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  Power Density Titration of Reversible Photoisomerization of a Fluorescent Protein Chromophore in the Presence of Thermally Driven Barrier Crossing Shown by Quantitative Millisecond Serial Synchrotron X-ray Crystallography

Baxter, J. M., Hutchison, C. D. M., Fadini, A., Maghlaoui, K., Cordon-Preciado, V., Morgan, R. M. L., et al. (2024). Power Density Titration of Reversible Photoisomerization of a Fluorescent Protein Chromophore in the Presence of Thermally Driven Barrier Crossing Shown by Quantitative Millisecond Serial Synchrotron X-ray Crystallography. Journal of the American Chemical Society, 146(24), 16394-16403. doi:10.1021/jacs.3c12883.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000F-6DFB-D Version Permalink: https://hdl.handle.net/21.11116/0000-000F-7262-2
Genre: Journal Article

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High-resolution SSX power titration chromophore-omit maps, occupancy fitting, crystallographic data tables, modeling of laser and X-ray heating, absorption spectra, flash photolysis error propagation and modeling, knife-edge fitting. Coordinates and structure factor amplitudes have been deposited in the PDB database. For preconverted (Trans) rsKiiro under different 400 nm illumination conditions: 0 mJ/mm2 (PDB 8UL0), 0.1 mJ/mm2 (PDB 8UL1), 0.53 mJ/mm2 (PDB 8UL2), 1.78 mJ/mm2 (PDB 8UL3), 6.74 mJ/mm2(PDB 8UL4), and 14.43 mJ/mm2 (PDB 8UL5)
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 Creators:
Baxter, J. M.1, Author
Hutchison, C. D. M.1, Author
Fadini, A.1, Author
Maghlaoui, K.1, Author
Cordon-Preciado, V.1, Author
Morgan, R. M. L.2, Author
Agthe, M.3, Author
Horrell, S.4, Author
Tellkamp, F.5, Author           
Mehrabi, P.6, Author           
Pfeifer, Y.7, Author
Müller-Werkmeister, H. M.7, Author
von Stetten, D.3, Author
Pearson, A. R.8, Author
van Thor, J. J.1, Author
Affiliations:
1Department of Life Sciences, Imperial College London, ou_persistent22              
2Center for Structural Biology, Imperial College London, ou_persistent22              
3European Molecular Biology Laboratory (EMBL), ou_persistent22              
4Department of Physics, Center for Free-Electron Laser Science, Institute for Nanostructure and Solid State Physics, University of Hamburg, ou_persistent22              
5Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_2074322              
6Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
7Institute of Chemistry-Physical Chemistry, University of Potsdam,, ou_persistent22              
8Institute for Nanostructure and Solid State Physics & The Hamburg Centre for Ultrafast Imaging, HARBOR, Universität Hamburg, ou_persistent22              

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 Abstract: We present millisecond quantitative serial X-ray crystallography at 1.7 Å resolution demonstrating precise optical control of reversible population transfer from Trans–Cis and Cis–Trans photoisomerization of a reversibly switchable fluorescent protein, rsKiiro. Quantitative results from the analysis of electron density differences, extrapolated structure factors, and occupancy refinements are shown to correspond to optical measurements of photoinduced population transfer and have sensitivity to a few percent in concentration differences. Millisecond time-resolved concentration differences are precisely and reversibly controlled through intense continuous wave laser illuminations at 405 and 473 nm for the Trans-to-Cis and Cis-to-Trans reactions, respectively, while the X-ray crystallographic measurement and laser illumination of the metastable Trans chromophore conformation causes partial thermally driven reconversion across a 91.5 kJ/mol thermal barrier from which a temperature jump between 112 and 128 K is extracted.

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Language(s): eng - English
 Dates: 2024-05-282023-11-162024-05-292024-06-072024-06-19
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jacs.3c12883
 Degree: -

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Project name : J.J.v.T. acknowledges support by the Biotechnology and Biological Sciences Research Council (BBSRC) [BB/P00752X/1]. A.R.P. is supported by the Clusters of Excellence “CUI: Advanced Imaging of Matter” of the Deutsche Forschungsgemeinschaft (DFG)─EXC 2056─project ID 390715994 and “The Hamburg Centre for Ultrafast Imaging”─EXC 1074─project ID 194651731. The authors acknowledge support from Imperial College London Centre for Structural Biology, the CCP4/DLS 2018 workshop, the Dynamic Structural Biology BAG as part of the UK XFEL hub, the DESY Beamline P11, BAG-20170381, and EMBL P14.2 BAG MX-660. T-REXX is supported by the Bundesministerium für Bildung und Forschung (Verbundforschungsprojekte 05K16GU1, 05K19GU1 & 05K22GU6). H.M.W. is supported by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation under Germany’s Excellence Strategy (EXC 2008/1-390540038, UniSysCat). The authors would like to acknowledge Prof. Nils Huse, Universität Hamburg, for the loan of equipment used in the SSX experiments.
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Title: Journal of the American Chemical Society
  Other : JACS
  Abbreviation : J. Am. Chem. Soc.
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 146 (24) Sequence Number: - Start / End Page: 16394 - 16403 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870