3V8A

Thaumatin by Classical Hanging Drop Vapour Diffusion after 18.1 MGy X-Ray dose at ESRF ID29 beamline (Worst Case)

3V8A の概要

• エントリーDOI: 10.2210/pdb3v8a/pdb
• 関連するPDBエントリー: 3ALD 3V7V 3V82 3V84 3V87 3V88 3VCE 3VCG 3VCH 3VCI 3VCJ 3VCK
• 分子名称: Thaumatin I, GLYCEROL (3 entities in total)
• 機能のキーワード: radiation damage, thin film, langmuir-blodgett, lb, plant protein
• 由来する生物種: Thaumatococcus daniellii (katemfe)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22596.42

構造登録者

Belmonte, L.,Scudieri, D.,Tripathi, S.,Pechkova, E.,Nicolini, C. (登録日: 2011-12-22, 公開日: 2012-11-07, 最終更新日: 2024-10-09)

主引用文献

Belmonte, L.,Pechkova, E.,Tripathi, S.,Scudieri, D.,Nicolini, C.
Langmuir-Blodgett nanotemplate and radiation resistance in protein crystals: state of the art.
CRIT.REV.EUKARYOT.GENE EXPR., 22:219-232, 2012

PubMed Abstract: A state-of-the-art review of the role of the Langmuir-Blodgett nanotemplate on protein crystal structures is here presented. Crystals grown by nanostructured template appear more radiation resistant than the classical ones, even in the presence of a third-generation highly focused beam at the European Synchrotron Radiation Facility. The electron density maps and the changes in parameters such as total diffractive power, B-factor, and pairwise R-factor have been discussed. Protein crystals, grown by the Langmuir-Blodgett nanotemplate-based method, proved to be more radiation resistant compared to crystals grown by the classical hanging drop method in terms of both global and specific damage.

PubMed: 23140163
DOI: 10.1615/CritRevEukarGeneExpr.v22.i3.50

実験手法

X-RAY DIFFRACTION (2.3 Å)