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![[Figure 4]](jc5035fig4mag.jpg)
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Figure 4
SAXS analysis of Sc-Rsm22. (a) Kratky scattering of both the Sc-Rsm22 monomer and dimer shows that the proteins are folded. (b) Pair distribution curve of both the Sc-Rsm22 monomer and dimer, showing Dmax values of 181 and 138 Å for the dimer and monomer, respectively. (c) The ab initio shape of the Sc-Rsm22 dimer. (d) The ab initio shape of the Sc-Rsm22 monomer. (e) Two identical Sc-Rsm22 monomeric ab initio shapes (red and salmon) are superimposed with the ab initio model of dimeric Sc-Rsm22 (green). (f) A 180° rotation of the superimposed model shown in (e). (g) A fitting curve of the Sc-Rsm22 dimer ab initio model against the experimental SAXS data calculated by the FoXS server. (h) A fitting curve of the Sc-Rsm22 monomer ab initio model against the experimental SAXS data calculated by the FoXS server. |
![[Figure 4]](jc5035fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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