8UL3

Structure of rsKiiro using SSX after illumination with 1.78 mJ/mm^2 of 405 nm light

This is a non-PDB format compatible entry.

Summary for 8UL3

• Entry DOI: 10.2210/pdb8ul3/pdb
• Descriptor: rsKiiro cis structure, SULFATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: rskiiro, fluorescent protein
• Biological source: Lobophyllia hemprichii; More
• Total number of polymer chains: 2
• Total formula weight: 50781.33

Authors

Baxter, J.M.,van Thor, J.J. (deposition date: 2023-10-16, release date: 2024-11-27)

Primary citation

Baxter, J.M.,Hutchison, C.D.M.,Fadini, A.,Maghlaoui, K.,Cordon-Preciado, V.,Morgan, R.M.L.,Agthe, M.,Horrell, S.,Tellkamp, F.,Mehrabi, P.,Pfeifer, Y.,Muller-Werkmeister, H.M.,von Stetten, D.,Pearson, A.R.,van Thor, J.J.
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.
J.Am.Chem.Soc., 146:16394-16403, 2024

PubMed 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.

PubMed: 38848551
DOI: 10.1021/jacs.3c12883

Experimental method

X-RAY DIFFRACTION (1.75 Å)