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Figure 3
MEMPROT and DADIMODO modelling results. (a) Model and scattering fit for the EptA:DDM complex and (b) the EptA:DPC complex. (a) (i) Representative MEMPROT generated model for the EptA:DDM complex. The atomic structure of EptA is represented in cartoon mode and coloured grey. The DDM corona around EptA is represented as pale blue spheres. (a) (ii) Comparison of the SAXS experimental result (red dots) with the MEMPROT calculated scattering curve (black solid line). The lower inset shows the error-weighted residual difference plot for the experimental SAXS model and the MEMPROT generated model (red dots). (b) (i) Representative MEMPROT generated model for the EptA:DPC complex. The atomic structure of EptA is represented in cartoon mode and coloured grey. The DPC corona around EptA is represented as orange spheres. (b) (ii) Comparison of the SAXS experimental result (blue dots) with the MEMPROT calculated scattering curve (black solid line). The lower inset shows the error-weighted residual difference plot for the experimental SAXS data and the MEMPROT generated model (blue dots). (b) (iii) Model of the EptA:DPC complex obtained with DADIMODO, assigning the soluble domain and transmembrane domain as rigid bodies connected by a flexible bridging helix and linker region. The atomic structure of EptA is represented in cartoon mode and coloured grey and the DPC corona around EptA is represented as orange spheres. (b) (iv) The lower inset shows the error-weighted residual difference plot for the experimental SAXS data and the DADIMODO generated model (blue dots).

IUCrJ
Volume 8| Part 5| September 2021| Pages 732-746
ISSN: 2052-2525
https://doi.org/10.1107/S2052252521005613