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lüll Organization of transmembrane helices in photosystem II: comparison of plants and cyanobacteria Barber J; Nield JPhilos Trans R Soc Lond B Biol Sci 2002[Oct]; 357 (1426): 1329-35; discussion 1335, 1367Electron microscopy and X-ray crystallography are revealing the structure of photosystem II. Electron crystallography has yielded a 3D structure at sufficient resolution to identify subunit positioning and transmembrane organization of the reaction-centre core complex of spinach. Single-particle analyses are providing 3D structures of photosystem II-light-harvesting complex II supercomplexes that can be used to incorporate high-resolution structural data emerging from electron and X-ray crystallography. The positions of the chlorins and metal centres within photosystem II are now available. It can be concluded that photosystem II is a dimeric complex with the transmembrane helices of CP47/D2 proteins related to those of the CP43/D1 proteins by a twofold axis within each monomer. Further, both electron microscopy and X-ray analyses show that P(680) is not a 'special pair' and that cytochrome b559 is located on the D2 side of the reaction centres some distance from P(680). However, although comparison of the electron microscopy and X-ray models for spinach and Synechococcus elongatus show considerable similarities, there seem to be differences in the number and positioning of some small subunits.|Crystallography, X-Ray[MESH]|Cyanobacteria/*chemistry[MESH]|Dimerization[MESH]|Models, Molecular[MESH]|Photosynthetic Reaction Center Complex Proteins/*chemistry/ultrastructure[MESH]|Photosystem II Protein Complex[MESH]|Plants/*chemistry[MESH]|Protein Conformation[MESH] |