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. 2020 Jul 9;11:3422. doi: 10.1038/s41467-020-17232-2

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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 Overview of the complex between INTS13 (orange) and INTS14 (green) with interface patches PL and P1-4 highlighted by orange ovals and labeled accordingly. b–g Close-up views of the interface patches PL and P1–4 as indicated in a. Secondary structure elements as well as side-chains of interface residues are shown and labeled. Dotted lines indicate hydrogen bonds. Residues mutated in this study are underlined. h List of point mutations in interface patches that were tested for effects on complex formation. i, j Coprecipitation experiments from HEK293T cells expressing patch double mutants in V5-SBP-INTS13 i or INTS14 j with the corresponding λN-HA-tagged binding partner. V5-SBP-MBP and the wt proteins were used as negative and positive controls, respectively. Inputs (αV5-blots 1%, αHA-blots 0.5%) and bound fractions (αV5-blots 4%, αHA-blots 20% and 10%) were analyzed by Western blotting.