Non-invasive nanoscale imaging of protein micro- and nanocrystals for screening crystallization conditions

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2FCZ______%3A_____%2F24%3AN0000086" target="_blank" >RIV/CZ______:_____/24:N0000086 - isvavai.cz</a>

Výsledek na webu

<a href="https://journals.iucr.org/j/issues/2024/06/00/nb5386/index.html" target="_blank" >https://journals.iucr.org/j/issues/2024/06/00/nb5386/index.html</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S1600576724010124" target="_blank" >10.1107/S1600576724010124</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Non-invasive nanoscale imaging of protein micro- and nanocrystals for screening crystallization conditions

Popis výsledku v původním jazyce

Crystallography has been the routine technique for studying high-resolution structures of proteins for over five decades. A major bottleneck in structure determination of macromolecules is obtaining crystals of a size and quality suitable for single-crystal X-ray crystallography experiments. Many challenging proteins either fail to grow into crystals or fail to grow into crystals of a size suitable for obtaining high-resolution structures using conventional X-ray crystallography. When it comes to smaller crystals, they can be used either for seeding to get larger crystals or for serial crystallography and electron diffraction for obtaining the structures. For both purposes, a limiting step is to non-invasively image such small crystals of sub-micrometre dimensions and to screen the conditions where such crystals prevail. Here we use cathodoluminescence-based (CL-based) nanoscopy to image protein nanocrystals. We show that crystals of micrometre and submicrometre dimensions can be non-invasively imaged by the CL-based nanoscope. The results presented here demonstrate the feasibility of non-invasive imaging of protein crystals with sub-100 nm resolution.

Název v anglickém jazyce

Non-invasive nanoscale imaging of protein micro- and nanocrystals for screening crystallization conditions

Popis výsledku anglicky

Crystallography has been the routine technique for studying high-resolution structures of proteins for over five decades. A major bottleneck in structure determination of macromolecules is obtaining crystals of a size and quality suitable for single-crystal X-ray crystallography experiments. Many challenging proteins either fail to grow into crystals or fail to grow into crystals of a size suitable for obtaining high-resolution structures using conventional X-ray crystallography. When it comes to smaller crystals, they can be used either for seeding to get larger crystals or for serial crystallography and electron diffraction for obtaining the structures. For both purposes, a limiting step is to non-invasively image such small crystals of sub-micrometre dimensions and to screen the conditions where such crystals prevail. Here we use cathodoluminescence-based (CL-based) nanoscopy to image protein nanocrystals. We show that crystals of micrometre and submicrometre dimensions can be non-invasively imaged by the CL-based nanoscope. The results presented here demonstrate the feasibility of non-invasive imaging of protein crystals with sub-100 nm resolution.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

—

Návaznosti

V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název periodika

JOURNAL OF APPLIED CRYSTALLOGRAPHY

ISSN

1600-5767

e-ISSN

—

Svazek periodika

57

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

6

Strana od-do

1907-1912

Kód UT WoS článku

001387959000019

EID výsledku v databázi Scopus

2-s2.0-85210928789