Cryoelectron tomography

Cryo-electron tomography (also cryo-ET or electron cryotomography) is a technique where an electron microscope is used to record a series of two-dimensional images as a biological sample held at cryogenic temperatures is tilted. Using computational methods, the two-dimensional images can be aligned to yield a three-dimensional (tomographic) reconstruction of the sample.

Latest Research and Reviews

  • Research |

    A combination of electron cryotomography and immunofluorescence microscopy reveals the structure of the core transmembrane subcomplex of the Legionella defective in organelle trafficking (Dot)/intracellular multiplication (Icm) type IVB secretion system (T4BSS) and an early-stage assembly process by which T4BSS components are targeted to the bacterial poles by DotU and IcmF.

    • Debnath Ghosal
    • , Kwangcheol C. Jeong
    • , Yi-Wei Chang
    • , Jacob Gyore
    • , Lin Teng
    • , Adam Gardner
    • , Joseph P. Vogel
    •  & Grant J. Jensen
  • Research |

    Clustered protocadherin ectodomains spontaneously assemble to form a zipper-like lattice of alternating cis and trans interactions at membrane contact sites, which probably represents their mode of function in neuronal self-recognition.

    • Julia Brasch
    • , Kerry M. Goodman
    • , Alex J. Noble
    • , Micah Rapp
    • , Seetha Mannepalli
    • , Fabiana Bahna
    • , Venkata P. Dandey
    • , Tristan Bepler
    • , Bonnie Berger
    • , Tom Maniatis
    • , Clinton S. Potter
    • , Bridget Carragher
    • , Barry Honig
    •  & Lawrence Shapiro
    Nature 569, 280-283
  • Research | | open

    Bacteria use contractile injection systems, such as type VI secretion systems (T6SS), to secrete proteins that mediate cell-cell interactions. Here, Szwedziak & Pilhofer show that both ends of a T6SS can attach to opposite sides of the cell, enabling the structure to contract in two opposite directions.

    • Piotr Szwedziak
    •  & Martin Pilhofer
  • Research | | open

    Microtubules in cilia are sufficiently stable to withstand the beating motion, but how they are stabilized while serving as tracks for intraflagellar transport and axonemal dyneins remains unknown. Here authors identify two microtubule inner proteins, FAP45 and FAP52, which stabilize the ciliary axonemes in Chlamydomonas.

    • Mikito Owa
    • , Takayuki Uchihashi
    • , Haru-aki Yanagisawa
    • , Takashi Yamano
    • , Hiro Iguchi
    • , Hideya Fukuzawa
    • , Ken-ichi Wakabayashi
    • , Toshio Ando
    •  & Masahide Kikkawa
  • Research | | open

    Lipid membrane fusion is an essential function in many biological processes but little is known about membrane fusion in prokaryotes. The authors here study how haloarchaeal pleomorphic viruses (HRPVs) infect archaeal hosts. The structure-function analysis of the spike proteins shed light on prokaryotic membrane fusion.

    • Kamel El Omari
    • , Sai Li
    • , Abhay Kotecha
    • , Thomas S. Walter
    • , Eduardo A. Bignon
    • , Karl Harlos
    • , Pentti Somerharju
    • , Felix De Haas
    • , Daniel K. Clare
    • , Mika Molin
    • , Felipe Hurtado
    • , Mengqiu Li
    • , Jonathan M. Grimes
    • , Dennis H. Bamford
    • , Nicole D. Tischler
    • , Juha T. Huiskonen
    • , David I. Stuart
    •  & Elina Roine

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