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4H9F

Radiation damage study of lysozyme - 0.91 MGy

4H9F の概要
エントリーDOI10.2210/pdb4h9f/pdb
関連するPDBエントリー4H8X 4H8Y 4H8Z 4H90 4H91 4H92 4H93 4H94 4H9A 4H9B 4H9C 4H9E 4H9H 4H9I
分子名称Lysozyme C, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
機能のキーワードhydrolase
由来する生物種Gallus gallus (bantam,chickens)
細胞内の位置Secreted: P00698
タンパク質・核酸の鎖数1
化学式量合計14499.59
構造登録者
Sutton, K.A. (登録日: 2012-09-24, 公開日: 2013-05-15, 最終更新日: 2024-10-16)
主引用文献Sutton, K.A.,Black, P.J.,Mercer, K.R.,Garman, E.F.,Owen, R.L.,Snell, E.H.,Bernhard, W.A.
Insights into the mechanism of X-ray-induced disulfide-bond cleavage in lysozyme crystals based on EPR, optical absorption and X-ray diffraction studies.
Acta Crystallogr.,Sect.D, 69:2381-2394, 2013
Cited by
PubMed Abstract: Electron paramagnetic resonance (EPR) and online UV-visible absorption microspectrophotometry with X-ray crystallography have been used in a complementary manner to follow X-ray-induced disulfide-bond cleavage. Online UV-visible spectroscopy showed that upon X-irradiation, disulfide radicalization appeared to saturate at an absorbed dose of approximately 0.5-0.8 MGy, in contrast to the saturating dose of ∼0.2 MGy observed using EPR at much lower dose rates. The observations suggest that a multi-track model involving product formation owing to the interaction of two separate tracks is a valid model for radiation damage in protein crystals. The saturation levels are remarkably consistent given the widely different experimental parameters and the range of total absorbed doses studied. The results indicate that even at the lowest doses used for structural investigations disulfide bonds are already radicalized. Multi-track considerations offer the first step in a comprehensive model of radiation damage that could potentially lead to a combined computational and experimental approach to identifying when damage is likely to be present, to quantitate it and to provide the ability to recover the native unperturbed structure.
PubMed: 24311579
DOI: 10.1107/S0907444913022117
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.2003 Å)
構造検証レポート
Validation report summary of 4h9f
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-13に公開中

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