9T6W

Higher-dose (260.0 kGy) structure of horse-heart myoglobin at room temperature

9T6W の概要

• エントリーDOI: 10.2210/pdb9t6w/pdb
• 関連するPDBエントリー: 9T6V 9T6X 9T6Y
• 分子名称: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: myo, myoglobin, radiation damage, room-temperature crystallography, metalloproteins, oxidoreductase
• 由来する生物種: Equus caballus (horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17731.20

構造登録者

Caramello, N.,Rose, S.L.,Engilberge, S.,Royant, A. (登録日: 2025-11-07, 公開日: 2026-03-04, 最終更新日: 2026-03-11)

主引用文献

Caramello, N.,Rose, S.L.,Mathieu, E.,Petit, L.,Tews, I.,Engilberge, S.,Royant, A.
Coupled on-line in crystallo UV-Vis absorption spectroscopy and X-ray crystallography to compare specific radiation damage in metal-containing proteins at room versus cryogenic temperature.
Acta Crystallogr D Struct Biol, 82:187-198, 2026

PubMed Abstract: Specific radiation damage (SRD) to proteins is a pertinent issue discovered during the development of cryo-crystallography at synchrotrons, often affecting the macromolecular active site and thus complicating the understanding of mechanistic insights from structural analysis. For proteins with a spectroscopic signature in the visible light spectrum, in crystallo UV-Vis absorption spectroscopy has regularly been used to estimate the dose scale of specific damage build-up and to develop diffraction data-collection strategies to mitigate its effects. Using a coupled spectroscopic and crystallographic approach, here we show that for two metal-containing proteins the structural response to X-ray-induced reduction of metals in their active site is markedly different at room temperature than at cryogenic temperature. This suggests that the use of controlled specific radiation damage to mimic and study a physiological redox transition in a metal-containing protein by X-ray crystallography should preferably be performed at room temperature rather than at cryogenic temperature.

PubMed: 41641581
DOI: 10.1107/S2059798326000690

実験手法

X-RAY DIFFRACTION (1.71 Å)