Observation of a single protein by ultrafast X-ray diffraction

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2FCZ______%3A_____%2F24%3AN0000003" target="_blank" >RIV/CZ______:_____/24:N0000003 - isvavai.cz</a>

Result on the web

<a href="https://www.nature.com/articles/s41377-023-01352-7" target="_blank" >https://www.nature.com/articles/s41377-023-01352-7</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41377-023-01352-7" target="_blank" >10.1038/s41377-023-01352-7</a>

Result language

angličtina

Original language name

Observation of a single protein by ultrafast X-ray diffraction

Original language description

The idea of using ultrashort X-ray pulses to obtain images of single proteins frozen in time has fascinated and inspired many. It was one of the arguments for building X-ray free-electron lasers. According to theory, the extremely intense pulses provide sufficient signal to dispense with using crystals as an amplifier, and the ultrashort pulse duration permits capturing the diffraction data before the sample inevitably explodes. This was first demonstrated on biological samples a decade ago on the giant mimivirus. Since then, a large collaboration has been pushing the limit of the smallest sample that can be imaged. The ability to capture snapshots on the timescale of atomic vibrations, while keeping the sample at room temperature, may allow probing the entire conformational phase space of macromolecules. Here we show the first observation of an X-ray diffraction pattern from a single protein, that of Escherichia coli GroEL which at 14 nm in diameter is the smallest biological sample ever imaged by X-rays, and demonstrate that the concept of diffraction before destruction extends to single proteins. From the pattern, it is possible to determine the approximate orientation of the protein. Our experiment demonstrates the feasibility of ultrafast imaging of single proteins, opening the way to single-molecule time-resolved studies on the femtosecond timescale.

Czech name

—

Czech description

—

Type

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

CEP classification

—

OECD FORD branch

10301 - Atomic, molecular and chemical physics (physics of atoms and molecules including collision, interaction with radiation, magnetic resonances, Mössbauer effect)

Project

<a href="/en/project/EF15_003%2F0000447" target="_blank" >EF15_003/0000447: Structural dynamics of biomolecular systems</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2024

Confidentiality

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

Name of the periodical

Light: Science & Applications

ISSN

2095-5545

e-ISSN

2047-7538

Volume of the periodical

13

Issue of the periodical within the volume

1

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

1-11

UT code for WoS article

001142025600001

EID of the result in the Scopus database

2-s2.0-85182166671