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Two-dimensional crystallization of the l ... plex from Rhodospirillum rubrum
Two-dimensional crystallization of the light-harvesting complex from Rhodospirillum rubrum.
18
Homogeneous detergent-solubilized B873 light-harvesting complexes from a carotenoid-less mutant of the purple non-sulfur bacterium, Rhodospirillum rubrum G9, were reassembled spontaneously into two-dimensional (2D) hexagonal arrays during extensive and controlled dialysis. As the complexes contain only 1 to 2 mol phospholipid per mol alpha beta dimer, the arrays formed by a self assembly process are primary due to protein-protein interactions. The hexagonal lattices were analyzed by negative stain electron microscopy and digital image processing. They exhibited a unit cell size of 12.3 nm, in close agreement with the particle diameter of the active photo-unit in native chromatophore membranes. The unit cell contains a central 5 nm stain-filled depression, embraced by a ring with an outer diameter of 10 nm.
Ghosh R, Hoenger A, Hardmeyer A, Mihailescu D, Bachofen R, Engel A, Rosenbusch JP
Journal of molecular biology
1993-05-20 00:00
231
2
501-4
Crystallization,Image Enhancement,Microscopy, Electron,Negative Staining,Photosynthetic Reaction Center Complex Proteins,Rhodospirillum,Photosynthetic Reaction Center Complex Proteins
Department of Microbiology, University of Basel, Switzerland
J. Mol. Biol.
0022-2836
10.1006/jmbi.1993.1298
S0022-2836(83)71298-2
582
True
8510160
