Movie S3.

FS-AFM imaging revealing several oligomers of the wild-type M/R complex relocating the dsDNA substrate via association with Rad50 coiled coil apices. The first oligomer of the Mre11/Rad50 complex arrives (09:00) soon after the protein sample is flowed through the fluid cell (08:00-08:30) and pulls one end of the DNA template to the left. This first oligomer seems to bind the double-helix firmly, apparently via the globular nucleotide binding sites, as the protein-DNA connection at this location remains stable throughout. The next two Mre11/Rad50 assemblies arrive in the observation frame and relocate the same DNA section from left to the right (10:30). (11:30) Over the course of the remaining observation time, the Mre11-Rad50 complexes stay in constant contact with the open DNA-ends while moving them in various directions. These substantial movements appear to result from the interactions with the Rad50 coiled-coil apices. See Supplementary Fig 2 for further explanations. The reactions were performed at room temperature in buffer over the course of 43:30 min. The timescale is min : sec and the z scale is 1.5 nm (dark to light). Movie speed = 2 frames per second.