English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase

MPS-Authors
/persons/resource/persons249431

Ostermeier,  Christian
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons249429

Iwata,  So
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137800

Michel,  Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Ostermeier, C., Iwata, S., Ludwig, B., & Michel, H. (1995). Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Nature Structural and Molecular Biology, 2(10), 842-846. doi:10.1038/nsb1095-842.


Cite as: http://hdl.handle.net/21.11116/0000-0006-FC2C-E
Abstract
Crystallization of membrane proteins, a prerequisite for their X-ray crystallographic analysis, remains difficult. Here, we demonstrate that the crystallization of the cytochrome c oxidase from Paracoccus denitrificans can be mediated by co-crystallization with an antibody Fv fragment. The crystals obtained contain all four subunits of this membrane protein complex and the Fv fragment. The approach of co-crystallizing membrane proteins with antibody fragments should be useful in obtaining well-ordered crystals of membrane proteins in general.