% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Weiel:862389,
      author       = {Weiel, Marie and Reinartz, Ines and Schug, Alexander},
      title        = {{R}apid interpretation of small-angle {X}-ray scattering
                      data},
      journal      = {PLoS Computational Biology},
      volume       = {15},
      number       = {3},
      issn         = {1553-7358},
      address      = {San Francisco, Calif.},
      publisher    = {Public Library of Science},
      reportid     = {FZJ-2019-02717},
      pages        = {e1006900 -},
      year         = {2019},
      abstract     = {The fundamental aim of structural analyses in biophysics is
                      to reveal a mutual relation between a molecule’s dynamic
                      structure and its physiological function. Small-angle X-ray
                      scattering (SAXS) is an experimental technique for
                      structural characterization of macromolecules in solution
                      and enables time-resolved analysis of conformational changes
                      under physiological conditions. As such experiments measure
                      spatially averaged low-resolution scattering intensities
                      only, the sparse information obtained is not sufficient to
                      uniquely reconstruct a three-dimensional atomistic model.
                      Here, we integrate the information from SAXS into molecular
                      dynamics simulations using computationally efficient native
                      structure-based models. Dynamically fitting an initial
                      structure towards a scattering intensity, such simulations
                      produce atomistic models in agreement with the target data.
                      In this way, SAXS data can be rapidly interpreted while
                      retaining physico-chemical knowledge and sampling power of
                      the underlying force field. We demonstrate our method’s
                      performance using the example of three protein systems.
                      Simulations are faster than full molecular dynamics
                      approaches by more than two orders of magnitude and
                      consistently achieve comparable accuracy. Computational
                      demands are reduced sufficiently to run the simulations on
                      commodity desktop computers instead of high-performance
                      computing systems. These results underline that
                      scattering-guided structure-based simulations provide a
                      suitable framework for rapid early-stage refinement of
                      structures towards SAXS data with particular focus on
                      minimal computational resources and time.},
      cin          = {JSC / NIC},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511)},
      pid          = {G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30901335},
      UT           = {WOS:000463877900064},
      doi          = {10.1371/journal.pcbi.1006900},
      url          = {https://juser.fz-juelich.de/record/862389},
}