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. Author manuscript; available in PMC: 2019 Mar 1.
Published in final edited form as: Proteins. 2018 Feb 7;86(Suppl 1):202–214. doi: 10.1002/prot.25452

Figure 4. Determination of Multimerization in Solution by SAXS.

Figure 4

Based on the crystallographic lattice and electron microscopy images, the crystallographers assigned FliD (Ts0886) as a hexamer. However, the molecular weight calculated from the SAXS data of the same sequence suggested that FliD was a dimer. Comparison of all possible dimers in the crystallographic lattice identified one as the most likely dimer. The involvement in domain swapping and in a two-helix bundle supported this dimer as biologically relevant. Another construct of FliD showed strong concentration dependence of assembly (dimer to dodecamer) and thus was not included as a target in CASP. We postulate that the dodecamer, observed also in the crystallographic lattice, is created from assembly of the dimeric form.