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. 2013 Nov 15;27(22):2500–2511. doi: 10.1101/gad.229385.113

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© 2013 Sysoeva 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 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/.

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Figure 1. — Nucleotide binding to NtrC1 ATPase and its X-ray-scattering response. (A) ITC measurements for NtrC1 titrated with ADP (closed squares) and ADP-BeF_x (open circles). (Solid lines) Fits to models with one or two binding sites, respectively (parameters are in Supplemental Table S1). (B) Time-resolved scattering profiles of NtrC1 after mixing with 1 mM ADP-BeF_x. For clarity of presentation, only every third profile from 5 msec to 3 min is shown; errors are illustrated only in the inset. (Green) Profile for apo NtrC1; (red) profile for protein pre-equilibrated with nucleotide. (C) Scattering intensity integrated over the Q-vector range of 0.01 to 0.12 Å⁻¹ (right axis; open circles) or radius of gyration (left axis; open rhombs) versus time after mixing NtrC1 with ADP-BeF_x (final concentrations 327 μM and 1 mM, respectively). (D) Same as C, but for NtrC1 equilibrated with the indicated concentrations of ADP-BeF_x before exposure to X-rays.