Two-dimensional crystallization and preliminary structure analysis of light harvesting II (B800-850) complex from the purple bacterium Rhodovulum sulfidophilum.
Light-harvesting complex II (B800/850) from the purple bacterium Rhodovulum (Rhv.) sulfidophilum has been isolated using a new protocol. It has been shown by analytical ultracentrifugation and native gels to be most likely an octamer. Two-dimensional crystals have been obtained by microdialysis. The plane group is p4212 with a = b = 157 A. The crystals diffract to 18 A in negative stain. Projection maps show clearly that LHII is organized in ring-like particles with an outer diameter of about 76 A.
Montoya
G
G
European Molecular Biology Laboratory, Heidelberg, Germany.
Cyrklaff
M
M
Sinning
I
I
D001419:Bacteria / Q000737:chemistry*; D001426:Bacterial Proteins; D003460:Crystallization; D007091:Image Processing, Computer-Assisted; D045342:Light-Harvesting Protein Complexes; D017551:Microdialysis; D008854:Microscopy, Electron; D015394:Molecular Structure; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; C081485:light-harvesting protein complex II, Rhodobacter capsulatus