Movie S1.

FS-AFM imaging reveals wild-type M/R binding of the DNA substrate via the Rad50 coiled-coil apices. The Rad50 coiled-coils extend from the globular protein core where the apices appear to alternately bind and disengage from the double-helix, creating an intermittently binding movement along the dsDNA template, while the dsDNA seems to be pushed rightwards at the same time (00:00-24:00). A second, larger, M/R aggregate arrives close to the DNA and the coiled-coil apices of this complex bind DNA at two locations. At the times between 24:30 and 25:00 min the DNA strand is pulled to towards the second M/R aggregate via the first connecting Rad50 coiled coil hook, before being released, while the contact between the second Rad50 coiled-coil and the DNA-end remains throughout. Reactions were performed at room temperature in buffer over the course of 29:00 mins. This video is also represented as series of individual frames in Fig 4A. Movie speed = 2 frames per second. The time scale is min : sec and the z scale is 2 nm (dark to light).

Modes of action of the archaeal Mre11/Rad50 DNA-repair complex revealed by fast-scan atomic force microscopy

Ekaterina Zabolotnaya, Ioanna Mela, Mark J. Williamson, Sian M. Bray, Siu Kei Yau, Dimitra Papatziamou, J. Michael Edwardson, Nicholas P. Robinson, and Robert M. Henderson

PNAS. 2020. 117:14936-14947 DOI: 10.1073/pnas.1915598117