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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. 1 — A Schematic representation of a yeast Rad52 subunit depicts N- and C-terminal regions that promote DNA binding, oligomerization, & protein–protein interactions. B Mass photometry analysis predominantly shows a single Rad52 species. The major species (>85%) shows a mass of 498.4 ± 23.8 kDa. A minor 991.8 ± 75.34 kDa species (~8–12%) is observed along with a small fraction of free monomers (72.9 ± 13.9 kDa). C Representative 2D classes of full-length yeast Rad52 observed in cryo-EM analysis and used for determination of the structure. D Color coded depiction of the local resolution mapped on to the Rad52 cryo-EM map. E Gold Standard Fourier shell correlation (FSC) curves estimated using Cryosparc. F De novo built atomic model of Rad52 overlaid on the cryo-EM map. G Atomic model of a Rad52 subunit (magenta) aligned with the crystal structure of human RAD52 (gray; PDB 1KN0) using Chimera with root-mean-square deviation (RMSD) of 0.849 Å for Cα atoms of 88 amino acid pairs. Source data are provided as a Source data file.