Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolution.
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Jelsch C, Lenfant F, Masson JM, Samama JP
Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolution.
FEBS Lett. 1992 Mar 9;299(2):135-42.
- PubMed ID
- 1544485 [ View in PubMed]
- 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.