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. 2020 Dec 11;11:6349. doi: 10.1038/s41467-020-20227-8

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© The Author(s) 2020

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. 2 — a The primary sequence of the hnRNPA1 fibril core. Residues forming the β-strand are highlighted in red. Glycine residues are in blue. Secondary structures are indicated below. b Top view of the cryoEM structure of hnRNPA1 LC fibril. Six layers of backbones are shown. The structure is colored by chain. The pseudo-2-fold screw axis is indicated. The sheet kink region is zoomed in with side chains shown. c Side views of the fibril structure in b.