Fig. 1: Fibril formation and stability of αA-crystallin fibrils. | Communications Chemistry

Fig. 1: Fibril formation and stability of αA-crystallin fibrils.

From: Cryo-EM structure of amyloid fibrils formed by full-length human αA-crystallin with pathogenic mutation R116C

Fig. 1

a Negative stain EM images of thick fibrils formed under neutral conditions (left) and the thin fibrils formed under acidic conditions (right). GdnHCl, guanidine hydrochloride; TFE, trifluoroethanol. Scale bar = 100 nm. b Negative stain EM images of αA-crystallin incubated in the same buffer of the thin fibrils with pH levels adjusted. c–d, f Negative stain EM images of the thin fibrils heated (c), incubated with pepsin (d), or diluted to buffers with indicated pH (f). e SDS-PAGE of samples filtered with 0.1 μm filters. re, retained fraction; ft, flowthrough fraction, -, no treatment; pep, incubated with pepsin; 75, heated to 75 °C; 100, heated to 100 °C. g ThT curves of αA-crystallin wild type (grey) and R116C (black). Data are shown as mean± s.d., n = 3 independent experiments. h, Negative stain EM image of fibrils formed by wild-type αA-crystallin.

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