6S45

Room temperature structure of the dark state of the LOV2 domain of phototropin-2 from Arabidopsis thaliana determined with a serial crystallography approach

Summary for 6S45

• Entry DOI: 10.2210/pdb6s45/pdb
• Descriptor: Phototropin-2, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: lov domain, photoactive protein, flavoprotein, time-resolved crystallography, plant protein
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 1
• Total formula weight: 15464.25

Authors

Aumonier, S.,Santoni, G.,Gotthard, G.,von Stetten, D.,Leonard, G.,Royant, A. (deposition date: 2019-06-26, release date: 2020-07-08, Last modification date: 2024-01-24)

Primary citation

Aumonier, S.,Santoni, G.,Gotthard, G.,von Stetten, D.,Leonard, G.A.,Royant, A.
Millisecond time-resolved serial oscillation crystallography of a blue-light photoreceptor at a synchrotron.
Iucrj, 7:728-736, 2020

PubMed Abstract: The recent development of serial crystallography has popularized time-resolved crystallography as a technique to determine the structure of protein-reaction intermediate states. However, most approaches rely on the availability of thousands to millions of microcrystals. A method is reported here, using monochromatic synchrotron radiation, for the room-temperature collection, processing and merging of X-ray oscillation diffraction data from <100 samples in order to observe the build up of a photoreaction intermediate species. Using this method, we monitored with a time resolution of 63 ms how the population of a blue-light photoreceptor domain in a crystal progressively photoconverts from the dark to the light state. The series of resulting snapshots allows us to visualize in detail the gradual rearrangement of both the protein and chromophore during this process.

PubMed: 32695419
DOI: 10.1107/S2052252520007411

Experimental method

X-RAY DIFFRACTION (2.2 Å)