Extended Data Fig. 4: Global and local resolution of cryo-EM reconstructions. | Nature

Extended Data Fig. 4: Global and local resolution of cryo-EM reconstructions.

From: Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function

Extended Data Fig. 4

Related to Figs. 1–3. a, Example micrograph reveals preferred orientation of nucleosomes. Scale bar, 20 nm. b, FSC plots for five reported reconstructions. c, Local resolution distribution. In some maps, the resolution varies from 3 Å (dark blue) through 4 Å (green) to 6 Å (red). The lower resolution of some DNA regions indicates flexibility. d, Angular distribution plots. Scale shows the number of particles assigned to a particular angle. Blue, a low number of particles; yellow, a high number of particles. e, Directional FSC plots for the reconstructions calculated on the 3DFSC server48. Sphericity, as the degree of anisotropy present in the reconstructions, is indicated above each plot. Histograms indicate the portion of voxels with a particular resolution. f, Visualization of different regions of the nucleosome–SOX11 map. In the nucleosome core, histone side chains are clearly visible; SOX density has a lower resolution, but helical densities are clearly distinguishable. g, Rigid-body fit of the SOX2–DNA structure (PDB code 1O4X) into the nucleosome–SOX2 cryo-EM map (left). Rigid-body fit of the SOX11–DNA X-ray structure into the nucleosome–SOX11 cryo-EM map (right). The region containing SOX and a short DNA stretch was isolated from the rest of the map for clarity.

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