Expression, purification, crystallization and preliminary X-ray analysis of the native class C β-lactamase from Enterobacter cloacae 908R and two mutants
| Autor: | Johan Wouters, Paulette Charlier, Didier Monnaie, E. Fonze, Jean-Marie Frère |
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| Jazyk: | angličtina |
| Rok vydání: | 2001 |
| Předmět: |
medicine.medical_treatment
Mutant General Medicine Polyethylene glycol Biology Crystallography X-Ray biology.organism_classification Recombinant Proteins beta-Lactamases law.invention Crystal Serine chemistry.chemical_compound Crystallography chemistry Mutagenesis Structural Biology law Enterobacter cloacae Beta-lactamase medicine Orthorhombic crystal system Crystallization |
| Zdroj: | Acta Crystallographica Section D: Biological Crystallography. 57(1):162-164 |
| ISSN: | 1399-0047 0907-4449 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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