Cryoelectron microscopy

Cryoelectron microscopy is a method for imaging frozen-hydrated specimens at cryogenic temperatures by electron microscopy. Specimens remain in their native state without the need for dyes or fixatives, allowing the study of fine cellular structures, viruses and protein complexes at molecular resolution.

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Latest Research and Reviews

  • Research
    | Open Access

    The E46K α-synuclein mutation causes familial Parkinson’s disease. Here, the authors present the cryo-EM structure of N-terminally acetylated E46K α-synuclein fibrils and find that it is distinct from other known α-synuclein fibril structures.

    • Kun Zhao
    • , Yaowang Li
    • , Zhenying Liu
    • , Houfang Long
    • , Chunyu Zhao
    • , Feng Luo
    • , Yunpeng Sun
    • , Youqi Tao
    • , Xiao-dong Su
    • , Dan Li
    • , Xueming Li
    •  & Cong Liu
  • Research
    | Open Access

    F1Fo ATP synthase consists of two coupled rotary molecular motors: the soluble ATPase F1 and the transmembrane Fo. Here, the authors present cryo-EM structures of E. coli ATP synthase in four discrete rotational sub-states at 3.1-3.4 Å resolution and observe a rotary sub-step of the Fo motor cring that reveals the mechanism of elastic coupling between the two rotary motors, which is essential for effective ATP synthesis.

    • Meghna Sobti
    • , James L. Walshe
    • , Di Wu
    • , Robert Ishmukhametov
    • , Yi C. Zeng
    • , Carol V. Robinson
    • , Richard M. Berry
    •  & Alastair G. Stewart
  • Research |

    RuBisCO is believed to be the most abundant enzyme on earth, and catalyses a critical step in carbon fixation. Assisted by different assembly factors, including Raf1, RuBisCO assembles into the holoenzyme comprising eight large subunits (RbcL) and eight small subunits (RbcS). Here, the researchers resolve high-resolution protein structures of the cyanobacterial RuBisCO octameric complex that reflect different steps of its assembly.

    • Ling-Yun Xia
    • , Yong-Liang Jiang
    • , Wen-Wen Kong
    • , Hui Sun
    • , Wei-Fang Li
    • , Yuxing Chen
    •  & Cong-Zhao Zhou
  • Research
    | Open Access

    There is a need to further improve the automation of cryo-EM sample preparation to make it more easily accessible for non-specialists, reduce sample waste and increase reproducibility. Here, the authors present VitroJet, a single device, where sub-nl volumes of samples are deposited by pin printing thus eliminating the need for sample blotting, which is followed by jet vitrification, and they show that high-resolution structures can be obtained using four standard proteins.

    • Raimond B. G. Ravelli
    • , Frank J. T. Nijpels
    • , Rene J. M. Henderikx
    • , Giulia Weissenberger
    • , Sanne Thewessem
    • , Abril Gijsbers
    • , Bart W. A. M. M. Beulen
    • , Carmen López-Iglesias
    •  & Peter J. Peters
  • Research |

    Cryo-electron microscopy reveals the structures of the mitochondrial calcium uniporter holocomplex in low- and high-calcium conditions, showing the gating mechanism that underlies uniporter activation in response to intracellular calcium signals.

    • Minrui Fan
    • , Jinru Zhang
    • , Chen-Wei Tsai
    • , Benjamin J. Orlando
    • , Madison Rodriguez
    • , Yan Xu
    • , Maofu Liao
    • , Ming-Feng Tsai
    •  & Liang Feng
    Nature, 1-5

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