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.; Franke, D.; Dörner, K.; Bajt, S.; Bean, R.; Custódio, T. F.; de Wijn, R.; Juncheng, E.; Henkel, A.; Gruzinov, A.; Jeffries, C. M.; Kim, Y.; Kirkwood, H.; Kloos, M.; Knoška, J.; Koliyadu, J.; Letrun, R.; Löw, C.; Makroczyova, J.; Mall, A.; Meijers, R.; Murillo, G. E. P.; Oberthür, D.; Round, E.; Seuring, C.; Sikorski, M.; Vagovic, P.; Valerio, J.; Wollweber, T.; Zhuang, Y.; Schulz, J.; Haas, H.; Chapman, H. N.; Mancuso, A. P.; Svergun, D.

doi:10.1038/s42003-023-05416-7

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

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

MPS-Authors

Ayyer, K.
The Hamburg Centre for Ultrafast Imaging, Universität Hamburg;
Computational Nanoscale Imaging, Condensed Matter Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Center for Free-Electron Laser Science CFEL, Deutsches Elektronen-Synchrotron DESY;

/persons/resource/persons260450

Mall, A.
Computational Nanoscale Imaging, Condensed Matter Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
International Max Planck Research School for Ultrafast Imaging & Structural Dynamics (IMPRS-UFAST), Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

Wollweber, T.
The Hamburg Centre for Ultrafast Imaging, Universität Hamburg;
Computational Nanoscale Imaging, Condensed Matter Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

Zhuang, Y.
The Hamburg Centre for Ultrafast Imaging, Universität Hamburg;
Computational Nanoscale Imaging, Condensed Matter Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

External Resource

https://doi.org/10.1038/s42003-023-05416-7
(Publisher version)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

s42003-023-05416-7.pdf
(Publisher version), 2MB

Supplementary Material (public)

suppl.zip
(Supplementary material), 6MB

Citation

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.

Cite as: https://hdl.handle.net/21.11116/0000-000D-D2C2-A

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.