Abstract
The Streptococcus pyogenes Cas9 (SpCas9) protein is the centerpiece of a transformative gene editing technology, widely used in molecular biology and precision medicine. Recently, a Cas9 homolog from the thermophilic bacterium G. stearothermophilus Cas9 (GeoCas9) was discovered to be stable in human plasma and functional at wide temperature ranges, offering a promise to optimize the CRISPR-Cas9 molecular tool. Here, AlphaFold2 was used to predict the structure of the full-length GeoCas9 protein, while solution NMR and MD simulations have been harnessed to characterize structure and dynamics of its HNH endonuclease.
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