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  Form factor determination of biological molecules with X-ray free electron laser small-angle scattering (XFEL-SAS)

Blanchet, C. E., Round, A., Mertens, H. D. T., Ayyer, K., Graewert, M., Awel, S., et al. (2023). Form factor determination of biological molecules with X-ray free electron laser small-angle scattering (XFEL-SAS). Communications Biology, 6: 1057. doi:10.1038/s42003-023-05416-7.

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s42003-023-05416-7.pdf (Publisher version), 2MB
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 Creators:
Blanchet, C. E.1, Author
Round, A.1, Author
Mertens, H. D. T.1, Author
Ayyer, K.2, 3, 4, Author           
Graewert, M.1, Author
Awel, S.1, Author
Franke, D.1, Author
Dörner, K.1, Author
Bajt, S.1, Author
Bean, R.1, Author
Custódio, T. F.1, Author
de Wijn, R.1, Author
Juncheng, E.1, Author
Henkel, A.1, Author
Gruzinov, A.1, Author
Jeffries, C. M.1, Author
Kim, Y.1, Author
Kirkwood, H.1, Author
Kloos, M.1, Author
Knoška, J.1, Author
Koliyadu, J.1, AuthorLetrun, R.1, AuthorLöw, C.1, AuthorMakroczyova, J.1, AuthorMall, A.3, Author           Meijers, R.1, AuthorMurillo, G. E. P.1, AuthorOberthür, D.1, AuthorRound, E.1, AuthorSeuring, C.1, AuthorSikorski, M.1, AuthorVagovic, P.1, AuthorValerio, J.1, AuthorWollweber, T.2, 3, Author           Zhuang, Y.2, 3, Author           Schulz, J.1, AuthorHaas, H.1, AuthorChapman, H. N.1, AuthorMancuso, A. P.1, AuthorSvergun, D.1, Author more..
Affiliations:
1external, ou_persistent22              
2The Hamburg Centre for Ultrafast Imaging, Universität Hamburg, ou_persistent22              
3Computational Nanoscale Imaging, Condensed Matter Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_3012829              
4Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY, ou_persistent22              

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 Abstract: Free-electron lasers (FEL) are revolutionizing X-ray-based structural biology methods. While protein crystallography is already routinely performed at FELs, Small Angle X-ray Scattering (SAXS) studies of biological macromolecules are not as prevalent. SAXS allows the study of the shape and overall structure of proteins and nucleic acids in solution, in a quasi-native environment. In solution, chemical and biophysical parameters that have an influence on the structure and dynamics of molecules can be varied and their effect on conformational changes can be monitored in time-resolved XFEL and SAXS experiments. We report here the collection of scattering form factors of proteins in solution using FEL X-rays. The form factors correspond to the scattering signal of the protein ensemble alone; the scattering contributions from the solvent and the instrument are separately measured and accurately subtracted. The experiment was done using a liquid jet for sample delivery. These results pave the way for time-resolved studies and measurements from dilute samples, capitalizing on the intense and short FEL X-ray pulses.

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Language(s): eng - English
 Dates: 2023-01-302023-10-042023-10-18
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s42003-023-05416-7
 Degree: -

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Project name : We acknowledge European XFEL in Schenefeld, Germany, for provision of X-ray free-electron laser beamtime at Scientific Instrument SPB/SFX (Single Particles, Clusters, and Biomolecules and Serial Femtosecond Crystallography) and would like to thank the staff for their assistance. The authors acknowledge the in-kind support of the DESY Strategy Fund Corona-related research project scheme (200702, to C.S., H.C., K.A., C.M.J. and D.S.V.). This work is also partly supported by the Cluster of Excellence “CUI: Advanced Imaging of Matter” of the Deutsche Forschungsgemeinschaft (DFG)-EXC 2056-project ID390715994. Open Access funding enabled and organized by Projekt DEAL.
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Title: Communications Biology
  Abbreviation : Commun. Biol.
Source Genre: Journal
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Publ. Info: London : Springer Nature
Pages: - Volume / Issue: 6 Sequence Number: 1057 Start / End Page: - Identifier: ISSN: 2399-3642
CoNE: https://pure.mpg.de/cone/journals/resource/2399-3642