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Christoph Kratky

Showing results (1-10 of 24) with videos related to

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Nature|August 30, 2013
A coordinated approach is key for open accessChristoph Kratky
Current Opinion in Chemical Biology|November 5, 2002
Coenzyme B(12) dependent glutamate mutaseKarl Gruber, Christoph Kratky
Progress in the Chemistry of Organic Natural Products|January 31, 2015
Structure elucidation of natural compounds by X-ray crystallographyUlrike Wagner, Christoph Kratky
Journal of Biotechnology|January 26, 2007
Structural determinants of the enantioselectivity of the hydroxynitrile lyase from Hevea brasiliensisGünter Gartler, Christoph Kratky, Karl Gruber
Angewandte Chemie (International Ed. in English)|October 10, 2001
Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase This work was supported by the Österreichische Akademie der Wissenschaften (APART fellowship 614), the Österreichische Fonds zur Förderung der wissenschaftlichen Forschung (FWF-project 11599), and the European Commission (TMR project number ERB 4061 PL 95-0307). Crystallographic data were collected at the EMBL-beamline BW7B at DESY in Hamburg, Germany. We thank the beamline scientists for their assistance, and Ingrid Dreveny, Günter Gartler, Gerwald Jogl, and Oliver Sauer for their help during data collection. This research emerged from a collaboration with Prof. W. Buckel (Marburg) who supplied us with clones of the glutamate mutase proteinsKarl Gruber, Riikka Reitzer, Christoph Kratky
Protein Science : a Publication of the Protein Society|January 16, 2002
The active site of hydroxynitrile lyase from Prunus amygdalus: modeling studies provide new insights into the mechanism of cyanogenesisIngrid Dreveny, Christoph Kratky, Karl Gruber
Chemistry (Weinheim an Der Bergstrasse, Germany)|November 24, 2005
Stabilisation of methylene radicals by cob(II)alamin in coenzyme B12 dependent mutasesWolfgang Buckel, Christoph Kratky, Bernard T Golding
The Journal of Biological Chemistry|June 6, 2008
Atomic resolution crystal structures and quantum chemistry meet to reveal subtleties of hydroxynitrile lyase catalysisAndrea Schmidt, Karl Gruber, Christoph Kratky, et al.
Angewandte Chemie (International Ed. in English)|February 16, 2005
B12-retro-riboswitches: constitutional switching of B12 coenzymes induced by nucleotidesSigrid Gschösser, Karl Gruber, Christoph Kratky, et al.
Angewandte Chemie (Weinheim an Der Bergstrasse, Germany)|March 20, 2024
Structure-Based Demystification of Radical Catalysis by a Coenzyme B<sub>12</sub> Dependent Enzyme-Crystallographic Study of Glutamate Mutase with Cofactor HomologuesKarl Gruber, Vanessa Csitkovits, Andrzej Łyskowski, et al.
Pageof 3

Showing results (1-10 of 24) with videos related to

Sort By:
Pageof 3
Nature|August 30, 2013
A coordinated approach is key for open accessChristoph Kratky
Current Opinion in Chemical Biology|November 5, 2002
Coenzyme B(12) dependent glutamate mutaseKarl Gruber, Christoph Kratky
Progress in the Chemistry of Organic Natural Products|January 31, 2015
Structure elucidation of natural compounds by X-ray crystallographyUlrike Wagner, Christoph Kratky
Journal of Biotechnology|January 26, 2007
Structural determinants of the enantioselectivity of the hydroxynitrile lyase from Hevea brasiliensisGünter Gartler, Christoph Kratky, Karl Gruber
Angewandte Chemie (International Ed. in English)|October 10, 2001
Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase This work was supported by the Österreichische Akademie der Wissenschaften (APART fellowship 614), the Österreichische Fonds zur Förderung der wissenschaftlichen Forschung (FWF-project 11599), and the European Commission (TMR project number ERB 4061 PL 95-0307). Crystallographic data were collected at the EMBL-beamline BW7B at DESY in Hamburg, Germany. We thank the beamline scientists for their assistance, and Ingrid Dreveny, Günter Gartler, Gerwald Jogl, and Oliver Sauer for their help during data collection. This research emerged from a collaboration with Prof. W. Buckel (Marburg) who supplied us with clones of the glutamate mutase proteinsKarl Gruber, Riikka Reitzer, Christoph Kratky
Protein Science : a Publication of the Protein Society|January 16, 2002
The active site of hydroxynitrile lyase from Prunus amygdalus: modeling studies provide new insights into the mechanism of cyanogenesisIngrid Dreveny, Christoph Kratky, Karl Gruber
Chemistry (Weinheim an Der Bergstrasse, Germany)|November 24, 2005
Stabilisation of methylene radicals by cob(II)alamin in coenzyme B12 dependent mutasesWolfgang Buckel, Christoph Kratky, Bernard T Golding
The Journal of Biological Chemistry|June 6, 2008
Atomic resolution crystal structures and quantum chemistry meet to reveal subtleties of hydroxynitrile lyase catalysisAndrea Schmidt, Karl Gruber, Christoph Kratky, et al.
Angewandte Chemie (International Ed. in English)|February 16, 2005
B12-retro-riboswitches: constitutional switching of B12 coenzymes induced by nucleotidesSigrid Gschösser, Karl Gruber, Christoph Kratky, et al.
Angewandte Chemie (Weinheim an Der Bergstrasse, Germany)|March 20, 2024
Structure-Based Demystification of Radical Catalysis by a Coenzyme B<sub>12</sub> Dependent Enzyme-Crystallographic Study of Glutamate Mutase with Cofactor HomologuesKarl Gruber, Vanessa Csitkovits, Andrzej Łyskowski, et al.
Pageof 3