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. 2021 Jan 27;12:636. doi: 10.1038/s41467-020-20608-z

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© This is a U.S. government work and not under copyright protection in the U.S.; foreign copyright protection may apply 2021

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Fig. 5 — a 3D variability analysis²⁸ of cryo-EM reconstructions of Nsp15 apo-states. Frame 1 (gray) and frame 20 (blue) of a 20-frame set describing the motion by the first eigenvector of the cryo-EM reconstructions. Black outlines demarcate the unique views of the endoU domains and dotted arrows demarcate regions of conformational heterogeneity. b Superposition of rigid-body docked models of the Nsp15 hexamer into the Apo Nsp15 H235A (dataset ii) reconstructions derived from 3D variability analysis. c View of the individual P1 protomer from (b) illustrating the conformational dynamics of the endoU domain. The linker between the endoU and MD is colored in gray.