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. 2016 Nov 1;30(21):2391–2403. doi: 10.1101/gad.291377.116

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© 2016 Jin et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 4. — Determinants for RNA-binding specificity. (A, top panel) EMSA of the binding of the wild-type (WT) and indicated mutants of G5N to the 13-mer U4 fragment used for obtaining the cocrystal structure. A 2:1 protein to RNA molar ratio was used in the assay. (Middle panel) Binding of G5N and its mutants to in vitro transcribed full-length U4 snRNA. (Bottom panel) G5N and its mutants used for EMSA experiments. (B–E) FP measurements of binding affinities of the wild-type and mutant G5N proteins to the 13-mer RNA. The derived dissociation constant (K_D) values are shown.