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. 2021 Jun 7;12:3396. doi: 10.1038/s41467-021-23691-y

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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 PR repeat polymer in complex with the ALS/FTD-associated prolyl isomerase PPIA. Only eight residues of the PR polymer could be built into the asymmetric unit; the displayed polymer chain was assembled from symmetry mates (2 mFo–DFc electron density map of PR20 contoured at 1.4σ level, depicted in gray). b Close-up view of the interface between the PR repeat polymer (gray) and PPIA (yellow/green). Hydrogen bonds are depicted by dashed black lines. c The continuous electron density for the PR polymer throughout the crystal lattice allowed a slider-like positioning of its N terminus. d, e Selected regions from the crystal lattice displaying continuous electron density of the PR polymer chain (gray stick model with semi-transparent electron density). PPIA molecules are shown in surface representation.