The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis

1989 ◽  
Vol 9 (4) ◽  
pp. 383-419 ◽  
Author(s):  
Johann Deisenhofer ◽  
Harmut Michel
Keyword(s):  
Membrane Protein ◽  
Protein Crystallization ◽  
Purple Bacterium ◽  
Membrane Protein Structure ◽  
Reaction Centre ◽  
Photosynthetic Membrane ◽  
Rhodopseudomonas Viridis ◽  
Membrane Protein Complex ◽  
Membrane Protein Crystallization ◽  
Photosynthetic Reaction Centre

We first describe the history and methods of membrane protein crystallization, and show how the structure of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis was solved. The structure of this membrane protein complex is correlated with its function as a light-driven electron pump across the photosynthetic membrane. Finally we draw conclusions on the structure of the photosystem II reaction centre from plants and discuss the aspects of membrane protein structure.

The Photosynthetic Reaction Centre from the Purple Bacterium Rhodopseudomonasviridis

2004 ◽  
Vol 24 (4-5) ◽  
pp. 323-361 ◽  
Author(s):  
Johann Deisenhofer ◽  
Harmut Michel
Keyword(s):  
Photosystem Ii ◽  
Membrane Protein ◽  
Protein Crystallization ◽  
Purple Bacterium ◽  
Membrane Protein Structure ◽  
Reaction Centre ◽  
Photosynthetic Membrane ◽  
Membrane Protein Complex ◽  
Membrane Protein Crystallization ◽  
Photosynthetic Reaction Centre

We first describe the history and methods of membrane protein crystallization, and show how the structure of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis was solved. The structure of this membrane protein complex is correlated with its function as a light-driven electron pump across the photosynthetic membrane. Finally we draw conclusions on the structure of the photosystem II reaction centre from plants and discuss the aspects of membrane protein structure.

scholarly journals Self-interaction chromatography as a tool for optimizing conditions for membrane protein crystallization

2009 ◽  
Vol 66 (1) ◽  
pp. 44-50 ◽  
Author(s):  
Mads Gabrielsen ◽  
Lisa A. Nagy ◽  
Lawrence J. DeLucas ◽  
Richard J. Cogdell
Keyword(s):  
Membrane Protein ◽  
Virial Coefficient ◽  
Protein Crystallization ◽  
Second Virial Coefficient ◽  
Rapid Screening ◽  
Reaction Centre ◽  
Core Complex ◽  
Light Harvesting Complex ◽  
Membrane Protein Crystallization ◽  
Crystallization Conditions

The second virial coefficient, orBvalue, is a measurement of how well a protein interacts with itself in solution. These interactions can lead to protein crystallization or precipitation, depending on their strength, with a narrow range ofBvalues (the `crystallization slot') being known to promote crystallization. A convenient method of determining theBvalue is by self-interaction chromatography. This paper describes how the light-harvesting complex 1–reaction centre core complex fromAllochromatium vinosumyielded single straight-edged crystals after iterative cycles of self-interaction chromatography and crystallization. This process allowed the rapid screening of small molecules and detergents as crystallization additives. Here, a description is given of how self-interaction chromatography has been utilized to improve the crystallization conditions of a membrane protein.

scholarly journals Amino acid sequence of the cytochrome subunit of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis

1987 ◽  
Vol 6 (8) ◽  
pp. 2197-2202 ◽  
Author(s):  
K. A. Weyer ◽  
F. Lottspeich ◽  
H. Gruenberg ◽  
F. Lang ◽  
D. Oesterhelt ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Purple Bacterium ◽  
Reaction Centre ◽  
Rhodopseudomonas Viridis ◽  
Photosynthetic Reaction Centre

Sequence Analysis of Mutants from Rhodopseudomonas viridis Resistant to the Herbicide Terbutryn

1987 ◽  
Vol 42 (6) ◽  
pp. 751-754 ◽  
Author(s):  
I. Sinning ◽  
H. Michel
Keyword(s):  
Sequence Analysis ◽  
Binding Site ◽  
Sequence Data ◽  
Purple Bacterium ◽  
Reaction Centre ◽  
Rhodopseudomonas Viridis ◽  
Dna Coding ◽  
Herbicide Binding ◽  
Mutant Strains ◽  
Photosynthetic Reaction Centre

Several mutants resistant to terbutryn (2-thiom ethyl-4-ethylamino-6-t-butylamino-s-triazine) from the purple bacterium Rhodopseudom onas viridis have been isolated. The sequence analysis of that part of the DNA coding for the herbicide binding site in the photosynthetic reaction centre showed that only two genetically different mutant strains were obtained. The sequence data are discussed with respect to recent crystallographic results.

The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis — An overview and recent advances

1990 ◽  
Vol 1018 (2-3) ◽  
pp. 115-118 ◽  
Author(s):  
Hartmut Michel ◽  
Irmgard Sinning ◽  
Juergen Koepke ◽  
Gunther Ewald ◽  
Günter Fritzsch
Keyword(s):  
Purple Bacterium ◽  
Reaction Centre ◽  
Rhodopseudomonas Viridis ◽  
Recent Advances ◽  
Photosynthetic Reaction Centre

Structural analysis of the photosynthetic membrane from Ectothiorhodospira halochloris

1983 ◽  
Vol 41 ◽  
pp. 740-741
Author(s):  
H. Engelhardt ◽  
R. Guckenberger ◽  
W. Baumeister
Keyword(s):  
Lattice Structure ◽  
Bacterial Species ◽  
Hexagonal Lattice ◽  
Reaction Centre ◽  
Photosynthetic Membrane ◽  
Rhodopseudomonas Viridis ◽  
Photosynthetic Membranes ◽  
Ectothiorhodospira Halochloris ◽  
Main Components

Bacterial photosynthetic membranes contain, apart from lipids and electron transport components, reaction centre (RC) and light harvesting (LH) polypeptides as the main components. The RC-LH complexes in Rhodopseudomonas viridis membranes are known since quite seme time to form a hexagonal lattice structure in vivo; hence this membrane attracted the particular attention of electron microscopists. Contrary to previous claims in the literature we found, however, that 2-D periodically organized photosynthetic membranes are not a unique feature of Rhodopseudomonas viridis. At least five bacterial species, all bacteriophyll b - containing, possess membranes with the RC-LH complexes regularly arrayed. All these membranes appear to have a similar lattice structure and fine-morphology. The lattice spacings of the Ectothiorhodospira haloohloris, Ectothiorhodospira abdelmalekii and Rhodopseudomonas viridis membranes are close to 13 nm, those of Thiocapsa pfennigii and Rhodopseudomonas sulfoviridis are slightly smaller (∼12.5 nm).

Phase Behavior of a Designed Cyclopropyl Analogue of Monoolein: Implications for Low-Temperature Membrane Protein Crystallization

2014 ◽  
Vol 127 (3) ◽  
pp. 1041-1045 ◽  
Author(s):  
Livia Salvati Manni ◽  
Alexandru Zabara ◽  
Yazmin M. Osornio ◽  
Jendrik Schöppe ◽  
Alexander Batyuk ◽  
...  
Keyword(s):  
Low Temperature ◽  
Membrane Protein ◽  
Phase Behavior ◽  
Protein Crystallization ◽  
Membrane Protein Crystallization
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