8BQN

Structure of empty Coxsackievirus A10 embedded in crystalline ice frozen at -140 degree

8BQN の概要

• エントリーDOI: 10.2210/pdb8bqn/pdb
• EMDBエントリー: 28627
• 分子名称: Capsid protein VP1, Capsid protein VP2, Capsid protein VP3 (3 entities in total)
• 機能のキーワード: coxsackievirus a10, empty coxsackievirus a10, crystalline ice, virus
• 由来する生物種: Coxsackievirus A10; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 87175.06

構造登録者

Shi, H.,Wu, C.,Zhang, X. (登録日: 2022-11-21, 公開日: 2023-01-11, 最終更新日: 2025-07-02)

主引用文献

Shi, H.,Wu, C.,Zhang, X.
Addressing compressive deformation of proteins embedded in crystalline ice.
Structure, 31:213-, 2023

PubMed Abstract: For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. Whether and how crystalline ice affects single-particle cryo-EM is still unclear. Here, single-particle cryo-EM was used to analyze three-dimensional structures of various proteins and viruses embedded in crystalline ice formed at various cooling rates. Low cooling rates led to shrinkage deformation and density distortions on samples having loose structures. Higher cooling rates reduced deformations. Deformation-free proteins in crystalline ice were obtained by modifying the freezing conditions, and reconstructions from these samples revealed a marked improvement over vitreous ice. This procedure also increased the efficiency of cryo-EM structure determinations and was essential for high-resolution reconstructions.

PubMed: 36586403
DOI: 10.1016/j.str.2022.12.001

実験手法

ELECTRON MICROSCOPY (3.1 Å)