X-ray spectroscopy meets native mass spectrometry: probing gas-phase protein complexes

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F25%3A00643564" target="_blank" >RIV/61388971:_____/25:00643564 - isvavai.cz</a>

Result on the web

<a href="https://pubs.rsc.org/en/content/articlelanding/2025/cp/d5cp00604j" target="_blank" >https://pubs.rsc.org/en/content/articlelanding/2025/cp/d5cp00604j</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/d5cp00604j" target="_blank" >10.1039/d5cp00604j</a>

Result language

angličtina

Original language name

X-ray spectroscopy meets native mass spectrometry: probing gas-phase protein complexes

Original language description

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 (structurally preserved) 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-Tof Ultima US, 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.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10606 - Microbiology

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2025

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Physical Chemistry Chemical Physics

ISSN

1463-9076

e-ISSN

1463-9084

Volume of the periodical

27

Issue of the periodical within the volume

25

Country of publishing house

GB - UNITED KINGDOM

Number of pages

9

Pages from-to

13234-13242

UT code for WoS article

001478857300001

EID of the result in the Scopus database

2-s2.0-105004049724