Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein

Jason Tenboer; Shibom Basu; Nadia Zatsepin; Kanupriya Pande; Despina Milathianaki; Matthias Frank; Mark Hunter; Sébastien Boutet; Garth J. Williams; Jason E. Koglin; Dominik Oberthuer; Michael Heymann; Christopher Kupitz; Chelsie Conrad; Jesse Coe; Shatabdi Roy-Chowdhury; Uwe Weierstall; Daniel James; Dingjie Wang; Thomas Grant; Anton Barty; Oleksandr Yefanov; Jennifer Scales; Cornelius Gati; Carolin Seuring; Vukica Srajer; Robert Henning; Peter Schwander; Raimund Fromme; Abbas Ourmazd; Keith Moffat; Jasper J. Van Thor; John Spence; Petra Fromme; Henry N. Chapman; Marius Schmidt

doi:10.1126/science.1259357

Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein

Jason Tenboer, Shibom Basu, Nadia Zatsepin, Kanupriya Pande, Despina Milathianaki, Matthias Frank, Mark Hunter, Sébastien Boutet, Garth J. Williams, Jason E. Koglin, Dominik Oberthuer, Michael Heymann, Christopher Kupitz, Chelsie Conrad, Jesse Coe, Shatabdi Roy-Chowdhury, Uwe Weierstall, Daniel James, Dingjie Wang, Thomas GrantAnton Barty, Oleksandr Yefanov, Jennifer Scales, Cornelius Gati, Carolin Seuring, Vukica Srajer, Robert Henning, Peter Schwander, Raimund Fromme, Abbas Ourmazd, Keith Moffat, Jasper J. Van Thor, John Spence, Petra Fromme, Henry N. Chapman, Marius Schmidt

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

380 Scopus citations

Abstract

Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics of biomolecules. We used microcrystals of photoactive yellow protein (a bacterial blue light photoreceptor) as a model system and obtained high-resolution, time-resolved difference electron density maps of excellent quality with strong features; these allowed the determination of structures of reaction intermediates to a resolution of 1.6 angstroms. Our results open the way to the study of reversible and nonreversible biological reactions on time scales as short as femtoseconds under conditions that maximize the extent of reaction initiation throughout the crystal.

Original language	English (US)
Pages (from-to)	1242-1246
Number of pages	5
Journal	Science
Volume	346
Issue number	6214
DOIs	https://doi.org/10.1126/science.1259357
State	Published - Dec 5 2014

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Tenboer, J., Basu, S., Zatsepin, N., Pande, K., Milathianaki, D., Frank, M., Hunter, M., Boutet, S., Williams, G. J., Koglin, J. E., Oberthuer, D., Heymann, M., Kupitz, C., Conrad, C., Coe, J., Roy-Chowdhury, S., Weierstall, U., James, D., Wang, D., ... Schmidt, M. (2014). Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein. Science, 346(6214), 1242-1246. https://doi.org/10.1126/science.1259357

Tenboer, J, Basu, S, Zatsepin, N, Pande, K, Milathianaki, D, Frank, M, Hunter, M, Boutet, S, Williams, GJ, Koglin, JE, Oberthuer, D, Heymann, M, Kupitz, C, Conrad, C, Coe, J, Roy-Chowdhury, S, Weierstall, U, James, D, Wang, D, Grant, T, Barty, A, Yefanov, O, Scales, J, Gati, C, Seuring, C, Srajer, V, Henning, R, Schwander, P, Fromme, R, Ourmazd, A, Moffat, K, Van Thor, JJ, Spence, J, Fromme, P, Chapman, HN & Schmidt, M 2014, 'Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein', Science, vol. 346, no. 6214, pp. 1242-1246. https://doi.org/10.1126/science.1259357

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title = "Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein",

abstract = "Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics of biomolecules. We used microcrystals of photoactive yellow protein (a bacterial blue light photoreceptor) as a model system and obtained high-resolution, time-resolved difference electron density maps of excellent quality with strong features; these allowed the determination of structures of reaction intermediates to a resolution of 1.6 angstroms. Our results open the way to the study of reversible and nonreversible biological reactions on time scales as short as femtoseconds under conditions that maximize the extent of reaction initiation throughout the crystal.",

author = "Jason Tenboer and Shibom Basu and Nadia Zatsepin and Kanupriya Pande and Despina Milathianaki and Matthias Frank and Mark Hunter and S{\'e}bastien Boutet and Williams, {Garth J.} and Koglin, {Jason E.} and Dominik Oberthuer and Michael Heymann and Christopher Kupitz and Chelsie Conrad and Jesse Coe and Shatabdi Roy-Chowdhury and Uwe Weierstall and Daniel James and Dingjie Wang and Thomas Grant and Anton Barty and Oleksandr Yefanov and Jennifer Scales and Cornelius Gati and Carolin Seuring and Vukica Srajer and Robert Henning and Peter Schwander and Raimund Fromme and Abbas Ourmazd and Keith Moffat and {Van Thor}, {Jasper J.} and John Spence and Petra Fromme and Chapman, {Henry N.} and Marius Schmidt",

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AU - Zatsepin, Nadia

AU - Pande, Kanupriya

AU - Milathianaki, Despina

AU - Frank, Matthias

AU - Hunter, Mark

AU - Boutet, Sébastien

AU - Williams, Garth J.

AU - Koglin, Jason E.

AU - Oberthuer, Dominik

AU - Heymann, Michael

AU - Kupitz, Christopher

AU - Conrad, Chelsie

AU - Coe, Jesse

AU - Roy-Chowdhury, Shatabdi

AU - Weierstall, Uwe

AU - James, Daniel

AU - Wang, Dingjie

AU - Grant, Thomas

AU - Barty, Anton

AU - Yefanov, Oleksandr

AU - Scales, Jennifer

AU - Gati, Cornelius

AU - Seuring, Carolin

AU - Srajer, Vukica

AU - Henning, Robert

AU - Schwander, Peter

AU - Fromme, Raimund

AU - Ourmazd, Abbas

AU - Moffat, Keith

AU - Van Thor, Jasper J.

AU - Spence, John

AU - Fromme, Petra

AU - Chapman, Henry N.

AU - Schmidt, Marius

PY - 2014/12/5

Y1 - 2014/12/5

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AB - Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics of biomolecules. We used microcrystals of photoactive yellow protein (a bacterial blue light photoreceptor) as a model system and obtained high-resolution, time-resolved difference electron density maps of excellent quality with strong features; these allowed the determination of structures of reaction intermediates to a resolution of 1.6 angstroms. Our results open the way to the study of reversible and nonreversible biological reactions on time scales as short as femtoseconds under conditions that maximize the extent of reaction initiation throughout the crystal.

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Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein

Abstract

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Time Resolved Serial Femtosecond Crystallography Captures High Resolution Intermediates of PYP

Time Resolved Serial Femtosecond Crystallography Captures High Resolution Intermediates of PYP

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Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein

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Time Resolved Serial Femtosecond Crystallography Captures High Resolution Intermediates of PYP

Time Resolved Serial Femtosecond Crystallography Captures High Resolution Intermediates of PYP

Cite this