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. 2021 Dec 8;4:1374. doi: 10.1038/s42003-021-02895-4

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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 Mapping cross-linked sites to the HTT-HAP40 sequence of different samples, with cross-linked residue pairs shown as orange circles. Intramolecular distances for HTT-HAP40 (PDBID: 6X9O) shown from grey to green as per the coloured scale bar with unmodelled regions of the protein shown in white. b Mapping cross-links to the HTT-HAP40 sequence of different samples, with exon 1 in red, N-HEAT in blue, bridge domain in green, IDR in grey, C-HEAT in purple and HAP40 in yellow. Cross-linked lysine residues are indicated in red and unmodified lysine residues are indicated in black on the numbered sequence. Intermolecular cross-links (HTT-HAP40) are shown in black, intramolecular cross-links (HAP40-HAP40 or HTT-HTT) are shown in grey and exon 1 cross-links are shown in red. All residues following the exon 1 region of the different constructs are numbered the same for clarity.