8UL2

Structure of rsKiiro using SSX after illumination with 0.53 mJ/mm^2 of 405 nm light

これはPDB形式変換不可エントリーです。

8UL2 の概要

• エントリーDOI: 10.2210/pdb8ul2/pdb
• 分子名称: rsKiiro cis structure, SULFATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: rskiiro, fluorescent protein
• 由来する生物種: Lobophyllia hemprichii; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50781.33

構造登録者

Baxter, J.M.,van Thor, J.J. (登録日: 2023-10-16, 公開日: 2024-11-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)