Extended Data Fig. 5: Cryo-EM densities of CyRPA in the binary complex and Rh5 in the ternary complex

a, Electron microscopy density showing the top view of the CyRPA β-propeller (left), and a cross-section of the same region showing the resolution of the 6-bladed β-sheets of CyRPA (right). b, Density of β-strands resolved in blades 1, 3 and 6 of the CyRPA β-propeller. c, Electron microscopy densities showing the individual α-helices (α2–α7) of Rh5. d, Model showing α7 helix of Rh5 inserted into the central cavity of CyRPA. e, Hydrophobic residues (L393, L397, F494 and I498) form a groove of Rh5, in contact with aromatic residues (Y185, F187 and F226) presented by B4 and B4–B5 loops of CyRPA. f, Models showing the hydrophobic groove of Rh5 and the binding aromatic residues of CyRPA (Y185, F187 and F226), shown in orange. g, Density maps and the refined atomic models showing the disordered B5 loop in CyRPA upon binding of Rh5 (left), the corresponding region showing the ordered B5 loop in CyRPA in the absence of Rh5 (middle) and the two superimposed blade 5 β-sheets of CyRPA in the absence (blue) and presence (red) of Rh5 (right). h, Tandem mass spectra of DSS cross-linked peptides identified from tryptic digestion of gel-purified Rh5–CyRPA–Ripr complex. High-resolution spectra from Q-Exactive mass spectrometer for two cross-linked peptides between Rh5(520–526) and CyRPA(37–50). Experiments were repeated three times with biologically independent samples, and were reproducible.