ArticleFEBS open bio2026
A light-triggered Time-Resolved X-ray Solution Scattering (TR-XSS) workflow with application to protein conformational dynamics.
Article in FEBS open bio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Optimizing photoexcitation conditions for time-resolved X-ray solution scattering experiments.FEBS open bio · 2026Article
- Dynamic photobiology: A collection of experimental protocols for time-resolved structural studies on light-activated proteins.FEBS open bio · 2026Article
- Real-time Structural Tracking of Slow P-type ATPase Dynamics.The Journal of membrane biology · 2026Article
- Assessing protein-specific radiation damage in time-resolved X-ray solution-scattering experiments at high-brilliance synchrotrons using fast detector readout.Acta crystallographica. Section D, Structural biology · 2026Article
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4 authors.
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Abstract
Time-resolved X-ray solution scattering (TR-XSS) is a synchrotron-based methodology that enables real-time structural characterization under near-native conditions to provide insight into dynamic and transient structural changes inaccessible to static high-resolution methods such as cryo-electron microscopy (cryo-EM) or X-ray crystallography. Here, we present a workflow for light-triggered TR-XSS experiments that spans data collection, data processing, kinetic analysis, and structural refinement, with accompanying Python scripts. A calcium-transporting P-type ATPase membrane protein (LMCA1) is used as an illustrative example, but the protocol is broadly applicable to diverse protein systems. This workflow offers a practical framework for collecting TR-XSS synchrotron data and subsequent data analysis and interpretation.
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