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Serial femtosecond and serial synchrotron crystallography yield data of equivalent quality: a systematic comparison

View ORCID ProfileP. Mehrabi, View ORCID ProfileR. Bücker, G. Bourenkov, H.M. Ginn, View ORCID ProfileD. von Stetten, View ORCID ProfileH.M. Müller-Werkmeister, A. Kuo, T. Morizumi, B.T. Eger, W.-L. Ou, S. Oghbaey, A. Sarracini, J.E. Besaw, O. Paré-Labrosse, S. Meier, H. Schikora, View ORCID ProfileF. Tellkamp, A. Marx, D.A. Sherrell, D. Axford, View ORCID ProfileR. Owen, O.P. Ernst, View ORCID ProfileE.F. Pai, View ORCID ProfileE.C. Schulz, R.J.D. Miller
doi: https://doi.org/10.1101/2020.08.21.257170
P. Mehrabi
1Department for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany
2Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, Ontario, M5G 1L7, Canada
12The Campbell Family Cancer Research Institute, Ontario, Cancer Institute, 101 College Street, Toronto, Ontario, M5G 1L7, Canada
13Center for Free-Electron Laser Science, Luruper Chaussee 149, 22761 Hamburg, Germany
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  • ORCID record for P. Mehrabi
  • For correspondence: pedram.Mehrabi@mpsd.mpg.de eike.schulz@mpsd.mpg.de
R. Bücker
1Department for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany
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G. Bourenkov
3European Molecular Biology Laboratory (EMBL), Hamburg Outstation c/o Deutsches Elektronen Synchrotron (DESY), Notkestrasse 85, D-22603 Hamburg, Germany
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H.M. Ginn
4Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK
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D. von Stetten
3European Molecular Biology Laboratory (EMBL), Hamburg Outstation c/o Deutsches Elektronen Synchrotron (DESY), Notkestrasse 85, D-22603 Hamburg, Germany
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H.M. Müller-Werkmeister
4Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK
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  • ORCID record for H.M. Müller-Werkmeister
A. Kuo
6Department of Biochemistry, University of Toronto, 1 King’s College Circle, Toronto, Ontario, M5S 1A8, Canada
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T. Morizumi
6Department of Biochemistry, University of Toronto, 1 King’s College Circle, Toronto, Ontario, M5S 1A8, Canada
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B.T. Eger
6Department of Biochemistry, University of Toronto, 1 King’s College Circle, Toronto, Ontario, M5S 1A8, Canada
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W.-L. Ou
6Department of Biochemistry, University of Toronto, 1 King’s College Circle, Toronto, Ontario, M5S 1A8, Canada
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S. Oghbaey
7Departments of Chemistry and Physics, University of Toronto, 80 St. George Street, Toronto, Ontario, M5S 3H6, Canada
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A. Sarracini
7Departments of Chemistry and Physics, University of Toronto, 80 St. George Street, Toronto, Ontario, M5S 3H6, Canada
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J.E. Besaw
6Department of Biochemistry, University of Toronto, 1 King’s College Circle, Toronto, Ontario, M5S 1A8, Canada
7Departments of Chemistry and Physics, University of Toronto, 80 St. George Street, Toronto, Ontario, M5S 3H6, Canada
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O. Paré-Labrosse
1Department for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany
7Departments of Chemistry and Physics, University of Toronto, 80 St. George Street, Toronto, Ontario, M5S 3H6, Canada
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S. Meier
8Department of Physics, Universität Hamburg, Jungiusstrasse 9, 20355 Hamburg, Germany
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H. Schikora
9Scientific Support Unit Machine Physics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany
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F. Tellkamp
9Scientific Support Unit Machine Physics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany
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A. Marx
1Department for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany
13Center for Free-Electron Laser Science, Luruper Chaussee 149, 22761 Hamburg, Germany
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D.A. Sherrell
4Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK
10Structural Biology Center, X-ray Science Division, Argonne National Laboratory, Argonne, IL, USA
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D. Axford
4Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK
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R. Owen
4Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, UK
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  • ORCID record for R. Owen
O.P. Ernst
6Department of Biochemistry, University of Toronto, 1 King’s College Circle, Toronto, Ontario, M5S 1A8, Canada
11Department of Molecular Genetics, University of Toronto, 1 King’s College Circle, Toronto, Ontario, M5S 1A8, Canada
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E.F. Pai
2Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, Ontario, M5G 1L7, Canada
6Department of Biochemistry, University of Toronto, 1 King’s College Circle, Toronto, Ontario, M5S 1A8, Canada
13Center for Free-Electron Laser Science, Luruper Chaussee 149, 22761 Hamburg, Germany
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E.C. Schulz
1Department for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany
13Center for Free-Electron Laser Science, Luruper Chaussee 149, 22761 Hamburg, Germany
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  • For correspondence: pedram.Mehrabi@mpsd.mpg.de eike.schulz@mpsd.mpg.de
R.J.D. Miller
1Department for Atomically Resolved Dynamics, Max Planck Institute for the Structure and Dynamics of Matter, Luruper Chaussee 149, 22761 Hamburg, Germany
7Departments of Chemistry and Physics, University of Toronto, 80 St. George Street, Toronto, Ontario, M5S 3H6, Canada
8Department of Physics, Universität Hamburg, Jungiusstrasse 9, 20355 Hamburg, Germany
13Center for Free-Electron Laser Science, Luruper Chaussee 149, 22761 Hamburg, Germany
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Abstract

For the two proteins myoglobin (MB) and fluoroacetate dehalogenase (FAcD), we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize comparability, we used the same batch of crystals, the same sample delivery device, as well as the same data analysis software. Overall figures of merit indicate that the data of both radiation sources are of equivalent quality. For both proteins reasonable data statistics can be obtained with approximately 5000 room temperature diffraction images irrespective of the radiation source. The direct comparability of SSX and SFX data indicates that diffraction quality is rather linked to the properties of the crystals than to the radiation source. Time-resolved experiments can therefore be conducted at the source that best matches the desired time-resolution.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted August 22, 2020.
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Serial femtosecond and serial synchrotron crystallography yield data of equivalent quality: a systematic comparison
P. Mehrabi, R. Bücker, G. Bourenkov, H.M. Ginn, D. von Stetten, H.M. Müller-Werkmeister, A. Kuo, T. Morizumi, B.T. Eger, W.-L. Ou, S. Oghbaey, A. Sarracini, J.E. Besaw, O. Paré-Labrosse, S. Meier, H. Schikora, F. Tellkamp, A. Marx, D.A. Sherrell, D. Axford, R. Owen, O.P. Ernst, E.F. Pai, E.C. Schulz, R.J.D. Miller
bioRxiv 2020.08.21.257170; doi: https://doi.org/10.1101/2020.08.21.257170
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Serial femtosecond and serial synchrotron crystallography yield data of equivalent quality: a systematic comparison
P. Mehrabi, R. Bücker, G. Bourenkov, H.M. Ginn, D. von Stetten, H.M. Müller-Werkmeister, A. Kuo, T. Morizumi, B.T. Eger, W.-L. Ou, S. Oghbaey, A. Sarracini, J.E. Besaw, O. Paré-Labrosse, S. Meier, H. Schikora, F. Tellkamp, A. Marx, D.A. Sherrell, D. Axford, R. Owen, O.P. Ernst, E.F. Pai, E.C. Schulz, R.J.D. Miller
bioRxiv 2020.08.21.257170; doi: https://doi.org/10.1101/2020.08.21.257170

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