6COA

1.2 A Structure of Thaumatin Crystallized in Gel

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6COA の概要

• エントリーDOI: 10.2210/pdb6coa/pdb
• 関連するPDBエントリー: 1THU 1THV 1THW
• 分子名称: Thaumatin-1, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: sweet tasting protein, agarose gel, microgravity, apcf, 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: 22377.15

構造登録者

Sauter, C.,Lorber, B.,Shabalin, I.G.,Porebski, P.J.,Brzezinski, D.,Giege, R. (登録日: 2018-03-12, 公開日: 2018-03-28, 最終更新日: 2024-10-30)

主引用文献

Sauter, C.,Lorber, B.,Giege, R.
Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature.
Proteins, 48:146-150, 2002

PubMed Abstract: One reason for introducing a gel in the crystallization medium of proteins is its ability to reduce convection in solution. This can lead to better nucleation and growth conditions, and to crystals having enhanced diffraction properties. We report here the X-ray characterization at room temperature of high-quality crystals of the intensely sweet thaumatin prepared in a sodium tartrate solution gelified with 0.15% (m/v) agarose. Using a synchrotron radiation, these crystals diffracted to a previously unachieved resolution. A diffraction dataset was collected from four crystals at a resolution of 1.2 A with a R(sym) of 3.6% and a completeness of 99%. Refinement was carried out to a final crystallographic R-factor of 12.0%. The quality of the electron density map allowed for the observation of fine structural details in the protein and its solvation shell. Crystallization in gel might be used more generally to improve the quality of macromolecular crystals. Advantages provided by the gelified medium in the frame of structural studies are emphasized.

PubMed: 12112683
DOI: 10.1002/prot.10125

実験手法

X-RAY DIFFRACTION (1.2 Å)