IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v541y2017i7636d10.1038_nature20599.html
   My bibliography  Save this article

Structures of riboswitch RNA reaction states by mix-and-inject XFEL serial crystallography

Author

Listed:
  • J. R. Stagno

    (Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute)

  • Y. Liu

    (Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute)

  • Y. R. Bhandari

    (Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute)

  • C. E. Conrad

    (Arizona State University
    Center for Applied Structural Discovery, The Biodesign Institute, Arizona State University)

  • S. Panja

    (Johns Hopkins University)

  • M. Swain

    (Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute)

  • L. Fan

    (Small Angle X-ray Scattering Core Facility, Center for Cancer Research, National Cancer Institute)

  • G. Nelson

    (Arizona State University)

  • C. Li

    (Arizona State University)

  • D. R. Wendel

    (Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute)

  • T. A. White

    (Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY)

  • J. D. Coe

    (Arizona State University
    Center for Applied Structural Discovery, The Biodesign Institute, Arizona State University)

  • M. O. Wiedorn

    (Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY
    University of Hamburg)

  • J. Knoska

    (Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY
    University of Hamburg)

  • D. Oberthuer

    (Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY)

  • R. A. Tuckey

    (Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute)

  • P. Yu

    (Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute)

  • M. Dyba

    (Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute)

  • S. G. Tarasov

    (Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute)

  • U. Weierstall

    (Center for Applied Structural Discovery, The Biodesign Institute, Arizona State University
    Arizona State University)

  • T. D. Grant

    (Hauptmann-Woodward Medical Research Institute)

  • C. D. Schwieters

    (Center for Information Technology, National Institutes of Health)

  • J. Zhang

    (Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health)

  • A. R. Ferré-D’Amaré

    (Laboratory of RNA Biophysics and Cellular Physiology, National Heart Lung and Blood Institute, National Institutes of Health)

  • P. Fromme

    (Arizona State University
    Center for Applied Structural Discovery, The Biodesign Institute, Arizona State University)

  • D. E. Draper

    (Johns Hopkins University)

  • M. Liang

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • M. S. Hunter

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • S. Boutet

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • K. Tan

    (Structural Biology Center, Advanced Photon Source, Argonne National Laboratory)

  • X. Zuo

    (Advanced Photon Source, Argonne National Laboratory)

  • X. Ji

    (Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute)

  • A. Barty

    (Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY)

  • N. A. Zatsepin

    (Center for Applied Structural Discovery, The Biodesign Institute, Arizona State University
    Arizona State University)

  • H. N. Chapman

    (Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY
    University of Hamburg)

  • J. C. H. Spence

    (Center for Applied Structural Discovery, The Biodesign Institute, Arizona State University
    Arizona State University)

  • S. A. Woodson

    (Johns Hopkins University)

  • Y.-X. Wang

    (Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute)

Abstract

Femtosecond XFEL crystallography is used to identify dynamic changes in the adenine riboswitch aptamer domain, with at least four states identified in real time, two in the apo form before binding and two with the ligand bound.

Suggested Citation

  • J. R. Stagno & Y. Liu & Y. R. Bhandari & C. E. Conrad & S. Panja & M. Swain & L. Fan & G. Nelson & C. Li & D. R. Wendel & T. A. White & J. D. Coe & M. O. Wiedorn & J. Knoska & D. Oberthuer & R. A. Tuc, 2017. "Structures of riboswitch RNA reaction states by mix-and-inject XFEL serial crystallography," Nature, Nature, vol. 541(7636), pages 242-246, January.
    • Handle: RePEc:nat:nature:v:541:y:2017:i:7636:d:10.1038_nature20599
    DOI: 10.1038/nature20599
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature20599
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature20599?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

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


    Cited by:

    1. Griffin M. Schroeder & Chapin E. Cavender & Maya E. Blau & Jermaine L. Jenkins & David H. Mathews & Joseph E. Wedekind, 2022. "A small RNA that cooperatively senses two stacked metabolites in one pocket for gene control," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    2. Tek Narsingh Malla & Kara Zielinski & Luis Aldama & Sasa Bajt & Denisse Feliz & Brendon Hayes & Mark Hunter & Christopher Kupitz & Stella Lisova & Juraj Knoska & Jose Manuel Martin-Garcia & Valerio Ma, 2023. "Heterogeneity in M. tuberculosis β-lactamase inhibition by Sulbactam," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Yanyan Xue & Jun Li & Dian Chen & Xizhu Zhao & Liang Hong & Yu Liu, 2023. "Observation of structural switch in nascent SAM-VI riboswitch during transcription at single-nucleotide and single-molecule resolution," Nature Communications, Nature, vol. 14(1), pages 1-14, 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:nature:v:541:y:2017:i:7636:d:10.1038_nature20599. 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.