Fig. 6: Structural characterization of the molecular mace density map. | Communications Biology

Fig. 6: Structural characterization of the molecular mace density map.

From: Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects

Fig. 6

a A representation of four α-Syn chains arranged as per the Greek-key architecture (PDB 2N0A) in cartoon representation (blue) inside the semi-transparent surface. Only the structured part (residue 37–99) is shown and the unstructured regions (residues 1–36 and 100–140, shown below) are not included in the structure. b The full structure shown in figure A could not be fitted into the density map of oligomer1 as a rigid piece. The ‘head’ and ‘base’ parts of figure A was fitted separately (orange CPK sphere representations) into the density map of oligomer1 generated from oligomers1 (semi-transparent orange). c Superimposition of the Greek-key structure from panel a (in blue) and the fitted model from panel b (in orange) represented in spheres, shows distortion in the fitted model near its ‘head’–‘base’ junction.

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