Table 2.
Binding affinities of Stl WT and dimerization mutants for trimeric and dimeric Duts
Dutɸ11 (BLI)a | DutɸDI (MST)b | ||||
---|---|---|---|---|---|
KD (M) (10−9) | kon (M−1 s−1) (104) | koff (s−1) (10−6) | KD (M) (10−10) | Signal/noisec | |
StlWT | 1.73 | 2.14 ± 0.01 | 37 ± 6.94 | 3.03 | 10.5 |
StlH73C | 10.3 | 2.45 ± 0.01 | 252 ± 5.29 | 148 | 48.8 |
StlH188C | 2.57 | 2.19 ± 0.01 | 56.3 ± 5.01 | 63.9 | 15.6 |
StlWT + DTTd | 6.72 | 4.18 ± 0.08 | 281 ± 22.7 | 8.60 | 14.8 |
StlH73C + DTTd | 5.22 | 2.19 ± 0.02 | 114 ± 9.4 | 12.7 | 12.4 |
StlH188C + DTTd | 5.10 | 1.54 ± 0.006 | 78.4 ± 4.35 | 61.3 | 15.1 |
StlWT + Cu-Pd | 11.6 | 2.32 ± 0.01 | 270 ± 5.27 | 4.24 | 17.1 |
StlH73C + Cu-Pd | NBDe | NBDe | 0.7 | ||
StlH188C + Cu-Pd | NBDe | NBDe | 3.2 |
aTrimeric Dutɸ11–Stl interactions were measured by biolayer interferometry (BLI)
bDimeric DutɸDI–Stl interactions were measured by Microscale-thermophoresis (MST)
cSignal/noise ratio was calculated by dividing the response amplitude by the noise of the run
dDTT and Cu-P were used at a final concentration of 1 mM
eNot binding detected in experimental condition (KD > 1 × 10−6 M in BLI or signal/noise <5 in MST)
Source data are provided as a Source Data file