In the realm of genome editing, Cas9 enzyme is a versatile tool, guided by RNA to precisely cleave DNA at specific sites. Cryo-electron microscopy structures of Streptococcus pyogenes Cas9 unveil the intricate process of target DNA binding, guiding us through the essential stages of hybridization, activation, and conformational changes that illuminate the mechanism underlying this transformative technology. In a recent study, exploration of Cas9's intricate dynamics, revealed through 19 structures bound to both on- and off-target DNAs, uncovers how Cas9 identifies off-target sites. This revelations hold promise towards unlocking the full potential of genome editing. Furthermore, insights into de novo protein design open doors to a realm of possibilities, where customized proteins could be tailored to tackle intricate biological challenges, revolutionizing fields such as medicine, biotechnology, and beyond.

Martin Pacesa is a postdoctoral researcher at the École polytechnique fédérale de Lausanne (EPFL), situated by the picturesque shores of Lake Geneva in Switzerland. As a real CRISPR enthusiast, he has made numerous significant contributions to the field of CRISPR research.

Introduction: to min. 9:00

CRISPR: min. 9:00-23:00

Computational protein design: from min. 23:00 to end.