Lipidic cubic phase serial millisecond crystallography using synchrotron radiation

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

doi:10.1107/S2052252514026487

Lipidic cubic phase serial millisecond crystallography using synchrotron radiation

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

Research output: Contribution to journal › Article › peer-review

164 Scopus citations

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.

Original language	English (US)
Pages (from-to)	168-176
Number of pages	9
Journal	IUCrJ
Volume	2
DOIs	https://doi.org/10.1107/S2052252514026487
State	Published - Feb 26 2015

Keywords

XFEL
bacteriorhodopsin
lipidic cubic phases
protein crystallography

ASJC Scopus subject areas

Chemistry(all)
Biochemistry
Materials Science(all)
Condensed Matter Physics

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10.1107/S2052252514026487

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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., Båth, P., Berntsen, P., Oberthuer, D., Panneels, V., Cherezov, V., ... Weierstall, U. (2015). Lipidic cubic phase serial millisecond crystallography using synchrotron radiation. IUCrJ, 2, 168-176. https://doi.org/10.1107/S2052252514026487

Nogly, P, James, D, Wang, D, White, TA, Zatsepin, N, Shilova, A, Nelson, G, Liu, H, Johansson, L, Heymann, M, Jaeger, K, Metz, M, Wickstrand, C, Wu, W, Båth, 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 2015, 'Lipidic cubic phase serial millisecond crystallography using synchrotron radiation', IUCrJ, vol. 2, pp. 168-176. https://doi.org/10.1107/S2052252514026487

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title = "Lipidic cubic phase serial millisecond crystallography using synchrotron radiation",

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±{\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.",

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author = "Przemyslaw Nogly and Daniel James and Dingjie Wang and White, {Thomas A.} 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 B{\aa}th 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",

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AU - Nogly, Przemyslaw

AU - James, Daniel

AU - Wang, Dingjie

AU - White, Thomas A.

AU - Zatsepin, Nadia

AU - Shilova, Anastasya

AU - Nelson, Garrett

AU - Liu, Haiguang

AU - Johansson, Linda

AU - Heymann, Michael

AU - Jaeger, Kathrin

AU - Metz, Markus

AU - Wickstrand, Cecilia

AU - Wu, Wenting

AU - Båth, Petra

AU - Berntsen, Peter

AU - Oberthuer, Dominik

AU - Panneels, Valerie

AU - Cherezov, Vadim

AU - Chapman, Henry

AU - Schertler, Gebhard

AU - Neutze, Richard

AU - Spence, John

AU - Moraes, Isabel

AU - Burghammer, Manfred

AU - Standfuss, Joerg

AU - Weierstall, Uwe

PY - 2015/2/26

Y1 - 2015/2/26

N2 - 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.

AB - 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.

KW - XFEL

KW - bacteriorhodopsin

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KW - protein crystallography

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Lipidic cubic phase serial millisecond crystallography using synchrotron radiation

Abstract

Keywords

ASJC Scopus subject areas

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