6CL9

2.20 A MicroED structure of proteinase K at 4.3 e- / A^2

6CL9 の概要

• エントリーDOI: 10.2210/pdb6cl9/pdb
• EMDBエントリー: 7490 7491 7492 7493 7494
• 分子名称: Proteinase K (1 entity in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Parengyodontium album (Engyodontium album, Tritirachium album)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28930.78

構造登録者

Hattne, J.,Shi, D.,Glynn, C.,Zee, C.-T.,Gallagher-Jones, M.,Martynowycz, M.W.,Rodriguez, J.A.,Gonen, T. (登録日: 2018-03-02, 公開日: 2018-05-16, 最終更新日: 2024-10-23)

主引用文献

Hattne, J.,Shi, D.,Glynn, C.,Zee, C.T.,Gallagher-Jones, M.,Martynowycz, M.W.,Rodriguez, J.A.,Gonen, T.
Analysis of Global and Site-Specific Radiation Damage in Cryo-EM.
Structure, 26:759-766.e4, 2018

PubMed Abstract: Micro-crystal electron diffraction (MicroED) combines the efficiency of electron scattering with diffraction to allow structure determination from nano-sized crystalline samples in cryoelectron microscopy (cryo-EM). It has been used to solve structures of a diverse set of biomolecules and materials, in some cases to sub-atomic resolution. However, little is known about the damaging effects of the electron beam on samples during such measurements. We assess global and site-specific damage from electron radiation on nanocrystals of proteinase K and of a prion hepta-peptide and find that the dynamics of electron-induced damage follow well-established trends observed in X-ray crystallography. Metal ions are perturbed, disulfide bonds are broken, and acidic side chains are decarboxylated while the diffracted intensities decay exponentially with increasing exposure. A better understanding of radiation damage in MicroED improves our assessment and processing of all types of cryo-EM data.

PubMed: 29706530
DOI: 10.1016/j.str.2018.03.021

実験手法

ELECTRON CRYSTALLOGRAPHY (2.2 Å)