5AVH
The 0.90 angstrom structure (I222) of glucose isomerase crystallized in high-strength agarose hydrogel
5AVH の概要
エントリーDOI | 10.2210/pdb5avh/pdb |
関連するPDBエントリー | 5AVD 5AVG |
分子名称 | Xylose isomerase (2 entities in total) |
機能のキーワード | xylose isomerase, hydrogel, isomerase |
由来する生物種 | Streptomyces rubiginosus |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 43095.06 |
構造登録者 | Sugiyama, S.,Shimizu, N.,Maruyama, N.,Sazaki, G.,Adachi, H.,Takano, K.,Murakami, S.,Inoue, T.,Mori, Y.,Matsumura, H. (登録日: 2015-06-16, 公開日: 2015-07-08, 最終更新日: 2024-03-20) |
主引用文献 | Sugiyama, S.,Maruyama, M.,Sazaki, G.,Hirose, M.,Adachi, H.,Takano, K.,Murakami, S.,Inoue, T.,Mori, Y.,Matsumura, H. Growth of protein crystals in hydrogels prevents osmotic shock J.Am.Chem.Soc., 134:5786-5789, 2012 Cited by PubMed Abstract: High-throughput protein X-ray crystallography offers a significant opportunity to facilitate drug discovery. The most reliable approach is to determine the three-dimensional structure of the protein-ligand complex by soaking the ligand in apo crystals. However, protein apo crystals produced by conventional crystallization in a solution are fatally damaged by osmotic shock during soaking. To overcome this difficulty, we present a novel technique for growing protein crystals in a high-concentration hydrogel that is completely gellified and exhibits high strength. This technique allowed us essentially to increase the mechanical stability of the crystals, preventing serious damage to the crystals caused by osmotic shock. Thus, this method may accelerate structure-based drug discoveries. PubMed: 22435400DOI: 10.1021/ja301584y 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (0.9 Å) |
構造検証レポート
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