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X-RAY CRYSTALLOGRAPHY
The biophysical technique of X-Ray Crystallography enables the study of protein structures at the atomic level, and can provide valuable information about protein conformation and active site interactions. The ligand protein interactions can thus be characterized in a very systematic manner and form a guide for Structure Guided Drug Discovery, Fragment Based Drug Discovery approaches.
Once a protein is crystallized the crystals is taken to the Synchrotron or a Lab source for data collection. The crystal is put in the x-ray beam and diffraction images are collected over a wide angular range. The images are then processed using computational methods and the remaining refinement work is also done on the computers. The resulting model that is developed from the data collected gives an insight into protein-ligand interactions. The medicinal chemists use this information for refining their thoughts on making the chemistry work for the target.
This technique requires protein that is greater than 95% pure and is stable at high (>10mgs/ml) concentrations for prolonged periods during the crystallization process. Based on the protein target it can be gene-incorporated into an E.Coli or Bacculo Virus system. The bacteria or virus can then be scaled up for protein production and subsequent purification. Learn more about Xpress, Xamine, and Xplore to discover the best proprietary pathway for gene to structure solutions.
After a model is generated many higher level software tools can be utilized to build and expand the chemistry, this can go into improvement of the molecule or look for additional ways of utilizing the technology. Visit the Xseed offering page to learn more about how XTAL can help the client plan and implement this growth with their VC partners.
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