Reference : Expression, purification, crystallization and preliminary X-ray analysis of the nativ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/78086
Expression, purification, crystallization and preliminary X-ray analysis of the native class C beta-lactamase from Enterobacter cloacae 908R and two mutants.
English
Wouters, J. [> > > >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
Monnaie, D. [> > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Fonze, E. [> > > >]
2001
Acta Crystallographica Section D-Biological Crystallography
Blackwell Publishing
57
Pt 1
162-4
Yes (verified by ORBi)
International
0907-4449
Oxford
United Kingdom
[en] Crystallization ; Crystallography, X-Ray ; Enterobacter cloacae/enzymology/genetics ; Mutagenesis ; Recombinant Proteins/chemistry/genetics ; beta-Lactamases/chemistry/genetics
[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.
http://hdl.handle.net/2268/78086

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