Extended Data Fig. 5: Additional analysis of filament bending deformations.
From: Bending forces and nucleotide state jointly regulate F-actin structure
a, Helically symmetric ADP-Pi–F-actin (left map) and cryoDRGN reconstructions sampling ADP-Pi–F-actin bending (right three maps). Maps are lowpass filtered to 8 Å, and strands are coloured in shades of orange. PE: pointed end; BE: barbed end. Scale bar, 10 nm. b, Stitched volumes of straight and bent maps from a, aligned on the bottom 16 protomers. Scale bar, 100 nm. c, Projections of zeroth (cyan) and ninth (magenta) cryoDRGN reconstructions from ADP–F-actin (left) and ADP-Pi–F-actin (right) aligned on the bottom protomer and oriented to display maximum displacement. d, Asymmetric reconstructions of ADP–F-actin from indicated curvature bins. Scale bar, 10 nm. e, Plots of central axis deviations from straight lines in ADP–F-actin and ADP-Pi–F-actin cryoDRGN reconstructions. First and second columns show principal component analysis of the cryoDRGN reconstructions’ central axes. Third column shows displacement of the cryoDRGN reconstructions’ central axes from straight lines which were aligned to the barbed-end terminal 56 Å of the central axes. f, Half-map Fourier Shell Correlation (FSC) curves for control asymmetric 16-protomer reconstructions. g, Twist and rise measurements of control asymmetric 16-protomer reconstructions.
