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. Author manuscript; available in PMC: 2016 Nov 2.
Published in final edited form as: Nat Struct Mol Biol. 2016 May 2;23(6):558–565. doi: 10.1038/nsmb.3224

Figure 3. The E.r. RT domain binds RNA with high affinity and specificity.

Figure 3

(a) The electrostatic surface of the E.r. RT domain in two views. Blue represents positive surface charge and red represents negative surface charge. (b) Sequence and predicted secondary structures of the E.r. intron D4A and D2. (c) Equilibrium RNA binding of E.r. RT domain. The x-axis shows the E.r. RT domain concentrations on log scale, and the y-axis shows the fraction of bound RNA at each protein concentration. Binding data for E.r. RT and D4A are shown in orange, and for E.r. RT and D2 in blue. Kd is shown as mean +/− sem; error bars, sd; n=4 independent experiments. N.A. indicates that binding between E.r. RT and D2 was too weak to be detected at the protein concentrations tested. The EMSA experiments used for determining this binding curve are shown in Supplementary Fig. 4b.