Resolving molecular diffusion and aggregation of antibody proteins with megahertz X-ray free-electron laser pulses.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
21 09 2022
21 09 2022
Historique:
received:
21
02
2022
accepted:
26
08
2022
entrez:
21
9
2022
pubmed:
22
9
2022
medline:
24
9
2022
Statut:
epublish
Résumé
X-ray free-electron lasers (XFELs) with megahertz repetition rate can provide novel insights into structural dynamics of biological macromolecule solutions. However, very high dose rates can lead to beam-induced dynamics and structural changes due to radiation damage. Here, we probe the dynamics of dense antibody protein (Ig-PEG) solutions using megahertz X-ray photon correlation spectroscopy (MHz-XPCS) at the European XFEL. By varying the total dose and dose rate, we identify a regime for measuring the motion of proteins in their first coordination shell, quantify XFEL-induced effects such as driven motion, and map out the extent of agglomeration dynamics. The results indicate that for average dose rates below 1.06 kGy μs
Identifiants
pubmed: 36130930
doi: 10.1038/s41467-022-33154-7
pii: 10.1038/s41467-022-33154-7
pmc: PMC9490738
doi:
Substances chimiques
Immunoglobulins
0
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5528Informations de copyright
© 2022. The Author(s).
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