Supplementary Figure 3: Eight unique fibril morphologies are observed in the 247DLIIKGISVHI257 cryo-EM sample.
From: Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2
(a) Negative stain EM image of the 247DLIIKGISVHI257 cryo-EM sample. 247DLIIKGISVHI257 fibrils were grown by shaking for one week at 1mM in water. Sample was stained with 2% uranyl acetate and visualized on the FEI T12 transmission electron microscope. Fibril samples illustrate multiple morphologies, including twisted helical assemblies. (b) Illustration of the eight different types of fibrils observed by cryo-EM. The eight fibrils demonstrate four different conformations of amyloid fibrils: helices, twists, cylinders, and sheets. (c) The relative abundance of the eight unique fibrils are displayed in a table. The 3-start helix represents the most abundant species, comprising approximately 60% of the sample.
