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O Dideberg

Showing results (21-30 of 80) with videos related to

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Acta Crystallographica. Section D, Biological Crystallography|March 1, 1995
Crystallization and preliminary X-ray diffraction studies of Escherichia coli glyceraldehyde-3-phosphate dehydrogenaseL Olivier, G Buisson, E Fanchon, et al.
The Journal of Biological Chemistry|August 9, 2001
The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharideG Michel, L Chantalat, E Fanchon, et al.
The Biochemical Journal|October 15, 1994
Site-directed mutagenesis of proposed active-site residues of penicillin-binding protein 5 from Escherichia coliM P van der Linden, L de Haan, O Dideberg, et al.
Biochemical Society Transactions|December 1, 1988
Penicillin-recognizing enzymesJ M Frère, B Joris, O Dideberg, et al.
Acta Crystallographica. Section D, Biological Crystallography|May 20, 2000
Expression, purification, crystallization and preliminary X-ray analysis of the iota-carrageenase from Alteromonas fortisG Michel, D Flament, T Barbeyron, et al.
Journal of Molecular Biology|May 16, 1997
A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+C Didierjean, S Rahuel-Clermont, B Vitoux, et al.
Journal of Molecular Biology|December 5, 1983
Crystallographic data for the beta-lactamase from Enterobacter cloacae P99P Charlier, O Dideberg, J M Frère, et al.
European Journal of Biochemistry|March 10, 1998
Kinetic studies of allosteric catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosaG Sainz, C Tricot, M F Foray, et al.
Journal of Molecular Biology|April 12, 1996
Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativityE Duée, L Olivier-Deyris, E Fanchon, et al.
Protein Engineering|October 1, 1991
Arginine 220 is a critical residue for the catalytic mechanism of the Streptomyces albus G beta-lactamaseF Jacob-Dubuisson, J Lamotte-Brasseur, O Dideberg, et al.
Pageof 8

Showing results (21-30 of 80) with videos related to

Sort By:
Pageof 8
Acta Crystallographica. Section D, Biological Crystallography|March 1, 1995
Crystallization and preliminary X-ray diffraction studies of Escherichia coli glyceraldehyde-3-phosphate dehydrogenaseL Olivier, G Buisson, E Fanchon, et al.
The Journal of Biological Chemistry|August 9, 2001
The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharideG Michel, L Chantalat, E Fanchon, et al.
The Biochemical Journal|October 15, 1994
Site-directed mutagenesis of proposed active-site residues of penicillin-binding protein 5 from Escherichia coliM P van der Linden, L de Haan, O Dideberg, et al.
Biochemical Society Transactions|December 1, 1988
Penicillin-recognizing enzymesJ M Frère, B Joris, O Dideberg, et al.
Acta Crystallographica. Section D, Biological Crystallography|May 20, 2000
Expression, purification, crystallization and preliminary X-ray analysis of the iota-carrageenase from Alteromonas fortisG Michel, D Flament, T Barbeyron, et al.
Journal of Molecular Biology|May 16, 1997
A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+C Didierjean, S Rahuel-Clermont, B Vitoux, et al.
Journal of Molecular Biology|December 5, 1983
Crystallographic data for the beta-lactamase from Enterobacter cloacae P99P Charlier, O Dideberg, J M Frère, et al.
European Journal of Biochemistry|March 10, 1998
Kinetic studies of allosteric catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosaG Sainz, C Tricot, M F Foray, et al.
Journal of Molecular Biology|April 12, 1996
Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativityE Duée, L Olivier-Deyris, E Fanchon, et al.
Protein Engineering|October 1, 1991
Arginine 220 is a critical residue for the catalytic mechanism of the Streptomyces albus G beta-lactamaseF Jacob-Dubuisson, J Lamotte-Brasseur, O Dideberg, et al.
Pageof 8