Extended Data Figure 4: Cross-links identified within RyR1.
From: Architecture and conformational switch mechanism of the ryanodine receptor

a, b, Graphical representation (a) and table (b) summarizing cross-links identified in cross-linking mass spectrometry experiments. a, Schematic representation of RyR1 domains colour-coded similar to domains in Fig. 1. The repeat 3–4 and EF-hand domains are shown as inserts into the α-solenoid 1.1 and α-solenoid 1.2 domains, respectively. The cross-links are shown by red lines. The approximate length of linkers joining domains is indicated by ‘Δ’ followed by the number of residues. Disordered regions of linking fragments are shown as fat dotted lines and their positions in the amino acid sequence are indicated. Domains containing β-sheets are depicted as circles, α-helical domains are shown as squares. b, Cross-linked residues are shown with ID score and their distances in the built model (see Supplementary Table 1 for complete list of identified cross-links).