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. 2020 Jul 31;28(1):251–266. doi: 10.1038/s41418-020-0598-9

Fig. 2. EM and AFM analysis of M45–RHIM and RIP3–RHIM amyloid fibrils.

Fig. 2

a Negative-stained EM images of RIP3 fibrils (left) and M45 fibrils (right). The amyloid fibrils assembled from 0.1 mg/ml human RIP3 (418–518 aa) or 0.2 mg/ml M45 (52–71 aa) as described in “Materials and Methods” (scale bar 100 nm). b The X-ray diffraction images of RIP3 fibrils (left) and M45 fibrils (right). The arrow indicated equatorial and meridional reflection of a cross-β-sheet structure arrangement. For RIP3 fibrils, the equatorial and meridional reflection were at about ~9.7 and 4.7 Å, respectively; while the equatorial and meridional reflection of M45 fibrils were at ~8.4 and 4.4 Å, respectively, different from RIP3. c AFM images and the height profile of RIP3 fibril and M45 fibril. The yellow triangle indicates the head-tail connection in RIP3 fibrils. The arrows indicate the positions to obtain the height profile data. RIP3 fibrils (upper) have a uniform height of 2.3 ± 0.3 nm; M45 fibrils (lower) composed of two kinds of height. One is 1.6 ± 0.3 nm and the other is 3.2 ± 0.3 nm.