The three-dimensional structure of the photosynthetic reaction center from Rhodobacter sphaeroides is described. The reaction center is a transmembrane protein that converts light into chemical energy. The protein has three subunits: L, M, and H. The mostly helical L and M subunits provide the scaffolding and the finely tuned environment in which the chromophores carry out electron transfer. The details of the protein-chromophore interactions are from studies of a trigonal crystal form that diffracted to 2.65-A resolution. Functional studies of the multi-subunit complex by site-specific replacement of key amino acid residues are summarized in the context of the molecular structure
AbstractThe molecular replacement method has been succesfully used to provide a structure for the ph...
doi:10.1016/j.jmb.2007.04.082Introduction The bacterial photosynthetic reaction center (RC) is a mem...
Photosynthetic reaction centers from anoxygenic bacteria are the best-characterized membrane protein...
The three-dimensional structure of the photosynthetic reaction center fromRhodobacter sphaeroides is...
Photosynthetic reaction centers from purple bacteria exhibit an approximate twofold symmetry axis, w...
The three-dimensional structure of the protein subunits of the reaction center (RC) of Rhodobacter s...
The energetics of membrane-protein interactions are analyzed with the three-dimensional model of the...
Photosynthetic reaction centers from purple bacteria exhibit an approximate twofold symmetry axis, w...
Photosynthetic reaction centers from purple bacteria exhibit an approximate twofold symmetry axis, w...
The energetics of membrane-protein interactions are analyzed with the three-dimensional model of the...
The molecular structure of the photosynthetic reaction centre from Rhodopseudomonas viridis has been...
The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) f...
The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) f...
The photosynthetic reaction center (RC) of the bacterium Rhodobacter sphaeroides is a pigment-protei...
Rhodobacter sphaeroides is a model organism for the study of bacterial photosynthesis. The R. sphaer...
AbstractThe molecular replacement method has been succesfully used to provide a structure for the ph...
doi:10.1016/j.jmb.2007.04.082Introduction The bacterial photosynthetic reaction center (RC) is a mem...
Photosynthetic reaction centers from anoxygenic bacteria are the best-characterized membrane protein...
The three-dimensional structure of the photosynthetic reaction center fromRhodobacter sphaeroides is...
Photosynthetic reaction centers from purple bacteria exhibit an approximate twofold symmetry axis, w...
The three-dimensional structure of the protein subunits of the reaction center (RC) of Rhodobacter s...
The energetics of membrane-protein interactions are analyzed with the three-dimensional model of the...
Photosynthetic reaction centers from purple bacteria exhibit an approximate twofold symmetry axis, w...
Photosynthetic reaction centers from purple bacteria exhibit an approximate twofold symmetry axis, w...
The energetics of membrane-protein interactions are analyzed with the three-dimensional model of the...
The molecular structure of the photosynthetic reaction centre from Rhodopseudomonas viridis has been...
The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) f...
The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) f...
The photosynthetic reaction center (RC) of the bacterium Rhodobacter sphaeroides is a pigment-protei...
Rhodobacter sphaeroides is a model organism for the study of bacterial photosynthesis. The R. sphaer...
AbstractThe molecular replacement method has been succesfully used to provide a structure for the ph...
doi:10.1016/j.jmb.2007.04.082Introduction The bacterial photosynthetic reaction center (RC) is a mem...
Photosynthetic reaction centers from anoxygenic bacteria are the best-characterized membrane protein...