Table 1.
Experimental and model SAXS parameters
| Proteins | Exp. I(0)a | Conc. (mg/ml)b | Estimated Mr (kDa)c | Mrd (kDa) | Number of amino acids | Rg (GNOM)e | Rg (Guinier)e | Dmaxf (nm) | Χ(over) | Χ(crysol) | Damaver NSDg |
|---|---|---|---|---|---|---|---|---|---|---|---|
| 4E-BP | 4883 | 1.86 | 20 | 12.8 | 117 | 4.86 ± 0.22 | 4.88 ± 0.17 | 16.0 ± 0.8 | 0.430 | NA | 2.50 ± 0.14 |
| eIF4E | 4256 | 1.26 | 26.6 | 25.05 | 217 | 2.34 ± 0.11 | 2.23 ± 0.44 | 6.8 ± 0.6 | 0.433 | 1364 | ND |
| eIF4E/4E-BP Complex | 5922 | 1.11 | 41.9 | 37.058 | 334 | 3.60 ± 0.03 | 3.52 ± 0.04 | 12.1 ± 0.6 | 1.360 | NA | 1.40 ± 0.08 |
| BSA | 40247 | 4.8 | 66.3 | 582 | ND | 3.1 ± 0.2 | 9.0 ± 0.4 | ND | ND | ND |
aValues for I(0) have been extrapolated by the Guinier approximation from the experimental scattering profiles.
bConcentration of the protein used for the calculation of the estimated Mr.
cRelative molecular mass estimated from I(0) and the concentration of the protein through BSA calibration.
dRelative molecular mass predicted from the sequence.
eRg (Guinier), Rg (GNOM), radius of gyration given by the Guinier approximation, and calculated by the program GNOM, respectively, given in nm.
fMaximum dimension of the macromolecules.
Χ(over) Discrepancy between the SAXS profile and its fit by the overall shapes-models calculated by DAMMIF, and Χ(crysol) the average discrepancy of the best atomic models estimated with the program CRYSOL (Supplementary Data). ND, not determined; NA, not appropriate.
gAverage of the normalized spatial discrepancies (NSD) obtained by Damaver for the different ab initio models generated by DAMMIF, DAMMIN and GASBOR.