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Updated: Feb 2, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
Published on: November 5, 2018
Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization
Inokentijs Josts1,2, Stephan Niebling3,1, Yunyun Gao2,4
1The Hamburg Center for Ultrafast Imaging, University of Hamburg, Hamburg 22761, Germany.
Abstract:
This work demonstrates a new method for investigating time-resolved structural changes in protein conformation and oligomerization via photocage-initiated time-resolved X-ray solution scattering by observing the ATP-driven dimerization of the MsbA nucleotide-binding domain. Photocaged small molecules allow the observation of single-turnover reactions of non-naturally photoactivatable proteins. The kinetics of the reaction can be derived from changes in X-ray scattering associated with ATP-binding and subsequent dimerization. This method can be expanded to any small-molecule-driven protein reaction with conformational changes traceable by X-ray scattering where the small molecule can be photocaged.
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