Skip to main content
. Author manuscript; available in PMC: 2020 Aug 17.
Published in final edited form as: Nat Struct Mol Biol. 2020 Feb 17;27(3):233–239. doi: 10.1038/s41594-020-0379-7

Extended Data Fig. 2. Cryo-EM data processing and validation.

Extended Data Fig. 2

a, Following initial 2D classification, several iterations of 3D classification were conducted. Classes are presented as 3D volumes. Percentages of particles sorted into each class are displayed below. The selected final 3D class is boxed, and was proceeded by a further round of 2D classification prior to masked global consensus refinement. b, A representative micrograph is shown. c, Angular distribution plot of final 3D consensus refinement. d, Fourier shell correlation plot. Final overall resolution is 3.2 Å (when FSC=0.143). e, Local resolution of the EM density map (Å) as computed by ResMap. f, EM density and modelled residues corresponding to catalytic motifs of the CtSmc1 ATPase domain, and the coiled-coils (RMSD 2.5). g, EM density and modelled residues corresponding to catalytic motifs of the Smc3 ATPase domain, and the coiled-coils (RMSD 2.5).