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![[Figure 8]](ji5008fig8mag.jpg)
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Figure 8
SAXS data for PmScsCΔLinker. (a) Scattering data collected at ∼0.1 mg ml−1 (blue; χ2 = 1.27), ∼0.5 mg ml−1 (orange; χ2 = 2.19), ∼2.0 mg ml−1 (green; χ2 = 6.89), ∼5.0 mg ml−1 (red; χ2 = 37.59) and ∼10.0 mg ml−1 (grey; χ2 = 177.29). 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 oligomeric composition of the solution is highly dependent on concentration. (c) The fraction of protein present as monomer, dimer and trimer, derived from the fitted global optimization models, shows that the monomeric species is dominant in solution at low concentrations. The concentration of trimer rises slowly and and is predicted to reach a protein fraction of ∼0.2 at 38 mg ml−1, which is the concentration at which crystallization was performed. |
![[Figure 8]](ji5008fig8.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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