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![[Figure 2]](gm5106fig2mag.jpg)
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Figure 2
Examples of results from time-resolved SX using three different methods for reaction initiation. (a) Time-resolved structural snapshots of the release of azo-CA4 from tubulin (Wranik, Weinert et al., 2023  ). The time arrow depicts the investigated time regime. The panels from left to right show the isomorphous difference maps obtained at 100 ns with changes centered on the ligand, 100 µs with changes centered on the binding pocket and 100 ms with conformational changes propagating throughout the protein. All panels show isomorphous difference maps in red (negative) and green (positive) at 3σ. The structure in the given time range (colored orange) is compared with that in the previous time range (colored gray). (b) shows the time-resolved difference electron-density (DED) maps of lysozyme following a temperature jump (T-jump; Wolff et al., 2023). Weighted DED maps are depicted for each time point around residues 97–100 of lysozyme visualized at an absolute contour level of ±0.04 e− Å−3. Positive DED is displayed as a blue map and the negative DED map is shown in orange. The green arrows depicted at the 200 µs time step indicate proposed coordinate motions derived from analysis of the DED. (c) Difference electron-density maps around the active center of both subunits (subunit A, top row; subunit B, lower row) of a lactamase at different time points of a mix-and-inject time-resolved experiment with the lactamase inhibitor sulbactam (Malla et al., 2023). Omit maps are shown in all subpanels except for subpanels d, f, j and l, which show polder maps (contour levels ±3σ). SUB, sulbactam; TEN, trans-enamine. Images and captions were taken and adapted from (a) Wranik, Weinert et al. (2023), (b) Wolff et al. (2023) and (c) Malla et al. (2023), licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/). |
![[Figure 2]](gm5106fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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