9FX4

Crystal structure of Cryo2RT Thaumatin at 100K

9FX4 の概要

• エントリーDOI: 10.2210/pdb9fx4/pdb
• 分子名称: Thaumatin I, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: cryo2rt, synchrotron, room-temperature, protein, plant protein
• 由来する生物種: Thaumatococcus daniellii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25613.97

構造登録者

Huang, C.Y.,Aumonier, S.,Olieric, V.,Wang, M. (登録日: 2024-07-01, 公開日: 2024-07-31, 最終更新日: 2024-10-16)

主引用文献

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

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: 39052318
DOI: 10.1107/S2059798324006697

実験手法

X-RAY DIFFRACTION (1.59 Å)