Unknown

Dataset Information

0

SpCas9 bound to 10 nucleotide complementary DNA substrate


ABSTRACT:

SUBMITTER: Martin Jinek 

PROVIDER: EMPIAR-11786 | biostudies-other |

REPOSITORIES: biostudies-other

altmetric image

Publications

R-loop formation and conformational activation mechanisms of Cas9.

Pacesa Martin M   Loeff Luuk L   Querques Irma I   Muckenfuss Lena M LM   Sawicka Marta M   Jinek Martin M  

Nature 20220824 7925


Cas9 is a CRISPR-associated endonuclease capable of RNA-guided, site-specific DNA cleavage<sup>1-3</sup>. The programmable activity of Cas9 has been widely utilized for genome editing applications<sup>4-6</sup>, yet its precise mechanisms of target DNA binding and off-target discrimination remain incompletely understood. Here we report a series of cryo-electron microscopy structures of Streptococcus pyogenes Cas9 capturing the directional process of target DNA hybridization. In the early phase o  ...[more]

Similar Datasets

| EMPIAR-11780 | biostudies-other
| EMPIAR-11781 | biostudies-other
| EMPIAR-11782 | biostudies-other
| EMPIAR-11787 | biostudies-other
| EMPIAR-11779 | biostudies-other
| EMPIAR-11783 | biostudies-other
| EMPIAR-11784 | biostudies-other
| S-EPMC5916121 | biostudies-literature
| S-EPMC3840713 | biostudies-literature
| S-EPMC6137436 | biostudies-literature