- EMDB-17995: Cryo-EM structure of mouse heavy-chain apoferritin -
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基本情報
登録情報
データベース: EMDB / ID: EMD-17995
タイトル
Cryo-EM structure of mouse heavy-chain apoferritin
マップデータ
Main sharpened and masked map
試料
複合体: Mouse heavy-chain apoferritin
タンパク質・ペプチド: Apoferritin
キーワード
apoferritin / METAL BINDING PROTEIN
機能・相同性
機能・相同性情報
Iron uptake and transport / Golgi Associated Vesicle Biogenesis / negative regulation of ferroptosis / iron ion sequestering activity / autolysosome / ferroxidase / intracellular sequestering of iron ion / ferroxidase activity / negative regulation of fibroblast proliferation / endocytic vesicle lumen ...Iron uptake and transport / Golgi Associated Vesicle Biogenesis / negative regulation of ferroptosis / iron ion sequestering activity / autolysosome / ferroxidase / intracellular sequestering of iron ion / ferroxidase activity / negative regulation of fibroblast proliferation / endocytic vesicle lumen / Neutrophil degranulation / ferric iron binding / ferrous iron binding / iron ion transport / iron ion binding / immune response / negative regulation of cell population proliferation / mitochondrion / extracellular region / identical protein binding / membrane / cytoplasm / cytosol 類似検索 - 分子機能
ジャーナル: Ultramicroscopy / 年: 2024 タイトル: Accurate magnification determination for cryoEM using gold. 著者: Joshua L Dickerson / Erin Leahy / Mathew J Peet / Katerina Naydenova / Christopher J Russo / 要旨: Determining the correct magnified pixel size of single-particle cryoEM micrographs is necessary to maximize resolution and enable accurate model building. Here we describe a simple and rapid ...Determining the correct magnified pixel size of single-particle cryoEM micrographs is necessary to maximize resolution and enable accurate model building. Here we describe a simple and rapid procedure for determining the absolute magnification in an electron cryomicroscope to a precision of <0.5%. We show how to use the atomic lattice spacings of crystals of thin and readily available test specimens, such as gold, as an absolute reference to determine magnification for both room temperature and cryogenic imaging. We compare this method to other commonly used methods, and show that it provides comparable accuracy in spite of its simplicity. This magnification calibration method provides a definitive reference quantity for data analysis and processing, simplifies the combination of multiple datasets from different microscopes and detectors, and improves the accuracy with which the contrast transfer function of the microscope can be determined. We also provide an open source program, magCalEM, which can be used to accurately estimate the magnified pixel size of a cryoEM dataset ex post facto.