5AVG
The 0.95 angstrom structure of thaumatin crystallized in high-strength agarose hydrogel
Summary for 5AVG
| Entry DOI | 10.2210/pdb5avg/pdb |
| Related | 5AVD 5AVH |
| Descriptor | Thaumatin-1 (2 entities in total) |
| Functional Keywords | thaumatin, high-strength agarose, hydrogel, plant protein |
| Biological source | Thaumatococcus daniellii (Katemfe) |
| Total number of polymer chains | 1 |
| Total formula weight | 22155.98 |
| Authors | Sugiyama, S.,Shimizu, N.,Maruyama, M.,Sazaki, G.,Hirose, M.,Adachi, H.,Takano, K.,Murakami, S.,Inoue, T.,Mori, Y.,Matsumura, H. (deposition date: 2015-06-16, release date: 2015-07-08, Last modification date: 2024-11-20) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.95 Å) |
Structure validation
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