English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Book Chapter

Crystallization and Structure of the Photosynthetic Reaction Centres from Rhodobacter sphaeroides - wild type and mutants

MPS-Authors
/persons/resource/persons137659

Fritzsch,  Günter
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137648

Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons252023

Merckel,  Michael C.
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 Resource
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

Fritzsch, G., Ermler, U., Merckel, M. C., & Michel, H. (1996). Crystallization and Structure of the Photosynthetic Reaction Centres from Rhodobacter sphaeroides - wild type and mutants. In M.-E. Michel-Beyerle (Ed.), The Reaction Center of Photosynthetic Bacteria (pp. 3-13). Berlin, Heidelberg: Springer.


Cite as: http://hdl.handle.net/21.11116/0000-0007-5C80-1
Abstract
Trigonal crystals of the photosynthetic reaction centres from the purple bacterium Rhodobacter sphaeroides have been grown with potassium phosphate as precipitant. These crystals diffract to 2.6 Å and are suitable for a detailed structure determination. The cofactor binding is similar to that observed in the reaction centres of Rhodopseudomonas viridis. A 23 Å long water chain connects the secondary quinone QB with the cytoplasm. The structures of the mutants Thr M222 → Val, Trp M252 → Phe, and Trp M252 → Tyr show minor differences compared with the wild type. In the carotenoidless strain R26 the carotenoid-binding site is occupied by a detergent molecule.