Fig. 3
From: Cryo-EM structures of tau filaments from the brains of mice transgenic for human mutant P301S Tau
Structure of P301S Tau filaments from the brainstem of Tg2541 mice. a, Cross-sections through the cryo-EM reconstructions, perpendicular to the helical axis and with a projected thickness of approximately one rung, are shown for the P301S Tau filaments from the brainstem of Tg2541 mice aged 8 weeks and 24 weeks. The cryo-EM map resolution (bottom left) and the percentages of a given filament type among the filaments in the datasets (top right) are shown. Scale bars, 5 nm. b, Sequence alignment of the microtubule-binding repeats (R1-R4) of Tau with the observed seven β-strand regions (β1-β7, arrows). Mutant serine residue at position 301 is highlighted in red. c, Sharpened high-resolution cryo-EM map of the P301S Tau filaments with the atomic model overlaid. Residues in R1-R4 and the C-terminal domain are coloured purple, blue, green, yellow and orange, respectively. Islands A and B are indicated in grey. d, Schematic of the Tg2541 Tau filament fold. Negatively charged residues are shown in red, positively charged residues in blue, polar residues in green, non-polar residues in white, sulphur-containing residues in yellow, prolines in purple and glycines in pink. Thick connecting lines with arrowheads indicate β-strands (β1-β7). Additional densities are shown in red. Unknown residues are indicated by question marks