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. 2022 Apr 21;29(5):420–429. doi: 10.1038/s41594-022-00755-1

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© The Author(s) 2022

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,b, Crosslinks between TRiC and tubulin (a) and between TRiC and actin/PhLP2A (b) reported from literature are mapped onto the TRiC structure with bound proteins. Left, identified crosslinks compatible with our structural models are indicated in green lines; crosslinks that are not sterically compatible with our model are indicated in yellow lines and could represent other stages of the substrate folding cycle that are not captured in our structures. Spheres represent lysine residues that are crosslinked. Right, magnified views showing the atomic environment of 3 TRiC–tubulin, 1 actin-PhLP2A, and 1 TRiC-PhLP2A crosslinks that support our models.