Results: 2

1.
Figure 2

Figure 2. From: A Broad Range of Conformations Contribute to the Solution Ensemble of the Essential Splicing Factor U2AF65.

The 20-PDB (light color) or 50-PDB (dark color) ensemble fits of (A) U2AF651,2 (blue) and (B) U2AF651,2FIR (green) SAXS data.The radii of gyration (RG) are plotted on the x-axis, and the frequency of a structure with a given RG on the y-axis. Gray dashed lines plot the randomized starting pool; Solid lines the selected pool. The most typical or divergent selected structures are inset.

Jermaine L. Jenkins, et al. Biochemistry. ;51(26):5223-5225.
2.
Figure 1

Figure 1. From: A Broad Range of Conformations Contribute to the Solution Ensemble of the Essential Splicing Factor U2AF65.

Comparison of U2AF structures and SAXS data. (A) Human U2AF65 domain organization and constructs used in this study. (B) Comparison of dU2AF651,2 (blue, PDB ID 2G4B) or FIR1,2 (green, PDB ID 2QFJ) crystal structures and the ‘open’ (maroon, PDB ID 2YH1) or ‘closed’ (brown, PDB ID 2YH0) NMR models of U2AF651,2. RNA ligands are omitted for clarity. The FIR1,2 structure in the absence of ligand is nearly identical (PDB ID 3UWT). N-and C-terminal secondary structures are colored dark blue or red, respectively. (C) Experimental P(r) functions of U2AF651,2 (gray, solid line) and U2AF651,2FIR (green, solid line) compared with calculated P(r) functions of the structures (dashed lines, colored as in A). Plots were scaled by the integrated area of the curves. (D) The χ2 values between the experimental U2AF651,2 (filled) U2AF651,2FIR (hatched) data and each of the structures shown in A, calculated as described in Supplementary Methods.

Jermaine L. Jenkins, et al. Biochemistry. ;51(26):5223-5225.

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