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

J. R. Stagno, Y. Liu, Y. R. Bhandari, C. E. Conrad, S. Panja, Mamata Swain (), L. Fan, Gerald Nelson, C. Li, D. R. Wendel, T. A. White, J. D. Coe, M. O. Wiedorn, J. Knoska, D. Oberthuer, R. A. Tuckey, P. Yu, M. Dyba, S. G. Tarasov, U. Weierstall, T. D. Grant, C. D. Schwieters, J. Zhang, A. R. Ferré-D’Amaré, P. Fromme, D. E. Draper, M. Liang, M. S. Hunter, S. Boutet, K. Tan, X. Zuo, X. Ji, A. Barty, N. A. Zatsepin, H. N. Chapman, J. C. H. Spence, S. A. Woodson and Y.-X. Wang ()
Additional contact information
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
S. Panja: Johns Hopkins University
L. Fan: Small Angle X-ray Scattering Core Facility, Center for Cancer Research, National Cancer Institute
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
M. O. Wiedorn: Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY
J. Knoska: Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY
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
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
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
H. N. Chapman: Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY
J. C. H. Spence: Center for Applied Structural Discovery, The Biodesign Institute, 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

Nature, 2017, vol. 541, issue 7636, 242-246

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.

Date: 2017
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DOI: 10.1038/nature20599

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