In extracto cryo-EM reveals eEF2 as a major hibernation factor on 60S and 80S particles
· 2026-09-03 · 原文
Cryogenic electron microscopy (cryo-EM) made impressive progress in resolving cellular macromolecules and their detailed interactions. Single-particle cryo-EM traditionally relies on purified macromolecules and lacks the complexity of cellular environments, whereas in situ cryo-EM and cryogenic electron tomography (cryo-ET) require extensive sample preparation and data acquisition, presenting challenges in achieving high resolution. We describe cryo-EM of cellular lysates— in extracto cryo-EM—allowing the flexibility and high-resolution of cryo-EM in the context of cellular components. High-resolution 2D template matching (2DTM) yields ~2.2 Å maps of the mammalian translational apparatus. Elongating ribosome abundances in primate cell lines (MCF-7 and BSC-1) and rabbit reticulocyte lysates
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1. 人话版
Cryogenic electron microscopy (cryo-EM) made impressive progress in resolving cellular macromolecules and their detailed interactions.
Single-particle cryo-EM traditionally relies on purified macromolecules and lacks the complexity of cellular environments, whereas in situ cryo-EM and cryogenic electron tomography (cryo-ET) require extensive sample preparation and data acquisition, presenting challenges in achieving high resolution.
2. 领域脉络
We describe cryo-EM of cellular lysates— in extracto cryo-EM—allowing the flexibility and high-resolution of cryo-EM in the context of cellular components.
3. 机制拆解
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4. 证据与数字
High-resolution 2D template matching (2DTM) yields ~2.2 Å maps of the mammalian translational apparatus.
Elongating ribosome abundances in primate cell lines (MCF-7 and BSC-1) and rabbit reticulocyte lysates
5. 反例与边界
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