ORBi: Wouters J. - Expression, purification, crystallization and preliminary X-ray analysis of the native class C beta-lactamase from Enterobacter cloacae 908R and two mutants.

Reference : Expression, purification, crystallization and preliminary X-ray analysis of the native c...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/78086

Title :	Expression, purification, crystallization and preliminary X-ray analysis of the native class C beta-lactamase from Enterobacter cloacae 908R and two mutants.
Language :	English
Author, co-author :	Wouters, J. [> > > >]
	Charlier, Paulette [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
	Monnaie, D. [> > > >]
	Frère, Jean-Marie [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Fonze, E. [> > > >]
Publication date :	2001
Journal title :	Acta Crystallographica Section D-Biological Crystallography
Publisher :	Blackwell Publishing
Volume :	57
Issue/season :	Pt 1
Pages :	162-4
Peer reviewed :	Yes (verified by ORBi)
Audience :	International
ISSN :	0907-4449
City :	Oxford
Country :	United Kingdom
Keywords :	[en] Crystallization ; Crystallography, X-Ray ; Enterobacter cloacae/enzymology/genetics ; Mutagenesis ; Recombinant Proteins/chemistry/genetics ; beta-Lactamases/chemistry/genetics
Abstract :	[en] Crystals have been obtained of the Enterobacter cloacae 908R beta-lactamase and two point mutants by the vapour-diffusion method using similar conditions [pH 9.0, polyethylene glycol (M(r) = 6000) as precipitant]. The three crystal forms belong to the orthorhombic space group P2(1)2(1)2, with roughly the same unit-cell parameters; i.e. for the wild-type crystals a = 46.46, b = 82.96, c = 95.31 A. In the best cases, the crystals diffract to about 2.1 A 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 beta-lactamases.
Permalink :	http://hdl.handle.net/2268/78086

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