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![[Figure 7]](ji5008fig7mag.jpg)
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Figure 7
SAXS data for native PmScsC. (a) Scattering data collected at ∼0.1 mg ml−1 (blue; χ2 = 2.55), ∼0.5 mg ml−1 (orange; χ2 = 7.05), ∼2.0 mg ml−1 (green; χ2 = 72.85), ∼5.0 mg ml−1 (red; χ2 = 371.94) and ∼10.0 mg ml−1 (grey; χ2 = 815.23). The overlaid line (black) on each scattering curve is the fitted linear combination of monomer and trimer scattering curves. (b) The pair-distance distribution function, p(r), derived from the scattering data normalized by concentration shows that the 0.1 mg ml−1 data set differs slightly from those at the other concentrations (which all overlay), indicating the possibility that monomer is present in solution at the lowest concentration. (c) The fraction of protein present as monomer and trimer, derived from the fitted global optimization models, shows that at total protein concentrations above 0.05 mg ml−1 (calculated concentration, or 0.1 mg ml−1 measured concentration) the protein is almost exclusively present as a trimer in solution. |
![[Figure 7]](ji5008fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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