Megahertz data collection from protein microcrystals at an X-ray free-electron laser

Marie Luise Grünbein; Johan Bielecki; Alexander Gorel; Miriam Stricker; Richard Bean; Marco Cammarata; Katerina Dörner; Lars Fröhlich; Elisabeth Hartmann; Steffen Hauf; Mario Hilpert; Yoonhee Kim; Marco Kloos; Romain Letrun; Marc Messerschmidt; Grant Mills; Gabriela Nass Kovacs; Marco Ramilli; Christopher M. Roome; Tokushi Sato; Matthias Scholz; Michel Sliwa; Jolanta Sztuk-Dambietz; Martin Weik; Britta Weinhausen; Nasser Al-Qudami; Djelloul Boukhelef; Sandor Brockhauser; Wajid Ehsan; Moritz Emons; Sergey Esenov; Hans Fangohr; Alexander Kaukher; Thomas Kluyver; Max Lederer; Luis Maia; Maurizio Manetti; Thomas Michelat; Astrid Münnich; Florent Pallas; Guido Palmer; Gianpietro Previtali; Natascha Raab; Alessandro Silenzi; Janusz Szuba; Sandhya Venkatesan; Krzysztof Wrona; Jun Zhu; R. Bruce Doak; Robert L. Shoeman; Lutz Foucar; Jacques Philippe Colletier; Adrian P. Mancuso; Thomas R.M. Barends; Claudiu A. Stan; Ilme Schlichting

doi:10.1038/s41467-018-05953-4

Megahertz data collection from protein microcrystals at an X-ray free-electron laser

Marie Luise Grünbein, Johan Bielecki, Alexander Gorel, Miriam Stricker, Richard Bean, Marco Cammarata, Katerina Dörner, Lars Fröhlich, Elisabeth Hartmann, Steffen Hauf, Mario Hilpert, Yoonhee Kim, Marco Kloos, Romain Letrun, Marc Messerschmidt, Grant Mills, Gabriela Nass Kovacs, Marco Ramilli, Christopher M. Roome, Tokushi SatoMatthias Scholz, Michel Sliwa, Jolanta Sztuk-Dambietz, Martin Weik, Britta Weinhausen, Nasser Al-Qudami, Djelloul Boukhelef, Sandor Brockhauser, Wajid Ehsan, Moritz Emons, Sergey Esenov, Hans Fangohr, Alexander Kaukher, Thomas Kluyver, Max Lederer, Luis Maia, Maurizio Manetti, Thomas Michelat, Astrid Münnich, Florent Pallas, Guido Palmer, Gianpietro Previtali, Natascha Raab, Alessandro Silenzi, Janusz Szuba, Sandhya Venkatesan, Krzysztof Wrona, Jun Zhu, R. Bruce Doak, Robert L. Shoeman, Lutz Foucar, Jacques Philippe Colletier, Adrian P. Mancuso, Thomas R.M. Barends, Claudiu A. Stan, Ilme Schlichting

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

92 Scopus citations

Abstract

X-ray free-electron lasers (XFELs) enable novel experiments because of their high peak brilliance and femtosecond pulse duration. However, non-superconducting XFELs offer repetition rates of only 10–120 Hz, placing significant demands on beam time and sample consumption. We describe serial femtosecond crystallography experiments performed at the European XFEL, the first MHz repetition rate XFEL, delivering 1.128 MHz X-ray pulse trains at 10 Hz. Given the short spacing between pulses, damage caused by shock waves launched by one XFEL pulse on sample probed by subsequent pulses is a concern. To investigate this issue, we collected data from lysozyme microcrystals, exposed to a ~15 μm XFEL beam. Under these conditions, data quality is independent of whether the first or subsequent pulses of the train were used for data collection. We also analyzed a mixture of microcrystals of jack bean proteins, from which the structure of native, magnesium-containing concanavalin A was determined.

