4X31

Room temperature structure of bacteriorhodopsin from lipidic cubic phase obtained with serial millisecond crystallography using synchrotron radiation

4X31 の概要

• エントリーDOI: 10.2210/pdb4x31/pdb
• 分子名称: Bacteriorhodopsin, RETINAL, 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL, ... (4 entities in total)
• 機能のキーワード: light-driven proton pump, seven transmembrane helix protein, room temperature structure, retinal-binding protein, proton transport
• 由来する生物種: Halobacterium salinarum
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P02945
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28541.70

構造登録者

Nogly, P.,James, D.,Wang, D.,White, T.,Zatsepin, N.,Shilova, A.,Nelson, G.,Liu, H.,Johansson, L.,Heymann, M.,Jaeger, K.,Metz, M.,Wickstrand, C.,Wu, W.,Baath, P.,Berntsen, P.,Oberthuer, D.,Panneels, V.,Cherezov, V.,Chapman, H.,Spence, J.,Schertler, G.,Neutze, R.,Moraes, I.,Burghammer, M.,Standfuss, J.,Weierstall, U. (登録日: 2014-11-27, 公開日: 2015-02-18, 最終更新日: 2024-10-23)

主引用文献

Nogly, P.,James, D.,Wang, D.,White, T.A.,Zatsepin, N.,Shilova, A.,Nelson, G.,Liu, H.,Johansson, L.,Heymann, M.,Jaeger, K.,Metz, M.,Wickstrand, C.,Wu, W.,Bath, P.,Berntsen, P.,Oberthuer, D.,Panneels, V.,Cherezov, V.,Chapman, H.,Schertler, G.,Neutze, R.,Spence, J.,Moraes, I.,Burghammer, M.,Standfuss, J.,Weierstall, U.
Lipidic cubic phase serial millisecond crystallography using synchrotron radiation.
Iucrj, 2:168-176, 2015

PubMed Abstract: Lipidic cubic phases (LCPs) have emerged as successful matrixes for the crystallization of membrane proteins. Moreover, the viscous LCP also provides a highly effective delivery medium for serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs). Here, the adaptation of this technology to perform serial millisecond crystallography (SMX) at more widely available synchrotron microfocus beamlines is described. Compared with conventional microcrystallography, LCP-SMX eliminates the need for difficult handling of individual crystals and allows for data collection at room temperature. The technology is demonstrated by solving a structure of the light-driven proton-pump bacteriorhodopsin (bR) at a resolution of 2.4 Å. The room-temperature structure of bR is very similar to previous cryogenic structures but shows small yet distinct differences in the retinal ligand and proton-transfer pathway.

PubMed: 25866654
DOI: 10.1107/S2052252514026487

実験手法

X-RAY DIFFRACTION (2.4 Å)