6QQF

Room temperature structure of Hen Egg White Lysozyme recorded after an accumulated dose of 100 kGy

6QQF の概要

• エントリーDOI: 10.2210/pdb6qqf/pdb
• 分子名称: Lysozyme C, CHLORIDE ION (3 entities in total)
• 機能のキーワード: lysozyme, disulphide bonds, radiation damage, hydrolase
• 由来する生物種: Gallus gallus (Chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14402.07

構造登録者

Gotthard, G.,Aumonier, S.,Royant, A. (登録日: 2019-02-18, 公開日: 2019-06-19, 最終更新日: 2024-10-16)

主引用文献

Gotthard, G.,Aumonier, S.,De Sanctis, D.,Leonard, G.,von Stetten, D.,Royant, A.
Specific radiation damage is a lesser concern at room temperature.
Iucrj, 6:665-680, 2019

PubMed Abstract: Carrying out macromolecular crystallography (MX) experiments at cryogenic temperatures significantly slows the rate of global radiation damage, thus facilitating the solution of high-resolution crystal structures of macromolecules. However, cryo-MX experiments suffer from the early onset of so-called specific radiation damage that affects certain amino-acid residues and, in particular, the active sites of many proteins. Here, a series of MX experiments are described which suggest that specific and global radiation damage are much less decoupled at room temperature than they are at cryogenic temperatures. The results reported here demonstrate the interest in reviving the practice of collecting MX diffraction data at room temperature and allow structural biologists to favourably envisage the development of time-resolved MX experiments at synchrotron sources.

PubMed: 31316810
DOI: 10.1107/S205225251900616X

実験手法

X-RAY DIFFRACTION (1.95 Å)