On‑the‑fy resolution enhancement in X‑ray protein crystallography using electric feld

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F10974938%3A_____%2F25%3A25_88_35" target="_blank" >RIV/10974938:_____/25:25_88_35 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.1007/s00249-025-01731-5" target="_blank" >https://doi.org/10.1007/s00249-025-01731-5</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00249-025-01731-5" target="_blank" >10.1007/s00249-025-01731-5</a>

Jazyk výsledku

angličtina

Název v původním jazyce

On‑the‑fy resolution enhancement in X‑ray protein crystallography using electric feld

Popis výsledku v původním jazyce

X-ray crystallography has tremendously served structural biology by routinely providing high-resolution 3D structures of macromolecules. The extent of information encoded in the X-ray crystallography is proportional to which resolution the crystals diffract and the structure can be refined to. Therefore, there is a continuous effort to obtain high-quality crystals, especially for those proteins, which are considered difficult to crystallize into high-quality protein crystals of suitable sizes for X-ray crystallography. Efforts in enhancing the resolution in X-ray crystallography have also been made by optimizing crystallization protocols using external stimuli such as an electric field and magnetic field during the crystallization. Here, we present the feasibility of on-the-fly post-crystallization resolution enhancement of the protein crystal diffraction by applying a high-voltage electric field. The electric field between 2 and 11 kV/cm, which was applied after mounting the crystals in the beamline, resulted in the enhancement of the resolution. The crystal diffraction quality improved progressively with the exposure time. Moreover, we also find that upto defined electric field threshold, the protein structure remains largely unperturbed, a conclusion further supported by molecular dynamics simulations.

Název v anglickém jazyce

On‑the‑fy resolution enhancement in X‑ray protein crystallography using electric feld

Popis výsledku anglicky

X-ray crystallography has tremendously served structural biology by routinely providing high-resolution 3D structures of macromolecules. The extent of information encoded in the X-ray crystallography is proportional to which resolution the crystals diffract and the structure can be refined to. Therefore, there is a continuous effort to obtain high-quality crystals, especially for those proteins, which are considered difficult to crystallize into high-quality protein crystals of suitable sizes for X-ray crystallography. Efforts in enhancing the resolution in X-ray crystallography have also been made by optimizing crystallization protocols using external stimuli such as an electric field and magnetic field during the crystallization. Here, we present the feasibility of on-the-fly post-crystallization resolution enhancement of the protein crystal diffraction by applying a high-voltage electric field. The electric field between 2 and 11 kV/cm, which was applied after mounting the crystals in the beamline, resulted in the enhancement of the resolution. The crystal diffraction quality improved progressively with the exposure time. Moreover, we also find that upto defined electric field threshold, the protein structure remains largely unperturbed, a conclusion further supported by molecular dynamics simulations.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

<a href="/cs/project/EF16_019%2F0000789" target="_blank" >EF16_019/0000789: Pokročilý výzkum s využitím fotonů a částic vytvořených vysoce intenzivními lasery</a><br>

Návaznosti

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

Rok uplatnění

2025

Kód důvěrnosti údajů

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

Název periodika

European Biophysics Journal

ISSN

0175-7571

e-ISSN

1432-1017

Svazek periodika

54

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

89–95

Kód UT WoS článku

001401954300001

EID výsledku v databázi Scopus

2-s2.0-85217236850