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. Author manuscript; available in PMC: 2018 Mar 10.
Published in final edited form as: Nature. 2016 Nov 16;539(7630):583–587. doi: 10.1038/nature20562

Extended Data Figure 2. The fluorophore-labelled E. coli MMR proteins used in these studies and the formation of an EcMutS sliding clamp on DNA.

Extended Data Figure 2

a, Coomassie stained (top) and fluorescent (bottom) SDS–PAGE gels of labelled MMR proteins. For gel source data, see Supplementary Fig. 1. b, A crystal structure of the N-terminal domain of EcMutL bound to AMP-PNP (top) and magnification of the binding domain (bottom; PDB ID: 1B63). AMP-PNP is shown in green and Arg-95 (R95) is shown in magenta24. c, An illustration of the kymograph construction of three separate EcMutS sliding clamps on a single mismatched DNA. d, The distribution of diffusion coefficients for the EcMutS sliding clamp. The data were fit to a Gaussian with the mean ± s.d. e, The distribution of dwell times (mean ± s.e.m.) for the EcMutS sliding clamp.