Revealing protein structures: crystallization of protein-ligand complexes - co-crystallization and crystal soaking

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F25%3A43910753" target="_blank" >RIV/60076658:12310/25:43910753 - isvavai.cz</a>

Výsledek na webu

<a href="https://febs.onlinelibrary.wiley.com/doi/epdf/10.1002/2211-5463.13913?getft_integrator=clarivate&src=getftr&utm_source=clarivate" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/epdf/10.1002/2211-5463.13913?getft_integrator=clarivate&src=getftr&utm_source=clarivate</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/2211-5463.13913" target="_blank" >10.1002/2211-5463.13913</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Revealing protein structures: crystallization of protein-ligand complexes - co-crystallization and crystal soaking

Popis výsledku v původním jazyce

Protein crystallogenesis represents a key step in X-ray crystallography studies that employ co-crystallization and ligand soaking for investigating ligand binding to proteins. Co-crystallization is a method that enables the precise determination of binding positions, although it necessitates a significant degree of optimization. The utilization of microseeding can facilitate a reduction in sample requirements and accelerate the co-crystallization process. Ligand soaking is the preferred method due to its simplicity; however, it requires careful control of soaking conditions to ensure the successful integration of the ligands. This research protocol details the procedures for co-crystallization and soaking to achieve protein-ligand complex formation, which is essential for advancing drug discovery. Additionally, a simple protocol for demonstrating soaking for educational purposes is described. Co-crystallization crystallizes a protein with its ligand, resulting in protein-ligand complex crystals. In contrast, soaking introduces a ligand into preformed protein crystals, allowing it to bind. Both methods produce crystals for X-ray diffraction, which generates diffraction patterns that are analyzed to determine the three-dimensional structure of the complex. This process uncovers key interactions critical to understanding the protein&apos;s biological functions. image

Název v anglickém jazyce

Revealing protein structures: crystallization of protein-ligand complexes - co-crystallization and crystal soaking

Popis výsledku anglicky

Protein crystallogenesis represents a key step in X-ray crystallography studies that employ co-crystallization and ligand soaking for investigating ligand binding to proteins. Co-crystallization is a method that enables the precise determination of binding positions, although it necessitates a significant degree of optimization. The utilization of microseeding can facilitate a reduction in sample requirements and accelerate the co-crystallization process. Ligand soaking is the preferred method due to its simplicity; however, it requires careful control of soaking conditions to ensure the successful integration of the ligands. This research protocol details the procedures for co-crystallization and soaking to achieve protein-ligand complex formation, which is essential for advancing drug discovery. Additionally, a simple protocol for demonstrating soaking for educational purposes is described. Co-crystallization crystallizes a protein with its ligand, resulting in protein-ligand complex crystals. In contrast, soaking introduces a ligand into preformed protein crystals, allowing it to bind. Both methods produce crystals for X-ray diffraction, which generates diffraction patterns that are analyzed to determine the three-dimensional structure of the complex. This process uncovers key interactions critical to understanding the protein&apos;s biological functions. image

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

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

Název periodika

FEBS Open Bio

ISSN

2211-5463

e-ISSN

2211-5463

Svazek periodika

15

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

542-550

Kód UT WoS článku

001336166200001

EID výsledku v databázi Scopus

2-s2.0-85206929737