Abstract
The photosynthetic reaction center (RC) from Rhodopseudomonas viridis (R. viridis) was one of the first integral membrane proteins which could be crystallized (Michel, 1982). The crystals turned out to be suitable for X-ray structure analysis at atomic resolution. In a study at 3A resolution, using phases determined from multiple isomorphous replacement experiments with heavy atom compounds, the arrangement of the major prosthetic groups (Deisenhofer et al., 1984), and the folding of the protein subunits (Deisenhofer et al., 1985) were determined. Sequencing of the RC’s protein subunits (Michel et al., 1985; Michel et al., 1986a; Weyer et al., 1987) facilitated interpretation of the electron density map and model building; information from X-ray diffraction and from sequencing together allowed a detailed description of pigment-protein interactions in the RC (Michel et al., 1986b).
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References
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© 1988 Springer Science+Business Media New York
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Deisenhofer, J., Michel, H. (1988). The Crystal Structure of the Photosynthetic Reaction Center from Rhodopseudomonas viridis . In: Breton, J., Verméglio, A. (eds) The Photosynthetic Bacterial Reaction Center. NATO ASI Series, vol 149. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0815-5_1
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DOI: https://doi.org/10.1007/978-1-4899-0815-5_1
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