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![[Figure 3]](rr5226fig3mag.jpg)
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Figure 3
Ab initio models used in molecular replacement. (a) Predicted local distance difference test (pLDDT) residue position plot as generated by ColabFold showing the confidence in each residue (y axis) and the relative residue location (x axis) for the RdfS amino-acid sequence. The predicted wHTH domain and additional C-terminal helix (positions 16–64) have the highest confidence scores for each model. (b) The RdfS16–64 truncated model used in molecular replacement as described in Section 3.3 ![[link]](../../../../../../logos/arrows/d_arr.gif) . (c) Superposition of all full AlphaFold-generated models [coloured to match (a): blue, orange, green, red and purple] with the finalized RdfS monomer (chain B) structure shown in black. (d) Overlaid backbone ribbon representation of RdfS16–64 for all AlphaFold models [coloured as in (c)] and each of the four RdfS chains (black). This region was highly similar between the models and each of the crystallographically determined RdfS chains (average r.m.s.d. between models of 1.0 Å: Supplementary Table S1). |
![[Figure 3]](rr5226fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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