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. Author manuscript; available in PMC: 2021 Jan 13.
Published in final edited form as: Nat Plants. 2018 Oct 29;4(11):904–909. doi: 10.1038/s41477-018-0271-1

Fig. 3 |. The supramolecular organization of Pp-PSI-L observed by single-particle cryo-electron microscopy analysis.

Fig. 3 |

a,b, 3D reconstruction and docking of Pp-PSI-L in the top (left) and side views (right panels). Scale bar for a and b, 50 Å. c, Fitted crystal structures showing the detailed organization of the extended LHCI antenna with respect to the PSI complex (dotted line contour). Lhca1–4 from the plant PSI crystal structure (5L8R) were split into two distinct rigid body dimers (Lhca1–4 as dimer 1 in red and Lhca2–3 as dimer 2 in orange) to be fitted into the additional LHCI belt density of Pp-PSI-L. It should be noted, however, that the orthologue of A. thaliana Lhca4 is missing in P. patens. Thus, the location for Lhca4 is replaced by another yet unidentified LHCI protein. In addition to the second belt, an LHCII-like trimer contacts PsaA, K and L, and the putative Lhcb9 central to the antenna. See Supplementary Fig. 8 for putative components of the unassigned density in Pp-PSI-L.