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-Structure paper
タイトル | MicroED structure of lipid-embedded mammalian mitochondrial voltage-dependent anion channel. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 117, Issue 51, Page 32380-32385, Year 2020 |
掲載日 | 2020年12月22日 |
![]() | Michael W Martynowycz / Farha Khan / Johan Hattne / Jeff Abramson / Tamir Gonen / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (電子線結晶学) |
解像度 | 3.12 Å |
構造データ | EMDB-23037, PDB-7kuh: |
由来 |
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![]() | TRANSPORT PROTEIN / Channel / mammalian / voltage dependent |