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10.1038/s41467-017-01496-2 http://scihub22266oqcxt.onion/10.1038/s41467-017-01496-2 C5680257!5680257!29123204     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2017 ; 8 (ä): ä Nephropedia Template TP {{tp|p=29123204|t=2017. Structural insights into DNA cleavage activation of CRISPR-Cas9 system |pdf=|usr=}}{{29123204}} gab.com Text Structural insights into DNA cleavage activation of CRISPR-Cas9 system JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=29123204 #FOAvip CRISPR-Cas9 technology has been widely used for genome engineering. Its RNA-guided endonuclease Cas9 binds specifically to target DNA and then cleaves the two DNA strands with HNH and RuvC nuclease domains. However, structural information regarding the DNA cleavage-activating state of two nuclease domains remains sparse. Here, we report a 5.2?Å cryo-EM structure of Cas9 in complex with sgRNA and target DNA. This structure reveals a conformational state of Cas9 in which the HNH domain is closest to the DNA cleavage site. Compared with two known HNH states, our structure shows that the HNH active site moves toward the cleavage site by about 25 and 13?Å, respectively. In combination with EM-based molecular dynamics simulations, we show that residues of the nuclease domains in our structure could form cleavage-compatible conformations with the target DNA. Together, these results strongly suggest that our cryo-EM structure resembles a DNA cleavage-activating architecture of Cas9. Twit Text FOAVip Structural insights into DNA cleavage activation of CRISPR-Cas9 system ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=29123204 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29123204 #FOAvip English Wikipedia <ref>{{Cite pmid|29123204}}</ref> Structural insights into DNA cleavage activation of CRISPR-Cas9 system #MMPMID29123204 Huai C; Li G; Yao R; Zhang Y; Cao M; Kong L; Jia C; Yuan H; Chen H; Lu D; Huang Q Nat Commun 2017[]; 8 (ä): ä PMID29123204show ga CRISPR-Cas9 technology has been widely used for genome engineering. Its RNA-guided endonuclease Cas9 binds specifically to target DNA and then cleaves the two DNA strands with HNH and RuvC nuclease domains. However, structural information regarding the DNA cleavage-activating state of two nuclease domains remains sparse. Here, we report a 5.2?Å cryo-EM structure of Cas9 in complex with sgRNA and target DNA. This structure reveals a conformational state of Cas9 in which the HNH domain is closest to the DNA cleavage site. Compared with two known HNH states, our structure shows that the HNH active site moves toward the cleavage site by about 25 and 13?Å, respectively. In combination with EM-based molecular dynamics simulations, we show that residues of the nuclease domains in our structure could form cleavage-compatible conformations with the target DNA. Together, these results strongly suggest that our cryo-EM structure resembles a DNA cleavage-activating architecture of Cas9. äStructural insights into DNA cleavage activation of CRISPR-Cas9 system(epmc).pdf DeepDyve Pubget Overpricing