Structure determination of protein-small molecule complex
The structural analysis of protein-small molecule complexes is of great
significance for understanding protein function, drug design, and analyzing
biomolecular interactions. X-ray crystallography, which determines the three-dimensional
structure of proteins, is a critical tool for these studies. The process
of X-ray crystallography involves crystallizing proteins to form structured, ordered
lattices, which is the key step in determining whether the protein structure
can be successfully resolved.
Co-crystallization Method
Co-crystallization involves mixing proteins with other biomolecules (such
as ligands, nucleic acids, enzymes, small molecules, or other proteins) to prepare
a complex. The commonly used crystallization methods, such as the sitting
drop and the hanging drop, are used to obtain complex crystals through high-throughput
screening with automated crystallization robot.
Soaking Method
A common technique for obtaining the structure of protein-small molecule complex.
Protein crystals that have already been grown are placed in a solution containing small molecule ligand, the ligand molecules diffuse through the solvent channels of the crystal and bind specifically to the protein, and then the soaked crystals are subjected to X-ray data collection to resolve the complex structure. Compared to co-crystallization, soaking is simpler and low cost.
Service Content
