- EMDB-31910: 1.96 A structure of human apoferritin obtained from Talos Arctica... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-31910
タイトル
1.96 A structure of human apoferritin obtained from Talos Arctica microscope
マップデータ
試料
複合体: Human apoferritin
タンパク質・ペプチド: Ferritin heavy chain
リガンド: ZINC ION
リガンド: SODIUM ION
リガンド: water
キーワード
Apoferritin / STRUCTURAL PROTEIN
機能・相同性
機能・相同性情報
iron ion sequestering activity / : / autolysosome / Scavenging by Class A Receptors / Golgi Associated Vesicle Biogenesis / ferroxidase / intracellular sequestering of iron ion / ferroxidase activity / negative regulation of fibroblast proliferation / ferric iron binding ...iron ion sequestering activity / : / autolysosome / Scavenging by Class A Receptors / Golgi Associated Vesicle Biogenesis / ferroxidase / intracellular sequestering of iron ion / ferroxidase activity / negative regulation of fibroblast proliferation / ferric iron binding / Iron uptake and transport / ferrous iron binding / tertiary granule lumen / iron ion transport / intracellular iron ion homeostasis / ficolin-1-rich granule lumen / iron ion binding / immune response / negative regulation of cell population proliferation / Neutrophil degranulation / extracellular exosome / extracellular region / identical protein binding / membrane / nucleus / cytoplasm / cytosol 類似検索 - 分子機能
National Natural Science Foundation of China (NSFC)
31830020
中国
Chinese Academy of Sciences
XDB37040102
中国
National Natural Science Foundation of China (NSFC)
31925026
中国
Ministry of Science and Technology (MoST, China)
2015DFG32140
中国
引用
ジャーナル: Nat Commun / 年: 2021 タイトル: A cryo-electron microscopy support film formed by 2D crystals of hydrophobin HFBI. 著者: Hongcheng Fan / Bo Wang / Yan Zhang / Yun Zhu / Bo Song / Haijin Xu / Yujia Zhai / Mingqiang Qiao / Fei Sun / 要旨: Cryo-electron microscopy (cryo-EM) has become a powerful tool to resolve high-resolution structures of biomacromolecules in solution. However, air-water interface induced preferred orientations, ...Cryo-electron microscopy (cryo-EM) has become a powerful tool to resolve high-resolution structures of biomacromolecules in solution. However, air-water interface induced preferred orientations, dissociation or denaturation of biomacromolecules during cryo-vitrification remains a limiting factor for many specimens. To solve this bottleneck, we developed a cryo-EM support film using 2D crystals of hydrophobin HFBI. The hydrophilic side of the HFBI film adsorbs protein particles via electrostatic interactions and sequesters them from the air-water interface, allowing the formation of sufficiently thin ice for high-quality data collection. The particle orientation distribution can be regulated by adjusting the buffer pH. Using this support, we determined the cryo-EM structures of catalase (2.29 Å) and influenza haemagglutinin trimer (2.56 Å), which exhibited strong preferred orientations using a conventional cryo-vitrification protocol. We further show that the HFBI film is suitable to obtain high-resolution structures of small proteins, including aldolase (150 kDa, 3.28 Å) and haemoglobin (64 kDa, 3.6 Å). Our work suggests that HFBI films may have broad future applications in increasing the success rate and efficiency of cryo-EM.