Fig. 4: Increasing temperature modulates substrate turnover.
From: Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography
XI active site, 60 s after reaction initiation at 20 °C, 30 °C, 40 °C, 45 °C, and 50 °C; a 2Fo − Fc density shown at RMSD levels from 1.0–3.5, strongest density is shown in red; b 2Fo − Fc absolute value electron number (END) maps shown at 0.7 e−/ Å3, are quantitatively comparable and therefore enable a side-by-side comparison of the electron density, demonstrating its increase with raising temperature; c Fo − Fo difference electron density (DED) maps shown at 2.7 ± RMSD show the modulation of the ligand density. An arrow highlights the electron density change around the closed-ring glucose O2-oxygen. The glucose ligand is shown in closed ring conformation (yellow) and the open-ring intermediate (blue), relevant XI active site residues are shown in grey, waters are omitted for clarity.
