SLAC National Accelerator Lab., Menlo Park, CA (United States)
Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany); The Hamburg Center for Ultrafast Imaging, Hamburg (Germany)
A*STAR (Agency for Science, Technology and Research) (Singapore)
National Univ. of Singapore (Singapore)
Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany); The Hamburg Center for Ultrafast Imaging, Hamburg (Germany); Univ. of Hamburg, Hamburg (Germany)
Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany); SLAC National Accelerator Lab., Menlo Park, CA (United States)
A*STAR (Agency for Science, Technology and Research) (Singapore); National Univ. of Singapore (Singapore); Okayama Univ., Okayama (Japan)
X-ray free electron lasers (XFELs) create new possibilities for structural studies of biological objects that extend beyond what is possible with synchrotron radiation. Serial femtosecond crystallography has allowed high-resolution structures to be determined from micro-meter sized crystals, whereas single particle coherent X-ray imaging requires development to extend the resolution beyond a few tens of nanometers. Here we describe an intermediate approach: the XFEL imaging of biological assemblies with helical symmetry. We collected X-ray scattering images from samples of microtubules injected across an XFEL beam using a liquid microjet, sorted these images into class averages, merged these data into a diffraction pattern extending to 2 nm resolution, and reconstructed these data into a projection image of the microtubule. Details such as the 4 nm tubulin monomer became visible in this reconstruction. These results illustrate the potential of single-molecule X-ray imaging of biological assembles with helical symmetry at room temperature.
@article{osti_1532435,
author = {Brändén, Gisela and Hammarin, Greger and Harimoorthy, Rajiv and Johansson, Alexander and Arnlund, David and Malmerberg, Erik and Barty, Anton and Tångefjord, Stefan and Berntsen, Peter and DePonte, Daniel P. and others},
title = {Coherent diffractive imaging of microtubules using an X-ray laser},
annote = {X-ray free electron lasers (XFELs) create new possibilities for structural studies of biological objects that extend beyond what is possible with synchrotron radiation. Serial femtosecond crystallography has allowed high-resolution structures to be determined from micro-meter sized crystals, whereas single particle coherent X-ray imaging requires development to extend the resolution beyond a few tens of nanometers. Here we describe an intermediate approach: the XFEL imaging of biological assemblies with helical symmetry. We collected X-ray scattering images from samples of microtubules injected across an XFEL beam using a liquid microjet, sorted these images into class averages, merged these data into a diffraction pattern extending to 2 nm resolution, and reconstructed these data into a projection image of the microtubule. Details such as the 4 nm tubulin monomer became visible in this reconstruction. These results illustrate the potential of single-molecule X-ray imaging of biological assembles with helical symmetry at room temperature.},
doi = {10.1038/s41467-019-10448-x},
url = {https://www.osti.gov/biblio/1532435},
journal = {Nature Communications},
issn = {ISSN 2041-1723},
number = {1},
volume = {10},
place = {United States},
publisher = {Nature Publishing Group},
year = {2019},
month = {06}}
Coherent X-ray Imaging Data Bank (Lawrence Berkeley National Laboratory); Uppsala University, CFEL DESY, University of Hamburg, SLAC National Accelerator Laboratory, Arizona State University, Lawrence Berkeley National Laboratoryhttps://doi.org/10.11577/1638360
