8F49

1.8 angstrom structure of apoferritin embedded in crystalline ice

8F49 の概要

• エントリーDOI: 10.2210/pdb8f49/pdb
• EMDBエントリー: 32695
• 分子名称: Ferritin heavy chain (1 entity in total)
• 機能のキーワード: ferritin, crystal ice, crystalline ice, crystal-ice, apo-ferritin, human apo-ferritin, human ferritin, metal binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 482797.13

構造登録者

Shi, H.,Wu, C.,Zhang, X. (登録日: 2022-11-10, 公開日: 2023-01-11, 最終更新日: 2024-06-19)

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 (1.8 Å)