Skip to main content
. 2024 Jul 12;13:RP93194. doi: 10.7554/eLife.93194

Figure 2. Rhino G31 point mutations do not affect Rhino’s ability to bind H3K9me3.

(A) Line graph summarizing size-exclusion chromatography with inline multiangle light scattering (SEC-MALS) results for the examined Rhino chromodomain constructs. The in solution molecular weight is indicated for each construct. (B) Isothermal titration calorimetry results showing the binding of indicated Rhino chromodomain constructs to the H3K9me3-modified histone tail peptide.

Figure 2.

Figure 2—figure supplement 1. Individual line graphs depicting size-exclusion chromatography with inline multiangle light scattering (SEC-MALS) results for the examined Rhino chromodomain constructs with in solution molecular weight measurements depicted in red.

Figure 2—figure supplement 1.

Figure 2—figure supplement 2. Purified Rhino point mutant chromo domains display normal protein folding.

Figure 2—figure supplement 2.

(A) Raw circular dichroism spectrum plots comparing the ellipticity versus wavelength for tested Rhino chromodomain constructs. (B) Bar graph summarizing circular dichroism spectrum measurements for the tested Rhino chromodomain constructs.