Fig. 7From: Insight into the molecular mechanism of the transposon-encoded type I-F CRISPR-Cas systemHead-to-tail TniQ dimerization: The C-terminal domain is made up of ten α-helices, whereas the N-terminal domain is made up of three α-helices. One TniQ monomer binds to the other TniQ monomer via hydrophilic interactions between α-helix 3 and α-helix 12 [15]. Created with BioRender.comBack to article page