Correlation Engine 2.0
Clear Search sequence regions

  • electron (8)
  • ion (2)
  • lipids (4)
  • mice (1)
  • mutant protein (1)
  • VDAC (6)
  • Sizes of these terms reflect their relevance to your search.

    A structure of the murine voltage-dependent anion channel (VDAC) was determined by microcrystal electron diffraction (MicroED). Microcrystals of an essential mutant of VDAC grew in a viscous bicelle suspension, making it unsuitable for conventional X-ray crystallography. Thin, plate-like crystals were identified using scanning-electron microscopy (SEM). Crystals were milled into thin lamellae using a focused-ion beam (FIB). MicroED data were collected from three crystal lamellae and merged for completeness. The refined structure revealed unmodeled densities between protein monomers, indicative of lipids that likely mediate contacts between the proteins in the crystal. This body of work demonstrates the effectiveness of milling membrane protein microcrystals grown in viscous media using a focused ion beam for subsequent structure determination by MicroED. This approach is well suited for samples that are intractable by X-ray crystallography. To our knowledge, the presented structure is a previously undescribed mutant of the membrane protein VDAC, crystallized in a lipid bicelle matrix and solved by MicroED.


    Michael W Martynowycz, Farha Khan, Johan Hattne, Jeff Abramson, Tamir Gonen. MicroED structure of lipid-embedded mammalian mitochondrial voltage-dependent anion channel. Proceedings of the National Academy of Sciences of the United States of America. 2020 Dec 22;117(51):32380-32385

    Expand section icon Mesh Tags

    Expand section icon Substances

    PMID: 33293416

    View Full Text