7KUH

MicroED structure of mVDAC

Summary for 7KUH

• Entry DOI: 10.2210/pdb7kuh/pdb
• EMDB information: 23037
• Descriptor: Voltage-dependent anion-selective channel protein 1 (1 entity in total)
• Functional Keywords: channel, mammalian, voltage dependent, transport protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 1
• Total formula weight: 32195.88

Authors

Martynowycz, M.W.,Khan, F.,Hattne, J.,Abramson, J.,Gonen, T. (deposition date: 2020-11-25, release date: 2020-12-23, Last modification date: 2024-03-06)

Primary citation

Martynowycz, M.W.,Khan, F.,Hattne, J.,Abramson, J.,Gonen, T.
MicroED structure of lipid-embedded mammalian mitochondrial voltage-dependent anion channel.
Proc.Natl.Acad.Sci.USA, 117:32380-32385, 2020

PubMed Abstract: 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.

PubMed: 33293416
DOI: 10.1073/pnas.2020010117

Experimental method

ELECTRON CRYSTALLOGRAPHY (3.12 Å)