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. 2018 May 2;69(15):3609–3623. doi: 10.1093/jxb/ery164

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© The Author(s) 2018. Published by Oxford University Press on behalf of the Society for Experimental Biology.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 5. — Reduced ligand binding activity of KAI2^ply2. Isothermal titration calorimetry (ITC) experiments were performed by titrating KAR₁ into recombinant KAI2 or KAI2^ply2 protein. The upper panels show raw ITC data. The lower panels present data for the enthalpy change derived from the upper panels. Corresponding thermodynamic properties of KAI2 and KAI2^ply2 are shown in Supplementary Table S1.