9EQS

8fs pulse duration 100uJ pulse energy thaumatin

9EQS の概要

• エントリーDOI: 10.2210/pdb9eqs/pdb
• 分子名称: Thaumatin I, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: radiation damage, xfel, pulse duration and intensity, disulphides, plant protein
• 由来する生物種: Thaumatococcus daniellii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22378.13

構造登録者

Owen, R.L.,Hough, M.A.,Worrall, J.,Williams, L. (登録日: 2024-03-22, 公開日: 2025-04-02, 最終更新日: 2025-05-14)

主引用文献

Williams, L.J.,Thompson, A.J.,Dijkstal, P.,Appleby, M.,Assmann, G.,Dworkowski, F.S.N.,Hiller, N.,Huang, C.Y.,Mason, T.,Perrett, S.,Prat, E.,Voulot, D.,Pedrini, B.,Beale, J.H.,Hough, M.A.,Worrall, J.A.R.,Owen, R.L.
Damage before destruction? X-ray-induced changes in single-pulse serial femtosecond crystallography.
Iucrj, 12:358-371, 2025

PubMed Abstract: Serial femtosecond crystallography (SFX) exploits extremely brief X-ray free-electron laser pulses to obtain diffraction data before destruction of the crystal. However, during the pulse X-ray-induced site-specific radiation damage can occur, leading to electronic state and/or structural changes. Here, we present a systematic exploration of the effect of single-pulse duration and energy (and consequently different dose rates) on site-specific radiation damage under typical SFX room-temperature experimental conditions. For the first time in SFX we directly measured the photon pulse duration, varying from less than 10 fs to more than 50 fs, and used three pulse energies to probe in-pulse damage in two radiation-sensitive proteins: the iron-heme peroxidase DtpAa and the disulfide-rich thaumatin. While difference-map features arising from radiation damage are observed, they do not lead to significant change in refined atomic coordinates or key bond lengths. Our work thus provides experimental verification that average atomic coordinates are not significantly perturbed by radiation damage in typical SFX experiments.

PubMed: 40227256
DOI: 10.1107/S2052252525002660

実験手法

X-RAY DIFFRACTION (1.46 Å)