Fig. 6: Time-resolved serial synchrotron crystallography.
A Pearson correlation using overlapping data bins shows a clear shift in states between 40–50 ms after photoactivation. Q-weighted isomorphous difference electron density maps (Fo(light)-Fo(dark), red, negative and green, positive contoured at 3.0 sigma) show the distribution of residue displacement across the whole protein. B, E Plot showing the integrated absolute density volume at 3.0 sigma in a 2 Å radius around each residue in the A2AR. Gray boxes show the position of loops along the A2AR protein and residues within 5 Å of the dark-state ligand are highlighted in blue. The density volume around the photoswitch is displayed in purple. C, F Model for changes observed in the binding pocket for state 1 (C) and state 2 (F). Dark state (gray) and light state (purple) models are displayed overlayed with q-weighted isomorphous difference maps (Fo(light)-Fo(dark), red, negative and green, positive at 3.0 sigma) carved around the highlighted residues and ligand. D, G View of the top of the A2AR binding pocket for the two states. Source data are provided as a source data file.
