Revealing protein structures: crystallization of protein-ligand complexes - co-crystallization and crystal soaking
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Revealing protein structures: crystallization of protein-ligand complexes - co-crystallization and crystal soaking
Original language description
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's biological functions. image
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEBS Open Bio
ISSN
2211-5463
e-ISSN
2211-5463
Volume of the periodical
15
Issue of the periodical within the volume
4
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
9
Pages from-to
542-550
UT code for WoS article
001336166200001
EID of the result in the Scopus database
2-s2.0-85206929737