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S. Online, Ab-initio modelling was performed using 15 DAMMIF models which were averaged by DAMAVER. Averaged model correlation with the diffusion curve was then checked using the damstart file as a starting envelope for DAMMIN. The polymerase DAMAVER envelope (Fig. 4a) appears as a pear shaped structure in which the homologous model can be fitted. Additional envelope volume is visible close to the endonuclease domain, implying that it adopts multiple conformations in solution. Using the same methodology, we determine RanBP5 to be a monomer in solution with a measured Mw of 144 kDa close to the theoretical Mw of 126 kDa (Table 3 and supplementary Figure 7). RanBP5 displays an Rg of 38.8 Å and a Dmax of 136 Å. With a Mw lower than that of PA-PB1(1-686), RanBP5 displays a larger Dmax and Rg indicating an extended structure. We have looked over the Protein Data Base (PDB) and found yeast, SAXS was used for the characterisation of PA-PB1(1-686), RanBP5 and PA-PB1(1-686)-RanBP5, respectively in solution. Using the Vc determination method 39 on the diffusion data of PA-PB1(1-686) shows a Mw estimate of 146 kDa (Table 3 and supplementary Figure 7

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