4V1W

3D structure of horse spleen apoferritin determined by electron cryomicroscopy

4V1W の概要

• エントリーDOI: 10.2210/pdb4v1w/pdb
• EMDBエントリー: 2788
• 分子名称: FERRITIN LIGHT CHAIN (1 entity in total)
• 機能のキーワード: storage protein, iron storage, iron transport, ferritins, apoferritins, horses, metals, spleen
• 由来する生物種: EQUUS CABALLUS (HORSE)
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 476938.27

構造登録者

Russo, C.J.,Passmore, L.A. (登録日: 2014-10-02, 公開日: 2014-12-10, 最終更新日: 2024-05-08)

主引用文献

Russo, C.J.,Passmore, L.A.
Electron Microscopy. Ultrastable Gold Substrates for Electron Cryomicroscopy.
Science, 346:1377-, 2014

PubMed Abstract: Despite recent advances, the structures of many proteins cannot be determined by electron cryomicroscopy because the individual proteins move during irradiation. This blurs the images so that they cannot be aligned with each other to calculate a three-dimensional density. Much of this movement stems from instabilities in the carbon substrates used to support frozen samples in the microscope. Here we demonstrate a gold specimen support that nearly eliminates substrate motion during irradiation. This increases the subnanometer image contrast such that α helices of individual proteins are resolved. With this improvement, we determine the structure of apoferritin, a smooth octahedral shell of α-helical subunits that is particularly difficult to solve by electron microscopy. This advance in substrate design will enable the solution of currently intractable protein structures.

PubMed: 25504723
DOI: 10.1126/SCIENCE.1259530

実験手法

ELECTRON MICROSCOPY (4.7 Å)