Table 3.
Dynamic light-scattering analyses of MutL proteins
| Protein | Dso/10−7 cm2 s−1 a | Stokes radius r (Å)b | f / foc | Distance (Å)d |
|---|---|---|---|---|
| WT (AMPPNP) | 3.86±0.08 (11) | 55.5 | 1.62 | 160 |
| Δ2 (AMPPNP) | 4.03±0.06 (24) | 53.2 | 1.58 | 111 |
| Δ5 (AMPPNP) | 4.48±0.08 (25) | 47.8 | 1.44 | 76 |
| Δ7 (AMPPNP) | 4.20±0.04 (14) | 51.0 | 1.54 | 98 |
| WT (EDTA) | 2.48±0.07 (8) | 86.4 | 2.53 | — |
| Δ2 (EDTA) | 2.45±0.04 (13) | 87.5 | 2.60 | — |
| Δ5 (EDTA) | 3.32±0.14 (8) | 64.5 | 1.92 | — |
| Δ7 (EDTA) |
3.12±0.06 (11) |
68.7 |
2.10 |
— |
| aAverage corrected diffusion coefficient based on data collected at angles of 90, 75, 60 and 45°. The number of measurements is shown in parentheses. | ||||
| bStokes radius, r, is calculated as r=kT/6πηDso, where k is Boltzmann's constant and η the viscosity of water at 20.0°C. | ||||
| cThe friction coefficient, f, is calculated as f=kT/Dso, and friction coefficient for a sphere of equivalent mass (M), fo, is given by fo=6πη(3Mv/4πN)1/3, where v is the partial specific volume of the protein and N is Avogadro's number. Deviation of f/fo from 1.0 indicates that the protein molecule is elongated. | ||||
| dLN40 dimer is translated relative to LC20 along a shared dyad axis. The distance between their centers of mass that results in a calculated diffusion coefficient consistent with those measured experimentally is listed. | ||||