Extended Data Fig. 2: Additional analysis of helically symmetric ADP–F-actin and ADP-Pi–F-actin models.
From: Bending forces and nucleotide state jointly regulate F-actin structure
a, Example cryo-EM map density superimposed with atomic model residues A131–A135 from ADP–F-actin (top) and ADP–Pi-F-actin (bottom). b, Individual ADP–F-actin protomer shown in Cα representation, coloured by per-residue RMSD between ADP–F-actin and ADP-Pi–F-actin. c, Same as b, but coloured by per-residue strain pseudo-energy. d, Superposition of extended 31-protomer ADP- (blue) and ADP-Pi-F-actin (orange) models, aligned at the terminal barbed end protomer. e, Water molecules (violet) contained within the ADP-Pi–F-actin filament’s core. Actin subunits are shown in transparent grey backbone representation. PE: pointed end; BE: barbed end.
