Extended Data Fig. 3: Workflow for obtaining the cryo-EM structure of the RAD52 undecamer.

a. Two data sets, 30° tilted and non-tilted, were collected for apo RAD52. b-c. For single particle analysis, micrographs were manually curated and multiple rounds of 2D classification were performed yielding a final stack of 623,559 particles which were used for ab-initio 3D reconstruction (d.). e. The final structures of apo RAD52 were obtained by performing a non-uniform refinement by imposing C1 (2.8 Å, left) and C11 (2.5 Å, right; EMD-41357) symmetries. The residues in the structures are colored by resolution suggesting the rigid core and DNA binding regions (blue) and more flexible loops (red). The three regions containing the DNA binding residues are shown as zoom-ins. The heatmaps of the angular distribution of particles used to generate the final structures of apo RAD52 are shown.