Fig. 2 | Nature Communications

Fig. 2

From: Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel

Fig. 2

Cryo-EM structures and atomic models of the aSyn rod and twister polymorphs. a The cryo-EM structures of the rod (left) and twister (right) polymorphs of the full-length aSyn fibrils shown as density slices (top inlet), as semitransparent surfaces overlaid with their atomic models viewed from two different angles (lower panels). The rod (blue) and twister (red) polymorphs contain two protofilaments composed of stacked β-sheets and packed by an approximate 21 screw axis of symmetry. Shown on the left and right sides are the 3D model of the rod and twister fibril polymorphs, respectively, with their distinctively different helical pitches depicted. b Model validation. Representative regions of density maps of both polymorphs are superimposed with their models showing match of side chain with cryo-EM densities. Intra-protofilament hydrogen bonds are shown in black dashed lines, and inter-protofilament hydrogen bonds are shown in magenta dashed lines. See details in Supplementary Figures 7 and 8

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