Fig. 2: Overview of all murine Aβ fibril structures.
a, Amino acid sequence of Aβ42. The sequence contains the following mutations for tg-SwDI: E22Q and D23N; and for tg-APPArcSwe: E22G. Solid lines indicate the part of the sequence for which atomic model building was possible (accordingly, dotted lines represent parts of the sequence that were not modeled). Arrows indicate β-strands. b–j, Each panel shows the reconstructed cryo-EM density along the helical axis with a close-up and a label denoting the helical twist (left); the cryo-EM density map (in transparent gray) with the corresponding atomic model (top right); a schematic of the fold, produced with atom2svg.py60 (red, acidic side chain; blue, basic side chain; green, hydrophilic side chain; white, hydrophobic side chain; pink, glycine; yellow, sulfur-containing) (bottom right). Cryo-EM structure of murine type III Aβ42 fibrils from APP/PS1 mouse brain (b), murine type III Aβ fibrils from ARTE10 mouse brain (c), type II Aβ42 fibrils from ARTE10 mouse brain (d), DI1 Aβ fibrils from tg-SwDI mouse brain (e), DI2 Aβ fibrils from tg-SwDI mouse brain (f), DI3 Aβ fibrils from tg-SwDI mouse brain (g), type II Aβ42 fibrils from tg-APPSwe mouse brain (h), type II Aβ42 fibrils from APP23 mouse brain (i) and murineArc type I fibrils from tg-APPArcSwe mouse brain (j). For f and g (DI2 and DI3 fibrils from tg-SwDI mouse brain), the displayed atomic models have limited accuracy owing to the medium resolution.
