Fig. 5: Chitobiose binding perturbs changes induced by T-jump.
From: Mapping protein dynamics at high spatial resolution with temperature-jump X-ray crystallography
a, Ribbon diagrams of lysozyme structures (laser off) in the apo (grey) and chitobiose (CHI)-bound (holo, orange) forms show a decrease in distance between the two lobes of the protein upon ligand binding, characteristic of the active site ‘closing’ motion. Chitobiose is shown as black sticks, along with a ligand omit map contoured to +4σ and carved within 5 Å of the chitobiose molecule. b, Visualization of weighted difference density maps (Ft – Fdark2) for chitobiose-bound datasets show similar in the apo and ligand-bound states. Maps were visualized at an absolute contour level of ±0.04 e− Å−3 alongside initial refined models for each pump–probe time delay. c, Comparing average IADDAT values for ligand-bound and apo maps revealed similar signal levels at 20 ns, with substantial differences appearing by 200 µs. d, Mapping absolute differences in IADDAT between 20 ns and 200 µs (|∆IADDAT|) values onto the structure (C-alphas as spheres) further reveals that time-resolved changes are more pronounced for the apo enzyme than for the inhibitor-bound enzyme.
