X-ray structure analysis shows that the monomer of trimeric photosystem I (PS I) of Synechococcus sp. consists of a catalytic domain and a smaller domain that connects the monomers. The 4Fe-4S clusters FX,FA and FB, 28 α-helices and 45 chlorophyll a molecules were located. The two large subunits of PS I are represented by nine a-helices each; they are related by a local 2-fold rotation axis passing through Fx. Electron densities close to this axis are interpreted as carriers of the electron transfer chain.
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