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TitleDisruption of electrostatic contacts in the HNH nuclease from a thermophilic Cas9 rewires allosteric motions and enhances high-temperature DNA cleavage.
Journal, issue, pagesJ. Chem. Phys., Vol. 157, Page 225103-225103, Year 2022
Publish dateNov 10, 2022 (structure data deposition date)
AuthorsBelato, H.B. / Norbrun, C. / Luo, J. / Pindi, C. / Sinha, S. / D'Ordine, A.M. / Jogl, G. / Palermo, G. / Lisi, G.P.
External linksJ. Chem. Phys. / PubMed:36546784
MethodsX-ray diffraction
Resolution1.37 Å
Structure data

PDB-8f43:
HNH Nuclease Domain from G. stearothermophilus Cas9, K597A mutant
Method: X-RAY DIFFRACTION / Resolution: 1.37 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • geobacillus stearothermophilus (bacteria)
KeywordsHYDROLASE / nuclease domain / CRISPR Cas9 / DNA binding protein

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