9F9E
Laser excitation effects on BR: Extrapolated 6 ps Light dataset recorded at 342 GW/cm2 at SwissFEL
9F9E の概要
エントリーDOI | 10.2210/pdb9f9e/pdb |
分子名称 | Bacteriorhodopsin, 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (5 entities in total) |
機能のキーワード | bacteriorhodospin, proton transport, membrane, retinal, time-resolved crystallography, serial crystallography, laser excitation |
由来する生物種 | Halobacterium salinarum 詳細 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 33931.76 |
構造登録者 | |
主引用文献 | Bertrand, Q.,Nogly, P.,Nango, E.,Kekilli, D.,Khusainov, G.,Furrer, A.,James, D.,Dworkowski, F.,Skopintsev, P.,Mous, S.,Martiel, I.,Borjesson, P.,Ortolani, G.,Huang, C.Y.,Kepa, M.,Ozerov, D.,Brunle, S.,Panneels, V.,Tanaka, T.,Tanaka, R.,Tono, K.,Owada, S.,Johnson, P.J.M.,Nass, K.,Knopp, G.,Cirelli, C.,Milne, C.,Schertler, G.,Iwata, S.,Neutze, R.,Weinert, T.,Standfuss, J. Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate. Nat Commun, 15:10278-10278, 2024 Cited by PubMed Abstract: Time-resolved serial crystallography at X-ray Free Electron Lasers offers the opportunity to observe ultrafast photochemical reactions at the atomic level. The technique has yielded exciting molecular insights into various biological processes including light sensing and photochemical energy conversion. However, to achieve sufficient levels of activation within an optically dense crystal, high laser power densities are often used, which has led to an ongoing debate to which extent photodamage may compromise interpretation of the results. Here we compare time-resolved serial crystallographic data of the bacteriorhodopsin K-intermediate collected at laser power densities ranging from 0.04 to 2493 GW/cm and follow energy dissipation of the absorbed photons logarithmically from picoseconds to milliseconds. Although the effects of high laser power densities on the overall structure are small, in the upper excitation range we observe significant changes in retinal conformation and increased heating of the functionally critical counterion cluster. We compare light-activation within crystals to that in solution and discuss the impact of the observed changes on bacteriorhodopsin biology. PubMed: 39604356DOI: 10.1038/s41467-024-54422-8 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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