Electron micrographs of photosynthetic membranes of the BChla-containing bacterium Rp, marina showed a quasi-crystalline structure. The photoreceptor units are arranged in a hexagonal lattice with a reaction center to reaction center distance of 102± Å. Purified B880-complex was concentrated up to an OD? of 60 which induced the formation of large protein vesicles. The protein complexes within these vesicles were highly ordered and showed a hexagonal lattice with the same center to center distance of 102±3 Å as was observed in the native membranes. Image processing of the micrographs revealed a ring-like structure of the B880-complex at 26 Å resolution and suggests that the B880-complex consists of 5 or 6 subunits. For the first time it can be shown that an isolated core-complex is in a stable, ring-like structure even without the reaction center which is supposed to be located in the middle of the B880-ring. The data indicate that the isolated B880-complex exhibits the same structure as in the native membrane.
