6NBB

Horse liver alcohol dehydrogenase determined using single-particle cryo-EM at 200 keV

6NBB の概要

• エントリーDOI: 10.2210/pdb6nbb/pdb
• EMDBエントリー: 0406
• 分子名称: Alcohol dehydrogenase E chain, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ZINC ION (3 entities in total)
• 機能のキーワード: dehydrogenase, nadh-binding, homo-2-mer, oxidoreductase
• 由来する生物種: Equus caballus (Horse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81295.03

構造登録者

Herzik Jr., M.A.,Wu, M.,Lander, G.C. (登録日: 2018-12-06, 公開日: 2019-03-13, 最終更新日: 2024-10-30)

主引用文献

Herzik Jr., M.A.,Wu, M.,Lander, G.C.
High-resolution structure determination of sub-100 kDa complexes using conventional cryo-EM.
Nat Commun, 10:1032-1032, 2019

PubMed Abstract: Determining high-resolution structures of biological macromolecules amassing less than 100 kilodaltons (kDa) has been a longstanding goal of the cryo-electron microscopy (cryo-EM) community. While the Volta phase plate has enabled visualization of specimens in this size range, this instrumentation is not yet fully automated and can present technical challenges. Here, we show that conventional defocus-based cryo-EM methodologies can be used to determine high-resolution structures of specimens amassing less than 100 kDa using a transmission electron microscope operating at 200 keV coupled with a direct electron detector. Our ~2.7 Å structure of alcohol dehydrogenase (82 kDa) proves that bound ligands can be resolved with high fidelity to enable investigation of drug-target interactions. Our ~2.8 Å and ~3.2 Å structures of methemoglobin demonstrate that distinct conformational states can be identified within a dataset for proteins as small as 64 kDa. Furthermore, we provide the sub-nanometer cryo-EM structure of a sub-50 kDa protein.

PubMed: 30833564
DOI: 10.1038/s41467-019-08991-8

実験手法

ELECTRON MICROSCOPY (2.9 Å)