Original language	English (US)
Article number	3487
Journal	Nature communications
Volume	9
Issue number	1
DOIs	https://doi.org/10.1038/s41467-018-05953-4
State	Published - Dec 1 2018
Externally published	Yes

ASJC Scopus subject areas

General Chemistry
General Biochemistry, Genetics and Molecular Biology
General Physics and Astronomy

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Grünbein, M. L., Bielecki, J., Gorel, A., Stricker, M., Bean, R., Cammarata, M., Dörner, K., Fröhlich, L., Hartmann, E., Hauf, S., Hilpert, M., Kim, Y., Kloos, M., Letrun, R., Messerschmidt, M., Mills, G., Nass Kovacs, G., Ramilli, M., Roome, C. M., ... Schlichting, I. (2018). Megahertz data collection from protein microcrystals at an X-ray free-electron laser. Nature communications, 9(1), Article 3487. https://doi.org/10.1038/s41467-018-05953-4

Grünbein, ML, Bielecki, J, Gorel, A, Stricker, M, Bean, R, Cammarata, M, Dörner, K, Fröhlich, L, Hartmann, E, Hauf, S, Hilpert, M, Kim, Y, Kloos, M, Letrun, R, Messerschmidt, M, Mills, G, Nass Kovacs, G, Ramilli, M, Roome, CM, Sato, T, Scholz, M, Sliwa, M, Sztuk-Dambietz, J, Weik, M, Weinhausen, B, Al-Qudami, N, Boukhelef, D, Brockhauser, S, Ehsan, W, Emons, M, Esenov, S, Fangohr, H, Kaukher, A, Kluyver, T, Lederer, M, Maia, L, Manetti, M, Michelat, T, Münnich, A, Pallas, F, Palmer, G, Previtali, G, Raab, N, Silenzi, A, Szuba, J, Venkatesan, S, Wrona, K, Zhu, J, Doak, RB, Shoeman, RL, Foucar, L, Colletier, JP, Mancuso, AP, Barends, TRM, Stan, CA & Schlichting, I 2018, 'Megahertz data collection from protein microcrystals at an X-ray free-electron laser', Nature communications, vol. 9, no. 1, 3487. https://doi.org/10.1038/s41467-018-05953-4

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title = "Megahertz data collection from protein microcrystals at an X-ray free-electron laser",

abstract = "X-ray free-electron lasers (XFELs) enable novel experiments because of their high peak brilliance and femtosecond pulse duration. However, non-superconducting XFELs offer repetition rates of only 10–120 Hz, placing significant demands on beam time and sample consumption. We describe serial femtosecond crystallography experiments performed at the European XFEL, the first MHz repetition rate XFEL, delivering 1.128 MHz X-ray pulse trains at 10 Hz. Given the short spacing between pulses, damage caused by shock waves launched by one XFEL pulse on sample probed by subsequent pulses is a concern. To investigate this issue, we collected data from lysozyme microcrystals, exposed to a ~15 μm XFEL beam. Under these conditions, data quality is independent of whether the first or subsequent pulses of the train were used for data collection. We also analyzed a mixture of microcrystals of jack bean proteins, from which the structure of native, magnesium-containing concanavalin A was determined.",

author = "Gr{\"u}nbein, {Marie Luise} and Johan Bielecki and Alexander Gorel and Miriam Stricker and Richard Bean and Marco Cammarata and Katerina D{\"o}rner and Lars Fr{\"o}hlich and Elisabeth Hartmann and Steffen Hauf and Mario Hilpert and Yoonhee Kim and Marco Kloos and Romain Letrun and Marc Messerschmidt and Grant Mills and {Nass Kovacs}, Gabriela and Marco Ramilli and Roome, {Christopher M.} and Tokushi Sato and Matthias Scholz and Michel Sliwa and Jolanta Sztuk-Dambietz and Martin Weik and Britta Weinhausen and Nasser Al-Qudami and Djelloul Boukhelef and Sandor Brockhauser and Wajid Ehsan and Moritz Emons and Sergey Esenov and Hans Fangohr and Alexander Kaukher and Thomas Kluyver and Max Lederer and Luis Maia and Maurizio Manetti and Thomas Michelat and Astrid M{\"u}nnich and Florent Pallas and Guido Palmer and Gianpietro Previtali and Natascha Raab and Alessandro Silenzi and Janusz Szuba and Sandhya Venkatesan and Krzysztof Wrona and Jun Zhu and Doak, {R. Bruce} and Shoeman, {Robert L.} and Lutz Foucar and Colletier, {Jacques Philippe} and Mancuso, {Adrian P.} and Barends, {Thomas R.M.} and Stan, {Claudiu A.} and Ilme Schlichting",

