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7ZY3

Room temperature structure of Archaerhodopsin-3 obtained 110 ns after photoexcitation

Summary for 7ZY3
Entry DOI10.2210/pdb7zy3/pdb
DescriptorArchaerhodopsin-3, RETINAL, nonane, ... (10 entities in total)
Functional Keywordsmembrane protein, proton tranport, rhodopsin, lipidic cubic phase, sfx, proton transport
Biological sourceHalorubrum sodomense
Total number of polymer chains1
Total formula weight28448.33
Authors
Kwan, T.O.C.,Judge, P.J.,Moraes, I.,Watts, A.,Axford, D.,Bada Juarez, J.F. (deposition date: 2022-05-23, release date: 2023-06-14, Last modification date: 2024-11-20)
Primary citationBirch, J.,Kwan, T.O.C.,Judge, P.J.,Axford, D.,Aller, P.,Butryn, A.,Reis, R.I.,Bada Juarez, J.F.,Vinals, J.,Owen, R.L.,Nango, E.,Tanaka, R.,Tono, K.,Joti, Y.,Tanaka, T.,Owada, S.,Sugahara, M.,Iwata, S.,Orville, A.M.,Watts, A.,Moraes, I.
A versatile approach to high-density microcrystals in lipidic cubic phase for room-temperature serial crystallography.
J.Appl.Crystallogr., 56:1361-1370, 2023
Cited by
PubMed Abstract: Serial crystallography has emerged as an important tool for structural studies of integral membrane proteins. The ability to collect data from micrometre-sized weakly diffracting crystals at room temperature with minimal radiation damage has opened many new opportunities in time-resolved studies and drug discovery. However, the production of integral membrane protein microcrystals in lipidic cubic phase at the desired crystal density and quantity is challenging. This paper introduces VIALS (versatile approach to high-density microcrystals in lipidic cubic phase for serial crystallography), a simple, fast and efficient method for preparing hundreds of microlitres of high-density microcrystals suitable for serial X-ray diffraction experiments at both synchrotron and free-electron laser sources. The method is also of great benefit for rational structure-based drug design as it facilitates crystal soaking and rapid determination of many co-crystal structures. Using the VIALS approach, room-temperature structures are reported of (i) the archaerhodopsin-3 protein in its dark-adapted state and 110 ns photocycle intermediate, determined to 2.2 and 1.7 Å, respectively, and (ii) the human A adenosine receptor in complex with two different ligands determined to a resolution of 3.5 Å.
PubMed: 37791355
DOI: 10.1107/S1600576723006428
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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