Extended Data Fig. 5: Agreement of rPrP106–145 model with core density in rPrPRes. | Nature Structural & Molecular Biology

Extended Data Fig. 5: Agreement of rPrP106–145 model with core density in rPrPRes.

From: Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core

Extended Data Fig. 5

a, Fourier Shell Correlation (FSC) between half-maps (blue) and the map and model (green) with resolutions at FSC = 0.5 (black dotted line) and 0.143 (gray dotted line) noted. b, Agreement of turn region with density looking down the fibril axis and (c) a side view of the same region shows clear strand separation. d, Overall fit of model into density. e, Magnified view of protofilament interface showing spacing between backbones at the center of the interface is at the most tightly spaced region between G114 of one chain and G119 of its mate. f, Magnified view of linchpin region with inferred salt bridge between residues H111 and D144 that seal off the interior of each chain and a side view (g) of the same region showing 4.8 Å separation between strands.

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