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AU - Grünbein, Marie Luise

AU - Bielecki, Johan

AU - Gorel, Alexander

AU - Stricker, Miriam

AU - Bean, Richard

AU - Cammarata, Marco

AU - Dörner, Katerina

AU - Fröhlich, Lars

AU - Hartmann, Elisabeth

AU - Hauf, Steffen

AU - Hilpert, Mario

AU - Kim, Yoonhee

AU - Kloos, Marco

AU - Letrun, Romain

AU - Messerschmidt, Marc

AU - Mills, Grant

AU - Nass Kovacs, Gabriela

AU - Ramilli, Marco

AU - Roome, Christopher M.

AU - Sato, Tokushi

AU - Scholz, Matthias

AU - Sliwa, Michel

AU - Sztuk-Dambietz, Jolanta

AU - Weik, Martin

AU - Weinhausen, Britta

AU - Al-Qudami, Nasser

AU - Boukhelef, Djelloul

AU - Brockhauser, Sandor

AU - Ehsan, Wajid

AU - Emons, Moritz

AU - Esenov, Sergey

AU - Fangohr, Hans

AU - Kaukher, Alexander

AU - Kluyver, Thomas

AU - Lederer, Max

AU - Maia, Luis

AU - Manetti, Maurizio

AU - Michelat, Thomas

AU - Münnich, Astrid

AU - Pallas, Florent

AU - Palmer, Guido

AU - Previtali, Gianpietro

AU - Raab, Natascha

AU - Silenzi, Alessandro

AU - Szuba, Janusz

AU - Venkatesan, Sandhya

AU - Wrona, Krzysztof

AU - Zhu, Jun

AU - Doak, R. Bruce

AU - Shoeman, Robert L.

AU - Foucar, Lutz

AU - Colletier, Jacques Philippe

AU - Mancuso, Adrian P.

AU - Barends, Thomas R.M.

AU - Stan, Claudiu A.

AU - Schlichting, Ilme

PY - 2018/12/1

Y1 - 2018/12/1

N2 - X-ray free-electron lasers (XFELs) enable novel experiments because of their high peak brilliance and femtosecond pulse duration. However, non-superconducting XFELs offer repetition rates of only 10–120 Hz, placing significant demands on beam time and sample consumption. We describe serial femtosecond crystallography experiments performed at the European XFEL, the first MHz repetition rate XFEL, delivering 1.128 MHz X-ray pulse trains at 10 Hz. Given the short spacing between pulses, damage caused by shock waves launched by one XFEL pulse on sample probed by subsequent pulses is a concern. To investigate this issue, we collected data from lysozyme microcrystals, exposed to a ~15 μm XFEL beam. Under these conditions, data quality is independent of whether the first or subsequent pulses of the train were used for data collection. We also analyzed a mixture of microcrystals of jack bean proteins, from which the structure of native, magnesium-containing concanavalin A was determined.

AB - X-ray free-electron lasers (XFELs) enable novel experiments because of their high peak brilliance and femtosecond pulse duration. However, non-superconducting XFELs offer repetition rates of only 10–120 Hz, placing significant demands on beam time and sample consumption. We describe serial femtosecond crystallography experiments performed at the European XFEL, the first MHz repetition rate XFEL, delivering 1.128 MHz X-ray pulse trains at 10 Hz. Given the short spacing between pulses, damage caused by shock waves launched by one XFEL pulse on sample probed by subsequent pulses is a concern. To investigate this issue, we collected data from lysozyme microcrystals, exposed to a ~15 μm XFEL beam. Under these conditions, data quality is independent of whether the first or subsequent pulses of the train were used for data collection. We also analyzed a mixture of microcrystals of jack bean proteins, from which the structure of native, magnesium-containing concanavalin A was determined.

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Megahertz data collection from protein microcrystals at an X-ray free-electron laser

Abstract

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