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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. 5 — a Sequences of Form II, Form IIa and 29-20-2 peptides. Residues changed from original the Form II sequences are highlighted with blue dots. b–d Cryo-EM of peptides Form II, Form IIa, and 29-20-2. Representative raw micrographs are shown on the left (scale bar 500 Å) out of a total number of 171, 233, and 347 images recorded, respectively. The cryo-EM reconstructions are shown in the middle, one view from outside highlighting right-handed 3-start helices, and another view from the inside of the nanotube lumen highlighting the left handed 11-start or 12-start helices. The side and top views of the atomic models are shown on the right. e Structural alignment of the asymmetric unit (helix-dimer) of the three peptide filaments. f Structural alignment of six asymmetric units of the three peptide filaments. The alignment RMSD is shown. g Helical nets for the Form II and 29-20-2 filaments. The helical nets show the unrolled surface lattice viewed from the outside of the filament. The right-handed 3-start helices can be clearly discerned for each assembly, although not explicitly highlighted. The positions of the left-handed 11- and 12-start helices are identified and are defined by the red lines crossing the green horizontal line. Subunits labeled n and n + 11 are connected with red lines.