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. 2016 Apr 7;6:23769. doi: 10.1038/srep23769

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Copyright © 2016, Macmillan Publishers Limited

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Isothermal titration calorimetry (ITC) measurement for the interaction of c-di-GMP and XOC_2102 (a) or XOC_4190 (b). The data indicate that the dissociation constants (K_d) are 2.90 ± 0.13 μM or 4.59 ± 0.36 μM, respectively. (c) Schematic representation of the two truncated XOC_4190 proteins. XOC_4190ΔE, the truncated XOC_4190 without EAL domain; XOC_4190ΔG, the truncated XOC_4190 with the only EAL domain. ITC measurement for the interaction between c-di-GMP and XOC_4190ΔG (d) or XOC_4190ΔE (e). The data indicate that the K_d is 4.46 ± 0.28 μM for interaction between c-di-GMP and XOC_4190ΔG. Top panels, the titration calorimetry of the proteins with c-di-GMP at room temperature; lower panels, normalized ITC data for titrations versus molar ratio of c-di-GMP and the proteins.