Fig. 1: Cryo-EM structures of the L1 αSyn fibrils.
a Sequence and secondary structure of human αSyn. Familial PD mutation sites (black arrow) localized within the lipid binding N-terminal region (residues 1–60)64. Green-colored residues bind to the lipid acyl chain, blue to the choline moiety20, and gray were not resolved. b–d Cryo-EM structures of L1A (b), L1B (c), and L1C (d) fibrils (protofilaments colored differently). The atomic models are shown as sticks. Labels denote the fibril width, the helical twist and rise, and residue numbers. The density maps in the lower panels are displayed using the carve feature in PyMOL at a distance of 2 Å. e Backbone of the L1 fibrils with the β1–β10 colored magenta and loops in gray. f–h Overlay of a sharpened high-resolution map shown in magenta (f), purple (g), and brown (h) and an unsharpened, 4.5 Å low-pass filtered density in gray. The backbone is shown as a black ribbon. Densities highlighted with a yellow background are reminiscent of lipid micelles.
