Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution

Structures of the OmpF porin crystallized in the presence of foscholine‐12

“…The three proteins are highly homologous, with 62% sequence identity between OmpF and OmpE, and 58% between OmpF and OmpC (mature forms). OmpF and OmpE were among the first membrane protein structures determined, 1 following the determination of the photosynthetic reaction centers of Rhodospeudomonas viridis 2 and Rhodobacter sphaeroides, 3 and the porin from Rhodobacter capsulatus. 4 All general porin monomers form 16-stranded b-barrels that associate in tightly packed trimers.…”

Crystallization and X‐ray analysis of the reaction center from the thermophilic green bacterium Chloroflexus aurantiacus

“…Although crystallization of Cf aurantiacus RC can be achieved under various conditions in the presence of different detergents, it is still difficult to consistently obtain well-or- [2][3][4][5][6]. Consequently, the number of molecules per asymmetric unit cannot be deduced unequivocally.…”

“…viridis and Rb. sphaeroides have been crystallized and their structures elucidated at atomic resolution [2][3][4][5][6]. Most RCs are comprised of three protein subunits which are called H (heavy), M (medium) and L (light) according to their electrophoretic mobilities in SDS-PAGE.…”

“…viridis was the first membrane protein to be crystallized and its threedimensional structure to be solved at atomic resolution [2,13,14]. Subsequently, the structure of three-dimensional crystals of a few other membrane proteins have been determined [2,[4][5][6][15][16][17][18][19].…”

Crystallization of two integral membrane pigment–protein complexes from the purple‐sulfur bacterium Chromatium purpuratum

“…There have been numerous reports of crystallization of peripheral antenna complexes from a variety of purple-nonsulfur organisms Welte et al, 1985;Hawthornethwaite et al, 1989;Michel, 1990;Guthrie et al, 1992;Nunn et al, 1992). The crystal structure of the RC from Rhodopseudomonas viridis was the first integral membrane protein structure solved at atomic resolution (Deisenhofer et al, 1985) followed by the RC from Rhodobacter sphaeroides (Allen et al, 1986;Chang et al, 1986). These structures were quite similar to one another, making it unclear as to whether certain RC structural features that are conserved between the two organisms are the result of functional constraints or reflect a close evolutionary relationship.…”