Electroneutral and electrogenic catalysis by dihaem-containing 
succinate:quinone oxidoreductases

Lancaster, C. Roy D.; Herzog, Elena; Juhnke, Hanno D.; Madej, Gregor M.; Müller, Florian G.; Paul, Rajsekhar; Schleidt, Philip G.

doi:10.1042/BST0360996

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Electroneutral and electrogenic catalysis by dihaem-containing succinate:quinone oxidoreductases

MPG-Autoren

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Lancaster, C. Roy D.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Cluster of Excellence “Macromolecular Complexes”, Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, 60438 Frankfurt am Main, Germany;
Chair of Structural Biology, Saarland University, Faculty of Medicine, 66421 Homburg, Germany;

/persons/resource/persons137704

Herzog, Elena
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Cluster of Excellence “Macromolecular Complexes”, Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, 60438 Frankfurt am Main, Germany;

/persons/resource/persons137726

Juhnke, Hanno D.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Cluster of Excellence “Macromolecular Complexes”, Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, 60438 Frankfurt am Main, Germany;

/persons/resource/persons137785

Madej, Gregor M.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Cluster of Excellence “Macromolecular Complexes”, Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, 60438 Frankfurt am Main, Germany;

/persons/resource/persons137816

Müller, Florian G.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Cluster of Excellence “Macromolecular Complexes”, Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, 60438 Frankfurt am Main, Germany;

/persons/resource/persons137830

Paul, Rajsekhar
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Cluster of Excellence “Macromolecular Complexes”, Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, 60438 Frankfurt am Main, Germany;

/persons/resource/persons137881

Schleidt, Philip G.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Cluster of Excellence “Macromolecular Complexes”, Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, 60438 Frankfurt am Main, Germany;

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Zitation

Lancaster, C. R. D., Herzog, E., Juhnke, H. D., Madej, G. M., Müller, F. G., Paul, R., et al. (2008). Electroneutral and electrogenic catalysis by dihaem-containing succinate:quinone oxidoreductases. Biochemical Society Transactions, 36(5), 996-1000. doi:10.1042/BST0360996.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-D82D-E

Zusammenfassung

X-ray structures of three different membrane proteins in complex with antibody fragments have been published. The binding of Fv or Fab fragments enlarges the hydrophilic part of integral membrane proteins, thereby providing additional surface for crystal contacts and space for the detergent micelle. In all reported cases, antibody binding was either essential for the crystallisation of the membrane protein or it substantially improved the diffraction quality of the crystals. Antibody-fragment-mediated crystallisation appears to be a valuable tool in particular for membrane proteins with very small hydrophilic or flexible domains.