Extended Data Fig. 1: Validation of ADP–Pi-F-actin preparation and helically symmetric reconstructions.
From: Bending forces and nucleotide state jointly regulate F-actin structure
a, Representative TIRF-microscopy video frames from cofilin severing assays. Cofilin-free controls are shown in the top row of each condition, indicated by a darker border. Scale bar, 40 μm. b, Quantification of TIRF videos showing the average normalized actin channel intensity. Error margin in graph indicates +/− 95% CI. Half-lives represent exponential decay at time 0 s, with 95% CI, and n values represent independent experiments: ADP–F-actin - cofilin (778 ± 24 s, n = 3); ADP-Pi–F-actin - cofilin (454 ± 14 s, n = 3); ADP-sulfate–F-actin - cofilin (348 ± 16 s, n = 3); ADP–F-actin + cofilin (50.4 ± 2.1 s, n = 4); ADP-Pi–F-actin + cofilin (177.5 ± 10.3 s, n = 3); ADP-sulfate–F-actin + cofilin (86.8 ± 2.5 s, n = 3). c, Half-map (left) and map-to-model (right) Fourier Shell Correlation (FSC) curves for helically symmetric reconstructions of ADP- and ADP-Pi-F-actin. d, Local resolution assessment of helically symmetric ADP–F-actin and ADP-Pi–F-actin. PE: pointed end; BE: barbed end. e, Potential hydrogen-bonding networks adjacent to the nucleosidyl region of ADP. Key side chains and back bone atoms participating in hydrogen-bonding networks are displayed and coloured by heteroatom.
