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. 2020 Aug 13;10:13775. doi: 10.1038/s41598-020-70749-w

Figure 3.

Figure 3

Small angle X-ray scattering of FjChiA_M. The Kratky plot (a) indicates a structured protein with some degree of flexibility while the pair distance distribution function (b) is consistent with an elongated and modular protein. (c) The fit of the ab initio envelope is shown as a blue line (χ2 = 1.20; generated in ATSAS as described in the methods) alongside the experimental data shown in red. (d) The domain organization of FjChiA, including regions predicted for the signal peptide (SigP) and type-9 secretion signal (T9-sec), shown along with the FjChiA_M ab initio SAXS envelope with putatively defined discrete modules uniquely colored. The Fn3-like (e) and Ig (f) domains from the pilin protein BcpA from Bacillus cereus (PDB accession 3kpt) and an antifreeze protein from Marinomonas primoryensis (PDB accession 4p99), respectively, display between 20–30% sequence identity with the putatively annotated regions in FjChiA_M.