Cryoelectron tomography articles within Nature Communications

Featured

• Article
  06 April 2016 | Open Access

  Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein

  Lysenin is member of the aerolysin family of small ß-barrel pore-forming toxins that include virulence factors from several human and animal pathogens. Here the authors determine the structure of the lysenin pore by single particle cryo- EM and propose a conserved pore formation mechanism for the aerolysin protein family.

  • Monika Bokori-Brown
  • , Thomas G. Martin
  •  & Christos G. Savva

• Article
  11 December 2015 | Open Access

  Structure of a bacterial type III secretion system in contact with a host membrane in situ

  Bacterial type III secretion systems (T3SSs) inject virulence effector proteins into eukaryotic cells and are activated by host membrane contact. Here the authors report the in situ structure of the Chlamydia trachomatisT3SS in the presence or absence of host membrane, and observe compaction of the basal body embedded in the bacterial envelope.

  • Andrea Nans
  • , Mikhail Kudryashev
  •  & Richard D. Hayward

• Article
  17 November 2015 | Open Access

  Direct visualization of dispersed lipid bicontinuous cubic phases by cryo-electron tomography

  Dispersed lipid self-assembly can form various types of particles, including cubosomes, which are useful for drug delivery. Here, Demurtas et al. visualize their three-dimensional structure, showing two continuous water channels separated by lipid bilayers and the mechanism of particle stabilization.

  • Davide Demurtas
  • , Paul Guichard
  •  & Laurent Sagalowicz

• Article | 22 January 2015

  Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography

  While the cytosolic translation machinery is well characterized, the mitochondrial translation system remains largely elusive. Using cryo-electron tomography, Pfeffer et al. describe the ordered organization of mitochondrial polysomes in which each ribosome is tethered to the inner membrane by two defined contacts on the large subunit in situ.

  • Stefan Pfeffer
  • , Michael W. Woellhaf
  •  & Friedrich Förster

• Article | 04 December 2014

  Cryo-electron tomography reveals ciliary defects underlying human RSPH1 primary ciliary dyskinesia

  Our current understanding of cilia biology and ciliary diseases is incomplete, in part because cilia are hard to visualize. Here, the authors use cryo-electron tomography to image the structure of human cilia with high resolution and uncover the elusive ciliary defects in Primary Ciliary Dyskinesia patients.

  • Jianfeng Lin
  • , Weining Yin
  •  & Daniela Nicastro

• Article
  19 June 2014 | Open Access

  Visualizing active membrane protein complexes by electron cryotomography

  Few tools are available to identify active membrane proteins within their native lipid environment. Here, Gold et al. report on a strategy that can be used for site-specific labelling of membrane proteins via electron cryotomography.

  • Vicki A.M. Gold
  • , Raffaele Ieva
  •  & Werner Kühlbrandt