AceCas9 and its metal dependence. a , Top: domain organization of AceCas9 shown as colored blocks in the direction from the N terminus to the C terminus. The regions corresponding to the structural domains are colored and labeled, and the relevant residues are labeled. RuvC-I–RuvC-III, discontinuous segments of the RuvC domain; BH, bridge helix; REC1, nucleic acid-recognition domain 1; REC2, nucleic acid-recognition domain 2; HNH, HNH nuclease domain; PID, PAM interaction domain. Bottom: ...
