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. 2013 May 10;452(Pt 2):223–230. doi: 10.1042/BJ20130269

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© 2013 The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Licence (CC-BY)(http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

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(A) View of Leu¹⁷⁰ and Val²⁰² at the dimer interface. These residues were each changed to aspartate to disrupt the interface. (B) Gel-filtration elution profiles of dimeric SsoCas6 and the SsoCas6-L170D/V202D variant, which elutes with a retention volume consistent with a monomeric composition (expected molecular mass of 33 kDa). (C) Thermofluor analysis of heat-induced denaturation of wild-type (WT) and monomeric SsoCas6, showing the 7°C difference in melting temperatures (Tm). (D) Single-turnover kinetic comparison of wild-type and monomeric SsoCas6. The catalytic activity of the monomer is reduced by 95% compared with the wild-type (WT) enzyme.