TY  - JOUR
AU  - Kung, Jocky Chun Kui
AU  - Kadek, Alan
AU  - Koelbel, Knut
AU  - Bandelow, Steffi
AU  - Bari, Sadia
AU  - Buck, Jens
AU  - Caleman, Carl
AU  - Commandeur, Jan
AU  - Damjanovic, Tomislav
AU  - Dörner, Simon
AU  - Fahmy, Karim
AU  - Flacht, Lara
AU  - Heidemann, Johannes
AU  - Huynh, Khon
AU  - Kopicki, Janine-Denise
AU  - Krichel, Boris
AU  - Lockhauserbaeumer, Julia
AU  - Lorenzen, Kristina
AU  - Lu, Yinfei
AU  - Pogan, Ronja
AU  - Rehmann, Jasmin
AU  - Schamoni-Kast, Kira
AU  - Lucas, Schwob
AU  - Schweikhard, Lutz
AU  - Springer, Sebastian
AU  - Svensson, Pamela
AU  - Simke, Florian
AU  - Trinter, Florian
AU  - Toleikis, Sven
AU  - Kierspel, Thomas
AU  - Uetrecht, Charlotte
TI  - X-ray Spectroscopy Meets Native Mass Spectrometry: Probing Gas-phase Protein Complexes
JO  - Physical chemistry, chemical physics
VL  - 27
SN  - 1463-9076
CY  - Cambridge
PB  - RSC Publ.
M1  - PUBDB-2025-01499
SP  - 13234 - 13242
PY  - 2025
AB  - Gas-phase activation and dissociation studies of biomolecules, proteins and their non-covalent complexes using X-rays hold great promise for revealing new insights into the structure and function of biological samples. This is due to the unique properties of X-ray molecular interactions, such as site-specific and rapid ionization. In this perspective, we report and discuss the promise of first proof-of-principle studies of X-ray-induced dissociation of native biological samples ranging from small 17 kDa monomeric proteins up to large 808 kDa non-covalent protein assemblies conducted at a synchrotron (PETRA III) and a free-electron laser (FLASH2). A commercially available quadrupole time-of-flight mass spectrometer (Q-ToF2, Micromass/Waters), modified for high-mass analysis by MS Vision, was further adapted for integration with the open ports at the corresponding beamlines. The protein complexes were transferred natively into the gas phase via nano-electrospray ionization and subsequently probed by extreme ultraviolet (FLASH2) or soft X-ray (PETRA III) radiation, in either their folded state or following collision-induced activation in the gas phase. Depending on the size of the biomolecule and the activation method, protein fragmentation, dissociation, or enhanced ionization were observed. Additionally, an extension of the setup by ion mobility is described, which can serve as a powerful tool for structural separation of biomolecules prior to X-ray probing. The first experimental results are discussed in the broader context of current and upcoming X-ray sources, highlighting their potential for advancing structural biology in the future.
LB  - PUB:(DE-HGF)16
C6  - pmid:40304431
DO  - DOI:10.1039/D5CP00604J
UR  - https://bib-pubdb1.desy.de/record/626598
ER  -