Apparent dissociation constants for UvsX binding to dsDNA or ssDNA^a.

a<p>Equilibrium binding data derived from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0066654#pone-0066654-g002" target="_blank">Figures 2</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0066654#pone-0066654-g003" target="_blank">3</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0066654#pone-0066654-g004" target="_blank">4</a>, and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0066654#pone-0066654-g006" target="_blank">6</a>.</p>b<p>No binding observed under the experimental conditions used.</p>c<p>Not Determined. Measuring the apparent <i>K_d</i> for dsDNA in the presence of ATP and heterologous ssDNA requires unattainably high protein concentrations.</p>d<p>Based on observation in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0066654#pone-0066654-g004" target="_blank">Figure 4</a> that homologous dsDNA does not destabilize UvsX-ssDNA interactions.