7KUH

MicroED structure of mVDAC

7KUH の概要

• エントリーDOI: 10.2210/pdb7kuh/pdb
• EMDBエントリー: 23037
• 分子名称: Voltage-dependent anion-selective channel protein 1 (1 entity in total)
• 機能のキーワード: channel, mammalian, voltage dependent, transport protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32195.88

構造登録者

Martynowycz, M.W.,Khan, F.,Hattne, J.,Abramson, J.,Gonen, T. (登録日: 2020-11-25, 公開日: 2020-12-23, 最終更新日: 2024-03-06)

主引用文献

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

実験手法

ELECTRON CRYSTALLOGRAPHY (3.12 Å)