Expression, purification, crystallization and preliminary X-ray analysis of the native class C β-lactamase from Enterobacter cloacae 908R and two mutants

J. Wouters, P. Charlier, D. Monnaie, J. M. Frère, E. Fonzé

Research output: Contribution to journalArticlepeer-review

Abstract

Crystals have been obtained of the Enterobacter cloacae 908R β-lactamase and two point mutants by the vapour-diffusion method using similar conditions [pH 9.0, polythylene glycol (Mr= 6000) as precipitant]. The three crystal forms belong to the orthorhombic space group P21212, with roughly the same unit-cell parameters; i.e. for the wild-type crystals a = 46.46, b = 82.96, c = 95.31 Å. In the best cases, the crystals diffract to about 2.1 Å resolution on a rotating-anode X-ray source at room temperature. Co-crystallization experiments of poor substrates with the wild-type protein and the active-site serine mutant (S64C) are planned and should lead to a better understanding of the catalytic mechanism of class C β-lactamases.

Original languageEnglish
Pages (from-to)162-164
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number1
DOIs
Publication statusPublished - 1 Feb 2001

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