9FX4
Crystal structure of Cryo2RT Thaumatin at 100K
Summary for 9FX4
| Entry DOI | 10.2210/pdb9fx4/pdb |
| Descriptor | Thaumatin I, L(+)-TARTARIC ACID (3 entities in total) |
| Functional Keywords | cryo2rt, synchrotron, room-temperature, protein, plant protein |
| Biological source | Thaumatococcus daniellii |
| Total number of polymer chains | 1 |
| Total formula weight | 25613.97 |
| Authors | Huang, C.Y.,Aumonier, S.,Olieric, V.,Wang, M. (deposition date: 2024-07-01, release date: 2024-07-31, Last modification date: 2024-10-16) |
| Primary citation | Huang, C.Y.,Aumonier, S.,Olieric, V.,Wang, M. Cryo2RT: a high-throughput method for room-temperature macromolecular crystallography from cryo-cooled crystals. Acta Crystallogr D Struct Biol, 80:620-628, 2024 Cited by PubMed Abstract: Advances in structural biology have relied heavily on synchrotron cryo-crystallography and cryogenic electron microscopy to elucidate biological processes and for drug discovery. However, disparities between cryogenic and room-temperature (RT) crystal structures pose challenges. Here, Cryo2RT, a high-throughput RT data-collection method from cryo-cooled crystals that leverages the cryo-crystallography workflow, is introduced. Tested on endothiapepsin crystals with four soaked fragments, thaumatin and SARS-CoV-2 3CL, Cryo2RT reveals unique ligand-binding poses, offers a comparable throughput to cryo-crystallography and eases the exploration of structural dynamics at various temperatures. PubMed: 39052318DOI: 10.1107/S2059798324006697 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.59 Å) |
Structure validation
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