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Lipidic cubic phase serial millisecond crystallography using synchrotron radiation

By Przemyslaw Nogly, Daniel James, Dingjie Wang, Thomas A. White, Nadia Zatsepin1, Anastasya Shilova, Garrett Charles Nelson1, Haiguang Liu1, Linda Johansson, Michael Heymann, Kathrin Jaeger, Markus Metz, Cecilia Wickstrand, Wenting Wu, Petra Båth, Peter Berntsen, Dominik Oberthuer, Valerie Panneels, Vadim Cherezov2, Henry Chapman3, Gebhard F.X. Schertler4, Richard Neutze, John Spence1, Isabel Moraes, Manfred Burghammer, Joerg Standfuss, Uwe Weierstall1

1. Arizona State University 2. Bridge Institute - University of Southern California 3. Center for Free-Electron Laser Science 4. ETH Zürich / Paul Scherrer Institut, Villigen Switzerland

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Category

BioXFEL Publications

Published on

Type

journal-article

Author

Przemyslaw Nogly and Daniel James and Dingjie Wang and Thomas A. White and Nadia Zatsepin and Anastasya Shilova and Garrett Nelson and Haiguang Liu and Linda Johansson and Michael Heymann and Kathrin Jaeger and Markus Metz and Cecilia Wickstrand and Wenting Wu and Petra Båth and Peter Berntsen and Dominik Oberthuer and Valerie Panneels and Vadim Cherezov and Henry Chapman and Gebhard Schertler and Richard Neutze and John Spence and Isabel Moraes and Manfred Burghammer and Joerg Standfuss and Uwe Weierstall

Citation

Nogly, P. et al., 2015. Lipidic cubic phase serial millisecond crystallography using synchrotron radiation. IUCrJ, 2(2), pp.168–176. Available at: http://dx.doi.org/10.1107/s2052252514026487.

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.

DOI

http://dx.doi.org/10.1107/s2052252514026487

Funding

NSF-STC Biology with X-ray Lasers (NSF-1231306)