6QQH
Cryogenic temperature structure of the ground state of AtPhot2LOV2 recorded after an accumulated dose of 2.68 MGy
Summary for 6QQH
| Entry DOI | 10.2210/pdb6qqh/pdb |
| Descriptor | Phototropin-2, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | room temperature macromolecular crystallography, cryo-crystallography, specific radiation damage, time-resolved crystallography, plant protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 15464.25 |
| Authors | Aumonier, S.,Gotthard, G.,Royant, A. (deposition date: 2019-02-18, release date: 2019-06-19, Last modification date: 2024-01-24) |
| Primary citation | Gotthard, G.,Aumonier, S.,De Sanctis, D.,Leonard, G.,von Stetten, D.,Royant, A. Specific radiation damage is a lesser concern at room temperature. Iucrj, 6:665-680, 2019 Cited by PubMed Abstract: Carrying out macromolecular crystallography (MX) experiments at cryogenic temperatures significantly slows the rate of global radiation damage, thus facilitating the solution of high-resolution crystal structures of macromolecules. However, cryo-MX experiments suffer from the early onset of so-called specific radiation damage that affects certain amino-acid residues and, in particular, the active sites of many proteins. Here, a series of MX experiments are described which suggest that specific and global radiation damage are much less decoupled at room temperature than they are at cryogenic temperatures. The results reported here demonstrate the interest in reviving the practice of collecting MX diffraction data at room temperature and allow structural biologists to favourably envisage the development of time-resolved MX experiments at synchrotron sources. PubMed: 31316810DOI: 10.1107/S205225251900616X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.38 Å) |
Structure validation
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