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. 2019 Feb 14;9:2012. doi: 10.1038/s41598-018-38353-1

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© The Author(s) 2019

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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Analysis of the Tim23-Tim50 interaction in vitro. Recombinantly expressed and purified versions of Tim50_IMS were incubated with Tim23_IMS in the presence of 1 mM DSS, as indicated. Cross-linking adducts were separated by SDS-PAGE and analyzed by staining with Coomassie Brilliant Blue (CBB) (top panel) or subjected to immunoblotting with antibodies raised against Tim50 (middle panel) and Tim23 (bottom panel). Arrows indicate the Tim23-Tim50 crosslink. Mutant D337V was not analyzed as it was largely insoluble after recombinant expression. The R339S mutant was partially degraded, suggesting that the recombinantly expressed mutant protein is less stable.