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. 2019 Mar 7;10:1104. doi: 10.1038/s41467-019-09033-z

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© The Author(s) 2019

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 — Interactions between the two protein stacks in the murine and human fibril. a Cross-sectional view of four molecular layers of the murine fibril with a close-up on the stack-stack interface. b Side view showing the ladder of ionic residues which make bidentate interactions between the two murine protein stacks. c Cross-sectional view of four molecular layers of the human fibril with a close-up on the interface between the protein stacks. d Cross-stack steric zipper formed by β-sheet β3 (residues Tyr29 and Ile 30) of the human fibril. e Cross-stack interactions between the α-amino group of Ser2 and the side chain carboxyl group of Asp33 from the other protein stack