%0 Journal Article %1 Nogly2015 %A Nogly, Przemyslaw %A James, Daniel %A Wang, Dingjie %A White, Thomas a. %A Zatsepin, Nadia %A Shilova, Anastasya %A Nelson, Garrett %A Liu, Haiguang %A Johansson, Linda %A Heymann, Michael %A Jaeger, Kathrin %A Metz, Markus %A Wickstrand, Cecilia %A Wu, Wenting %A B\aath, Petra %A Berntsen, Peter %A Oberthuer, Dominik %A Panneels, Valerie %A Cherezov, Vadim %A Chapman, Henry %A Schertler, Gebhard %A Neutze, Richard %A Spence, John %A Moraes, Isabel %A Burghammer, Manfred %A Standfuss, Joerg %A Weierstall, Uwe %D 2015 %J IUCrJ %K myown %N 2 %P 168--176 %R 10.1107/S2052252514026487 %T Lipidic cubic phase serial millisecond crystallography using synchrotron radiation %U http://scripts.iucr.org/cgi-bin/paper?S2052252514026487 %V 2 %X \textlessp\textgreaterLipidic 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 \AA. 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.\textless/p\textgreater

@article{Nogly2015, abstract = {{\textless}p{\textgreater}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 {\AA}. 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.{\textless}/p{\textgreater}}, added-at = {2019-11-28T11:57:04.000+0100}, author = {Nogly, Przemyslaw and James, Daniel and Wang, Dingjie and White, Thomas a. and Zatsepin, Nadia and Shilova, Anastasya and Nelson, Garrett and Liu, Haiguang and Johansson, Linda and Heymann, Michael and Jaeger, Kathrin and Metz, Markus and Wickstrand, Cecilia and Wu, Wenting and B{\aa}th, Petra and Berntsen, Peter and Oberthuer, Dominik and Panneels, Valerie and Cherezov, Vadim and Chapman, Henry and Schertler, Gebhard and Neutze, Richard and Spence, John and Moraes, Isabel and Burghammer, Manfred and Standfuss, Joerg and Weierstall, Uwe}, biburl = {https://puma.ub.uni-stuttgart.de/bibtex/22ffe4307aa33e6d64bffd38bf30f9125/michaelheymann}, doi = {10.1107/S2052252514026487}, file = {:Users/mh/Documents/Mendeley Desktop/Nogly et al/2015/Nogly et al.{\_}2015{\_}Lipidic cubic phase serial millisecond crystallography using synchrotron radiation.pdf:pdf}, interhash = {d87f484ff24bc1f3387271b1d3b0b2d4}, intrahash = {2ffe4307aa33e6d64bffd38bf30f9125}, issn = {2052-2525}, journal = {IUCrJ}, keywords = {myown}, number = 2, pages = {168--176}, timestamp = {2019-11-28T12:55:04.000+0100}, title = {{Lipidic cubic phase serial millisecond crystallography using synchrotron radiation}}, url = {http://scripts.iucr.org/cgi-bin/paper?S2052252514026487}, volume = 2, year = 2015 }