , stereochemistry , enzyme , x ray crystallography , mathematics , combinatorics , biochemistry , computer science , quantum mechanics , gene , artificial intelligence , programming language , embedded system
The crystal structure of β‐lactamase TEM1 from E. coli has been solved to 2.5 Å 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 α coordinates of S. Aureus PC1 enzyme, provided a set of phases used for heavy atom derivatives analysis. The E. coli β‐lactamase TEM1 is made up of two domains whose topology is similar to that of the PC1 enzyme. However, global superposition or the two proteins shows significant differences.