Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Buchkapitel

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

MPG-Autoren
/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;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

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.


Zitierlink: https://hdl.handle.net/21.11116/0000-0007-5C80-1
Zusammenfassung
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.