IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v8y2017i1d10.1038_s41467-017-00630-4.html
   My bibliography  Save this article

Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons

Author

Listed:
  • Tobias Weinert

    (Paul Scherrer Institut)

  • Natacha Olieric

    (Paul Scherrer Institut)

  • Robert Cheng

    (LeadXpro AG)

  • Steffen Brünle

    (Max-Planck Institute of Biophysics)

  • Daniel James

    (Paul Scherrer Institut)

  • Dmitry Ozerov

    (Paul Scherrer Institut)

  • Dardan Gashi

    (Paul Scherrer Institut
    Paul Scherrer Institut)

  • Laura Vera

    (Swiss Light Source, Paul Scherrer Institut)

  • May Marsh

    (Swiss Light Source, Paul Scherrer Institut)

  • Kathrin Jaeger

    (Paul Scherrer Institut)

  • Florian Dworkowski

    (Swiss Light Source, Paul Scherrer Institut)

  • Ezequiel Panepucci

    (Swiss Light Source, Paul Scherrer Institut)

  • Shibom Basu

    (Swiss Light Source, Paul Scherrer Institut)

  • Petr Skopintsev

    (Paul Scherrer Institut)

  • Andrew S. Doré

    (Heptares Therapeutics Ltd)

  • Tian Geng

    (Heptares Therapeutics Ltd)

  • Robert M. Cooke

    (Heptares Therapeutics Ltd)

  • Mengning Liang

    (SLAC National Accelerator Laboratory)

  • Andrea E. Prota

    (Paul Scherrer Institut)

  • Valerie Panneels

    (Paul Scherrer Institut)

  • Przemyslaw Nogly

    (Paul Scherrer Institut)

  • Ulrich Ermler

    (Max-Planck Institute of Biophysics)

  • Gebhard Schertler

    (Paul Scherrer Institut
    ETH Zurich)

  • Michael Hennig

    (LeadXpro AG)

  • Michel O. Steinmetz

    (Paul Scherrer Institut
    University of Basel)

  • Meitian Wang

    (Swiss Light Source, Paul Scherrer Institut)

  • Jörg Standfuss

    (Paul Scherrer Institut)

Abstract

Historically, room-temperature structure determination was succeeded by cryo-crystallography to mitigate radiation damage. Here, we demonstrate that serial millisecond crystallography at a synchrotron beamline equipped with high-viscosity injector and high frame-rate detector allows typical crystallographic experiments to be performed at room-temperature. Using a crystal scanning approach, we determine the high-resolution structure of the radiation sensitive molybdenum storage protein, demonstrate soaking of the drug colchicine into tubulin and native sulfur phasing of the human G protein-coupled adenosine receptor. Serial crystallographic data for molecular replacement already converges in 1,000–10,000 diffraction patterns, which we collected in 3 to maximally 82 minutes. Compared with serial data we collected at a free-electron laser, the synchrotron data are of slightly lower resolution, however fewer diffraction patterns are needed for de novo phasing. Overall, the data we collected by room-temperature serial crystallography are of comparable quality to cryo-crystallographic data and can be routinely collected at synchrotrons.

Suggested Citation

  • Tobias Weinert & Natacha Olieric & Robert Cheng & Steffen Brünle & Daniel James & Dmitry Ozerov & Dardan Gashi & Laura Vera & May Marsh & Kathrin Jaeger & Florian Dworkowski & Ezequiel Panepucci & Shi, 2017. "Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons," Nature Communications, Nature, vol. 8(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00630-4
    DOI: 10.1038/s41467-017-00630-4
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-017-00630-4
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-017-00630-4?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Maximilian Wranik & Michal W. Kepa & Emma V. Beale & Daniel James & Quentin Bertrand & Tobias Weinert & Antonia Furrer & Hannah Glover & Dardan Gashi & Melissa Carrillo & Yasushi Kondo & Robin T. Stip, 2023. "A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Maximilian Wranik & Tobias Weinert & Chavdar Slavov & Tiziana Masini & Antonia Furrer & Natacha Gaillard & Dario Gioia & Marco Ferrarotti & Daniel James & Hannah Glover & Melissa Carrillo & Demet Keki, 2023. "Watching the release of a photopharmacological drug from tubulin using time-resolved serial crystallography," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. M. Wilamowski & D. A. Sherrell & Y. Kim & A. Lavens & R. W. Henning & K. Lazarski & A. Shigemoto & M. Endres & N. Maltseva & G. Babnigg & S. C. Burdette & V. Srajer & A. Joachimiak, 2022. "Time-resolved β-lactam cleavage by L1 metallo-β-lactamase," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00630-4. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.