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. 2023 Oct 5;14:6215. doi: 10.1038/s41467-023-41993-1

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© The Author(s) 2023

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — Tryptophan quenching experiments with A poly(dT) or B (dT)₈₄ reveal two ssDNA binding phases for Rad52 with sites sizes of 56 ± 3 and 158 ± 3, respectively. C Mass photometry analysis of (dT)₈₄ or Rad52 + (dT)₈₄ (1:0.1 or 1:1, Rad52^decamer:ssDNA) show that a single Rad52 homodecamer binds to (dT)₈₄. The small fraction of higher order Rad52 molecules also bind to ssDNA and behave as a single DNA-bound complex. D Tryptophan quenching of Rad52 as a function of ssDNA length shows that DNA lengths of >(dT)₄₅ are required to observe maximal signal quenching. Data are representative of at least 3 independent replicates and error bars shown are +/− SEM for each data point. Source data are provided as a Source data file.