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Time-resolved scattering methods for biological samples at the CoSAXS beamline, MAX IV Laboratory

Herranz-Trillo, Fátima LU ; Sørensen, Henrik Vinther LU ; Dicko, Cedric LU orcid ; Pérez, Javier ; Lenton, Samuel LU ; Foderà, Vito ; Fornell, Anna LU ; Skepö, Marie LU orcid ; Plivelic, Tomás S. LU and Berntsson, Oskar LU , et al. (2024) In Methods in Enzymology 709. p.245-296
Abstract

CoSAXS is a state-of-the-art SAXS/WAXS beamline exploiting the high brilliance of the MAX IV 3 GeV synchrotron. By coupling advances in sample environment control with fast X-ray detectors, millisecond time-resolved scattering methods can follow structural dynamics of proteins in solution. In the present work, four sample environments are discussed. A sample environment for combined SAXS with UV–vis and fluorescence spectroscopy (SUrF) enables a comprehensive understanding of the time evolution of conformation in a model protein upon acid-driven denaturation. The use of microfluidic chips with SAXS allows the mapping of concentration with very small sample volumes. For highly reproducible sequences of mixing of components, it is... (More)

CoSAXS is a state-of-the-art SAXS/WAXS beamline exploiting the high brilliance of the MAX IV 3 GeV synchrotron. By coupling advances in sample environment control with fast X-ray detectors, millisecond time-resolved scattering methods can follow structural dynamics of proteins in solution. In the present work, four sample environments are discussed. A sample environment for combined SAXS with UV–vis and fluorescence spectroscopy (SUrF) enables a comprehensive understanding of the time evolution of conformation in a model protein upon acid-driven denaturation. The use of microfluidic chips with SAXS allows the mapping of concentration with very small sample volumes. For highly reproducible sequences of mixing of components, it is possible using stopped-flow and SAXS to access the initial effects of mixing at 2 millisecond timescales with good signal to noise to allow structural interpretation. The intermediate structures in a protein are explored under light and temperature perturbations by using lasers to “pump” the protein and SAXS as the “probe”. The methods described demonstrate that features at low q, corresponding to cooperative motions of the atoms in a protein, could be extracted at millisecond timescales, which results from CoSAXS being a highly-stable, low background, dedicated SAXS beamline.

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organization
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
keywords
BioSAXS, CoSAXS, Fluorescence, Microfluidics, SAXS, Stopped-flow, Time-resolved SAXS, Time-resolved X-ray solution scattering, TR-XSS, UV–vis
host publication
Time-Resolved Methods in Structural Biology
series title
Methods in Enzymology
volume
709
pages
52 pages
publisher
Academic Press
external identifiers
  • scopus:85208024355
  • pmid:39608946
ISSN
0076-6879
1557-7988
ISBN
9780443314568
DOI
10.1016/bs.mie.2024.10.019
language
English
LU publication?
yes
id
bfdb0294-5e30-48be-b962-7ef2dddac529
date added to LUP
2024-12-16 13:34:38
date last changed
2025-06-03 02:27:52
@inbook{bfdb0294-5e30-48be-b962-7ef2dddac529,
  abstract     = {{<p>CoSAXS is a state-of-the-art SAXS/WAXS beamline exploiting the high brilliance of the MAX IV 3 GeV synchrotron. By coupling advances in sample environment control with fast X-ray detectors, millisecond time-resolved scattering methods can follow structural dynamics of proteins in solution. In the present work, four sample environments are discussed. A sample environment for combined SAXS with UV–vis and fluorescence spectroscopy (SUrF) enables a comprehensive understanding of the time evolution of conformation in a model protein upon acid-driven denaturation. The use of microfluidic chips with SAXS allows the mapping of concentration with very small sample volumes. For highly reproducible sequences of mixing of components, it is possible using stopped-flow and SAXS to access the initial effects of mixing at 2 millisecond timescales with good signal to noise to allow structural interpretation. The intermediate structures in a protein are explored under light and temperature perturbations by using lasers to “pump” the protein and SAXS as the “probe”. The methods described demonstrate that features at low q, corresponding to cooperative motions of the atoms in a protein, could be extracted at millisecond timescales, which results from CoSAXS being a highly-stable, low background, dedicated SAXS beamline.</p>}},
  author       = {{Herranz-Trillo, Fátima and Sørensen, Henrik Vinther and Dicko, Cedric and Pérez, Javier and Lenton, Samuel and Foderà, Vito and Fornell, Anna and Skepö, Marie and Plivelic, Tomás S. and Berntsson, Oskar and Andersson, Magnus and Magkakis, Konstantinos and Orädd, Fredrik and Ahn, Byungnam and Appio, Roberto and Da Silva, Jackson and Da Silva, Vanessa and Lerato, Marco and Terry, Ann E.}},
  booktitle    = {{Time-Resolved Methods in Structural Biology}},
  isbn         = {{9780443314568}},
  issn         = {{0076-6879}},
  keywords     = {{BioSAXS; CoSAXS; Fluorescence; Microfluidics; SAXS; Stopped-flow; Time-resolved SAXS; Time-resolved X-ray solution scattering; TR-XSS; UV–vis}},
  language     = {{eng}},
  pages        = {{245--296}},
  publisher    = {{Academic Press}},
  series       = {{Methods in Enzymology}},
  title        = {{Time-resolved scattering methods for biological samples at the CoSAXS beamline, MAX IV Laboratory}},
  url          = {{http://dx.doi.org/10.1016/bs.mie.2024.10.019}},
  doi          = {{10.1016/bs.mie.2024.10.019}},
  volume       = {{709}},
  year         = {{2024}},
}