Extended Data Fig. 3: Cryo-EM reconstructions and atomic models.
From: Heteromeric amyloid filaments of ANXA11 and TDP-43 in FTLD-TDP type C
a, Cryo-EM reconstructions of filaments from FTLD-TDP Type C individual 1 with two alternative conformations of the TDP-43 glycine-rich region (indicated with arrows), shown as central slices perpendicular to the helical axis. The resolution of each reconstruction is indicated. Scale bars, 2 nm. b, Fourier shell correlation (FSC) curves for the two independently-refined cryo-EM half-maps (black lines); for the refined atomic model against the cryo-EM density map (magenta); for the atomic model shaken and refined using the first half-map against the first half-map (cyan); and for the same atomic model against the second half-map (yellow). FSC thresholds of 0.143 (black dashed line) and 0.5 (magenta dashed line) are shown. c, Local resolution estimates for the cryo-EM reconstructions. d, Cryo-EM reconstructions viewed along the helical axis. Scale bar, 1 nm. e,f, Views of the cryo-EM reconstructions and atomic models showing representative densities for ordered solvent (red arrows) (e) and main chain oxygen atoms in β-strands (f), which reveal the chirality of the map.
