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Crystal structures of the class D beta-lactamase OXA-13 in the native form and in complex with meropenem.
TLDR
The low level of penicillinase activity revealed by the kinetic analysis of OXA-13 could be related to the specific presence in position 73 of a serine residue located close to the general base Lys70, which results in a decrease of the number of hydrogen-bonding interactions stabilising the catalytic water molecule.
Crystal Structure of the protein drug urate oxidase-inhibitor complex at 2.05 Å resolution
TLDR
The structure of the active site of urate oxidase around the 8-azaxanthine inhibitor reveals an original mechanism of oxidation that does not require any ions or prosthetic groups.
Structure of the imipenem-hydrolyzing class A beta-lactamase SME-1 from Serratia marcescens.
TLDR
The structure of the beta-lactamase SME-1 from Serratia marcescens, a class A enzyme characterized by its significant activity against imipenem, has been determined and it is suggested that a significant conformational change may be necessary in SMe-1 to properly position the hydrolytic water molecule involved in the Hydrolysis of the acyl-enzyme intermediate.
The Multiwavelength Anomalous Solvent Contrast (MASC) Method in Macromolecular Crystallography.
TLDR
The main steps of a MASC experiment are discussed in the context of a MAD-like data collection optimized for accurate measurements of intensities of anomalous pairs at low resolution and the results of preliminary experiments on two protein crystals are reported.
Purification, crystallization, and preliminary X-Ray diffraction analysis of the carbapenem-hydrolyzing class A beta-lactamase Sme-1 from Serratia marcescens.
TLDR
The carbapenem-hydrolyzing class A beta-lactamase Sme-1 from Serratia marcescens S6 was expressed in Escherichia coli and purified by ion-exchange chromatography and gel filtration and crystals of the purified enzyme are suitable for X-ray structure analysis.
Purification, Crystallization, and Preliminary X-Ray Diffraction Analysis of the Carbapenem-Hydrolyzing Class A β-Lactamase Sme-1 fromSerratia marcescens
Abstract The carbapenem-hydrolyzing class A β-lactamase Sme-1 from Serratia marcescens S6 was expressed in Escherichia coli and purified by ion-exchange chromatography and gel filtration. Crystals of
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