Extended Data Fig. 7: Measured binding affinities of a full-length and truncated tRNAAla to dBa1Cas12a3.
From: RNA-triggered Cas12a3 cleaves tRNA tails to execute bacterial immunity
Binding of the activated dBa1Cas12a3 ternary complex to the indicated fluorescent RNA substrate was quantified by MST. dBa1Cas12a3 contains the E1065A mutation in the RuvC endonuclease domain to render it catalytically inactive. Symbols and error bars represent the mean ± standard deviation of independent experiments (n = 3).
