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• W2065784414 abstract "The determination of the structure of PSII at high resolution is required in order to fully understand its reaction mechanisms. Two-dimensional crystals of purified highly active Synechococcus elongatus PSII dimers were obtained by in vitro reconstitution. Images of these crystals were recorded by electron cryo-microscopy, and their analysis revealed they belong to the two-sided plane group p22121, with unit cell parameters a = 121 Å, b = 333 Å, and α = 90°. From these crystals, a projection map was calculated to a resolution of approximately 16 Å. The reliability of this projection map is confirmed by its close agreement with the recently presented three-dimensional model of the same complex obtained by X-ray crystallography. Comparison of the projection map of the Synechococcus elongatus PSII complex with data obtained by electron crystallography of the spinach PSII core dimer reveals a similar organization of the main transmembrane subunits. However, some differences in density distribution between the cyanobacterial and higher plant PSII complexes exist, especially in the outer region of the complex between CP43 and cytochrome b559 and adjacent to the B-helix of the D1 protein. These differences are discussed in terms of the number and organization of some of the PSII low molecular weight subunits." @default.
• W2065784414 created "2016-06-24" @default.
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• W2065784414 date "2002-03-27" @default.
• W2065784414 modified "2023-09-27" @default.
• W2065784414 title "Electron Crystallographic Study of Photosystem II of the Cyanobacterium <i>Synechococcus elongatus</i>" @default.
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• W2065784414 doi "https://doi.org/10.1021/bi0120650" @default.
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