Fig. 3: 3DFlex applied to the TRPV1 dataset, demonstrating the capacity for 3DFlex to resolve motion of smaller, membrane proteins.
From: 3DFlex: determining structure and motion of flexible proteins from cryo-EM
See Supplementary Videos 2 and 3. a, Scatter plots showing the distribution of learned particle latent coordinates. b, Convected densities from 3DFlex at minus one (red) and plus one (blue) standard deviations along each of the two dimensions in the latent space. The first reveals a motion where opposite soluble domains move together or apart. The second reveals motion of all four soluble domains twisting around the axis of the central pore. c, Density maps from conventional nonuniform refinement (left) and the 3DFlex canonical map, both colored by local resolution on the same scale. Both are filtered and sharpened identically, and displayed at the same threshold level. d,e, Detailed views from top (d) and side (e) showing helical density in the flexible soluble domains. f,g, FSC curves are measured between half-map reconstructions from disjoint half-sets of particles and during training experimental data only up to 4.3 Å resolution is used (DC denotes constant signal). f, FSC of the entire map. g,h, FSC of the flexible peripheral domain (mask shown in h) including FSC curve (red) for local rigid refinement using the same mask (g).
