Extended Data Fig. 4: Crosslinks between all OPA1 subunits in membrane-bound conformation.

a, b, Chemical cross-linking and mass spectrometry reveals protein-protein interaction (PPI) maps of the human S-OPA1 polymers. Circular plot showing the distribution of DSG (a) and DSS (b) chemical crosslinks mapped to human OPA1 represented as coloured circles with amino acid positions labelled. Orange bars indicate the positions of lysine residues, and crosslinks connecting the lysine residues are represented by black lines between the corresponding amino acid pairs. c, Crosslinks that are gained (red) in the S-OPA1 polymer upon membrane binding. Identified inter-molecular crosslinks are mapped on the S-OPA1 subunits. CX-MS reveals a cluster of contacts between S-OPA1 paddle domains, indicating strong interactions in membrane-bound conformation. d, Crosslinks between all OPA1 domains. Domains are arranged based on sequence (coloured blocks). The DSG (red) and DSS (blue) crosslinks that satisfy the distance restraint (30 Å) are mapped onto the membrane-bound cryo-EM structure of human S-OPA1. Crosslinks identified in both DSG and DSS datasets are shown in purple.