6V20

Rabbit muscle aldolase determined using single-particle cryo-EM at 200 keV

6V20 の概要

• エントリーDOI: 10.2210/pdb6v20/pdb
• EMDBエントリー: 21023
• 分子名称: Fructose-bisphosphate aldolase A (2 entities in total)
• 機能のキーワード: homo-4-mer, lyase, d-fructose, glycolysis
• 由来する生物種: Oryctolagus cuniculus (Rabbit)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 149210.41

構造登録者

Wu, M.,Lander, G.C.,Herzik, M.A. (登録日: 2019-11-21, 公開日: 2020-02-12, 最終更新日: 2024-05-29)

主引用文献

Wu, M.,Lander, G.C.,Herzik Jr., M.A.
Sub-2 Angstrom resolution structure determination using single-particle cryo-EM at 200 keV.
J Struct Biol X, 4:100020-100020, 2020

PubMed Abstract: Although the advent of direct electron detectors (DEDs) and software developments have enabled the routine use of single-particle cryogenic electron microscopy (cryo-EM) for structure determination of well-behaved specimens to high-resolution, there nonetheless remains a discrepancy between the resolutions attained for biological specimens and the information limits of modern transmission electron microscopes (TEMs). Instruments operating at 300 kV equipped with DEDs are the current paradigm for high-resolution single-particle cryo-EM, while 200 kV TEMs remain comparatively underutilized for purposes beyond sample screening. Here, we expand upon our prior work and demonstrate that one such 200 kV microscope, the Talos Arctica, equipped with a K2 DED is capable of determining structures of macromolecules to as high as ∼1.7 Å resolution. At this resolution, ordered water molecules are readily assigned and holes in aromatic residues can be clearly distinguished in the reconstructions. This work emphasizes the utility of 200 kV electrons for high-resolution single-particle cryo-EM and applications such as structure-based drug design.

PubMed: 32647824
DOI: 10.1016/j.yjsbx.2020.100020

実験手法

ELECTRON MICROSCOPY (2.13 Å)