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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 Table 4.

Diffusion coefficients

Protein conformation [NaCI] (mM) Mean ± S.D. (10−3 µm2s−1)
EcMutS sliding clamp 100 43 ± 16

EcMutS-EcMutL complex 50 4±2
75 4±3
100 4±2
125 5±3
150 5±3

Fast diffusing EcMutL 25 453 ± 311
100 888 ± 393
150 1716 ±623
200 2220 ± 778

EcMutS-EcMutL(R95F) complex 100 3±2

(EcMutS)-EcMutL-EcMutH* 100 10±10

EcMutS-EcMutL-EcMutH 50 4±2
75 5±3
100 5±3

Free EcMutL-EcMutH complex§ 50 24 ±23
100 41 ± 34
150 118 ±151
*

Oscillating complexes potentially containing unlabelled EcMutS (EcMutS) with co-localized EcMutL-Cy3 and EcMutH-AF647.

A two-sample t-test suggests a significant difference (P=0.001) in diffusion coefficient between the EcMutS-EcMutL complex and (EcMutS)-EcMutL-EcMutH at 100 mM NaCl.

Complexes containing co-localized EcMutS-AF555, unlabelled EcMutL and EcMutH-AF647.

§

See Methods.

A two-sample t-test suggests a significant difference (P<0.0001) in diffusion coefficient between the free EcMutL-EcMutH complex and (EcMutS)-EcMutL-EcMutH at 100 mM NaCl.