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. 2021 Jan 18;12:407. doi: 10.1038/s41467-020-20689-w

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Helical nets for the peptide 15-10-3, 29-17-3 (Form I), 29-24-3, and 36-31-3 filaments. The helical nets show the unrolled surface lattice viewed from the outside of the filament. One of the right-handed n-start helices–associated with a cross-α protofilament within the respective assembly–is indicated with a straight line in the corresponding helical net diagram. Adjacent helices shown in c with the conserved interactions are highlighted in a purple box. b Structural alignment of a single cross-α stack containing five helices (left) and their Cα RMSD (right). c Structural alignment of two adjacent helices (left) and their Cα RMSD (right). d Structural alignment of two cross-α stacks (left) and their Cα RMSD (right).