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. 2020 Sep 11;3:125. doi: 10.1038/s42004-020-00372-3

Fig. 4. 3D models of Waltz peptide assemblies.

Fig. 4

Reconstructed fibril 3D models from each assembly reaction, HYFNIF (a), RVFNIM (b), and VIYKI (c) are displayed. Each fibril in the three data sets was reconstructed as a 3D models using information and 3D coordinates extracted directly from the AFM data. The average cross-sectional area and the helical symmetry was determined from the generation of each 3D model. All of the models are shown with identical scale and the colour represent the local radius to the screw axis for visualisation. All fibril models displayed here are cropped to 500 nm segments for visualisation if the contour length is longer than 500 nm. The models are shown with their individual index numbers used throughout (see Supplementary Data), are arranged by similarity (see Fig. 7 and Supplementary Fig. 5), and are placed in the same order as Supplementary Fig. 1. A selection of the models matching the images shown in Fig. 3 are displayed in the Supplementary Fig. 2.