Showing 1 - 12 results of 12 for search '"Cryo Electron Tomography"', query time: 0.05s Refine Results
  1. 1

    Cryo-electron tomography pipeline for plasma membranes by Willy W. Sun, Dennis J. Michalak, Kem A. Sochacki, Prasanthi Kunamaneni, Marco A. Alfonzo-Méndez, Andreas M. Arnold, Marie-Paule Strub, Jenny E. Hinshaw, Justin W. Taraska

    Published 2025-01-01
    “…Abstract Cryo-electron tomography (cryoET) provides sub-nanometer protein structure within the dense cellular environment. …”
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  2. 2

    MPicker: visualizing and picking membrane proteins for cryo-electron tomography by Xiaofeng Yan, Shudong Li, Weilin Huang, Hao Wang, Tianfang Zhao, Mingtao Huang, Niyun Zhou, Yuan Shen, Xueming Li

    Published 2025-01-01
    “…Abstract Advancements in cryo-electron tomography (cryoET) allow the structure of macromolecules to be determined in situ, which is crucial for studying membrane protein structures and their interactions in the cellular environment. …”
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  3. 3

    The big chill: Growth of in situ structural biology with cryo-electron tomography by Mikhail Kudryashev

    Published 2024-01-01
    “…In situ structural biology with cryo-electron tomography (cryo-ET) and subtomogram averaging (StA) is evolving as a major method to understand the structure, function, and interactions of biological molecules in cells in a single experiment. …”
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  4. 4

    Protocol for estimating the contrast transfer function and absolute tilt angle offset for cryo-electron tomography using CTFMeasure by Ranhao Zhang, Yuan Shen, Xueming Li

    Published 2025-03-01
    “…Summary: Contrast transfer function (CTF) estimation is essential to the data processing workflow of cryo-electron tomography (cryoET). Here, we present a protocol for CTF estimation of the cryoET tilt series with CTFMeasure. …”
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    Rapid structural analysis of bacterial ribosomes in situ by Barrett M. Powell, Tyler S. Brant, Joseph H. Davis, Shyamal Mosalaganti

    Published 2025-01-01
    “…In contrast, analogous structural analysis in cells via cryo-electron tomography (cryo-ET) remains challenging due to critical technical bottlenecks, including low-throughput sample preparation and imaging, and laborious data processing methods. …”
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  7. 7

    Size-controlled assembly of phase separated protein condensates with interfacial protein cages by Hyeok Jin Oh, Yongsuk Lee, Haerang Hwang, Kibeom Hong, Hyeongjoo Choi, Jin Young Kang, Yongwon Jung

    Published 2025-01-01
    “…In addition, the 3D structures of intact protein condensates with interfacial cages are visualized with cryo-electron tomography (ET). This work offers a versatile platform for designing size-controlled, surface-engineered protein condensate materials.…”
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  8. 8

    Dynamics of the mammalian pyruvate dehydrogenase complex revealed by in-situ structural analysis by Chen Wang, Cheng Ma, Yuanyou Xu, Shenghai Chang, Hangjun Wu, Chunlan Yan, Jinghua Chen, Yongping Wu, Shaoya An, Jiaqi Xu, Qin Han, Yujie Jiang, Zhinong Jiang, Xiakun Chu, Haichun Gao, Xing Zhang, Yunjie Chang

    Published 2025-01-01
    “…Here, we report the in-situ architecture of intact mammalian PDHc by cryo-electron tomography. The organization of peripheral E1 and E3 components varies substantially among the observed PDHcs, with an average of 21 E1 surrounding each PDHc core, and up to 12 E3 locating primarily along the pentagonal openings. …”
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    A single residue switch mediates the broad neutralization of Rotaviruses by Yang Huang, Feibo Song, Yuanjun Zeng, Hui Sun, Roufang Sheng, Xuechun Wang, Liqin Liu, Guoxing Luo, Yanan Jiang, Yaling Chen, Mengxuan Zhang, Shiyin Zhang, Ying Gu, Hai Yu, Shaowei Li, Tingdong Li, Qingbing Zheng, Shengxiang Ge, Jun Zhang, Ningshao Xia

    Published 2025-01-01
    “…A combination of time-resolved cryo-electron microscopy (cryo-EM) and in situ cryo-electron tomography (cryo-ET) analysis reveals a counterintuitive dynamic process of virus inactivation, in which 7H13 asymmetrically binds to a conserved epitope in the capsid-proximal aspect of VP4, triggers a conformational switch in a critical residue—F418—thereby disrupts the meta-stable conformation of VP4 essential for normal viral infection. …”
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