Extended Data Fig. 6: Electron microscopy density map of Ripr in the ternary complex, and orientation of the Rh5–CyRPA–Ripr complex on the erythrocyte membrane.

a, Density map corresponding to Ripr (yellow) and CyRPA (red), showing several β-sheets in Ripr. b, Secondary structure prediction using the Phyre2 server indicated that two putative high-confidence α-helices (in dashed rectangles) reside in the N terminus of Ripr²³. c, The cryo-EM structure of Rh5–CyRPA–Ripr overlaid with the crystal structure of the Rh5–basigin (BSG) complex. The overlaid structures suggest the Rh5–CyRPA–Ripr complex is positioned parallel to the erythrocyte membrane before insertion. The crystal structures of CyRPA–C12, CyRPA–8A7 and Rh5–9AD4 antigen–antibodies complexes were also overlaid with the Rh5–CyRPA–Ripr cryo-EM structure. The overlaid structures suggest these monoclonal antibodies function to inhibit the docking of the invasion complex to the erythrocyte membrane. d, The crystal structure of the N-terminal domain of SipB is superimposed with the C-terminal helical bundles of Rh5. Over 144 residues of SipB were aligned with Rh5 C terminus, with a root mean square deviation of 3.4 Å. e, The Rh5 C-terminal helical bundle containing the α4–α7 helices is shown in cartoon and surface representation. Hydrophobic residues lining one side of the helical bundle are coloured in red, whereas hydrophilic residues lining the opposite side of the helical bundle are coloured in blue.