Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolution. |
| |
Authors: | C Jelsch F Lenfant J M Masson J P Samama |
| |
Institution: | 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. |
| |
Keywords: | |
|
|