1LY0
Structure of thaumatin crystallized in the presence of glycerol
1LY0 の概要
| エントリーDOI | 10.2210/pdb1ly0/pdb |
| 関連するPDBエントリー | 1LXZ |
| 分子名称 | Thaumatin I, L(+)-TARTARIC ACID (3 entities in total) |
| 機能のキーワード | taste-modifying protein, sweet protein, plant protein |
| 由来する生物種 | Thaumatococcus daniellii (miracle fruit) |
| 細胞内の位置 | Cytoplasmic vesicle: P02883 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 22377.15 |
| 構造登録者 | Charron, C.,Kadri, A.,Robert, M.C.,Giege, R.,Lorber, B. (登録日: 2002-06-06, 公開日: 2003-01-14, 最終更新日: 2024-11-20) |
| 主引用文献 | Charron, C.,Kadri, A.,Robert, M.C.,Giege, R.,Lorber, B. Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin. Acta Crystallogr.,Sect.D, 58:2060-2065, 2002 Cited by PubMed Abstract: The intensely sweet protein thaumatin has been crystallized at 293 K in the presence of sodium tartrate and 25%(v/v) glycerol for X-ray diffraction data collection at 100 K. A comparison of the three-dimensional structure model derived from a crystal grown in the presence of glycerol with that of a control deprived of this additive reveals only minor changes in the overall structure but a approximately 20% reduction in the number of water molecules. X-ray topography analyses show that the overall quality of the crystals prepared in the presence of this cryoprotectant is enhanced. PubMed: 12454465DOI: 10.1107/S0907444902017183 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.36 Å) |
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