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![[Figure 4]](ag5054fig4_combined_mag.jpg)
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Figure 4
Low-salt versus high-salt data comparison for SFPQ1–598. (a) SEC-SAXS scattering data of SFPQ1–598 shown as a log(I) versus log(q) plot. The fit of the EOM ensemble is shown as a blue line. The χ2 of 0.891 indicates an excellent fit to the data. (b) Normalized residual plot for the EOM fit indicating reasonable variation around the fit. (c) Guinier analysis indicates a linear fit within the appropriate qRg range and an Rg smaller than that for SFPQ1–598 in high salt. (d) The normalized residuals for Guinier analysis indicating reasonable variation of the data around the fit. (e) Distance distribution functions of SFPQ1–598 in both salt conditions. (f) Dimensionless Kratky analysis comparing SFPQ1–598 in high-salt and low-salt conditions. (g) Frequency versus Rg plot of initial random and selected ensemble pools. (h) Atomistic models from the ensemble that fits the data. (i) The sequence of the N-terminal IDR of SFPQ (residues 1–276) with charged/proline residues coloured by identity (histidine, purple; arginine and lysine, blue; aspartate and glutamate, red; proline, grey). The AlphaFold pLDDT score is shown beneath the sequence, with regions in orange and yellow having a low confidence score and regions in blue having a moderate–high confidence. (j) Electrostatic map of an SFPQ homodimer with one of the coiled-coil domains removed for space and simplicity. Blue shading shows positively charged pockets and red shading shows negatively charged pockets. The N-terminal IDR is represented as an unrealistic cartoon line with an alternating charge. |
![[Figure 4]](ag5054fig4_combined.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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