9C8V

Human DNA polymerase alpha/primase - CHAPSO (4 mM)

9C8V の概要

• エントリーDOI: 10.2210/pdb9c8v/pdb
• 関連するPDBエントリー: 8VY3
• EMDBエントリー: 43627
• 分子名称: DNA primase small subunit, DNA primase large subunit, DNA polymerase alpha catalytic subunit, ... (6 entities in total)
• 機能のキーワード: human dna poly alpha/primase, chapso, replication
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 277624.90

構造登録者

Abe, K.M.,Li, G.,He, Q.,Grant, T.,Lim, C. (登録日: 2024-06-13, 公開日: 2024-09-04, 最終更新日: 2024-12-18)

主引用文献

Abe, K.M.,Li, G.,He, Q.,Grant, T.,Lim, C.J.
Small LEA proteins mitigate air-water interface damage to fragile cryo-EM samples during plunge freezing.
Nat Commun, 15:7705-7705, 2024

PubMed Abstract: Air-water interface (AWI) interactions during cryo-electron microscopy (cryo-EM) sample preparation cause significant sample loss, hindering structural biology research. Organisms like nematodes and tardigrades produce Late Embryogenesis Abundant (LEA) proteins to withstand desiccation stress. Here we show that these LEA proteins, when used as additives during plunge freezing, effectively mitigate AWI damage to fragile multi-subunit molecular samples. The resulting high-resolution cryo-EM maps are comparable to or better than those obtained using existing AWI damage mitigation methods. Cryogenic electron tomography reveals that particles are localized at specific interfaces, suggesting LEA proteins form a barrier at the AWI. This interaction may explain the observed sample-dependent preferred orientation of particles. LEA proteins offer a simple, cost-effective, and adaptable approach for cryo-EM structural biologists to overcome AWI-related sample damage, potentially revitalizing challenging projects and advancing the field of structural biology.

PubMed: 39231985
DOI: 10.1038/s41467-024-52091-1

実験手法

ELECTRON MICROSCOPY (3.39 Å)