Extended Data Figure 3  Intra- and Inter-filament Interactions
(a) The triangular structure seen in cross section. ‘Side 1’ of the triangular structure has the atomic model placed in the density. The G-domain-to-G-domain contact between adjacent sides is circled.
(b) The sum of the 3 sides with the model fit in density.
(c) Ribbon diagram of the same atomic model as in (b). The rotated view shows 8 chains each of DRP1 and MID49. The chains further from the reader are rendered transparent.
(d) An isolated tetramer of DRP1 from the filament, rendered to highlight the stalk interfaces 1, 2 and 3 observed for DRP1 and other dynamin-family of GTPases.
(e) Expanded view of the circular region in (a) illustrating a salt bridge between adjacent G-domains.
(f) DRP1-only wild type polymers with GMPPCP versus (g) DRP1 coassembly with wild type MID49126-454 and GMPPCP and high-magnification inset.
(h) DRP1E116R mutant polymers versus (i) DRP1E116R mutant coassembly with MiD49126-454. Shorter, single-sided filaments predominate. Disordered “triangular assemblies” were also observed, but were much shorter and infrequent compared with the wild type proteins. Bars = 50nm.
E