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CreMap™ Epitope Mapping Service by X-ray Crystallography

Staffed by dedicated scientists with combined knowledge and expertise in antibody engineering and protein X-ray crystallography, Creative Biolabs has extensive experience in crystallizing antibody-antigen complexes and resolving their 3D structures. Based on our extensive knowledge, we are fully equipped to reach out to our clients who may have the problem or difficulty dealing with epitope mapping.

An epitope is the portion of an antigen recognized by the immune system, especially by an antibody. The determination of the amino acid sequence of epitopes is drawing much interest in broad areas such as vaccines and therapeutics. X-ray crystallography of an antibody-antigen complex is the gold standard approach, also the most unambiguous method for epitope mapping. Taking advantage of the interatomic spacing of most crystalline solids, it provides a high-resolution structure of the complex and the molecular details of the interaction are defined as well. Based on the structure and interaction with the antibody, epitopes could be categorized into two types, linear epitopes, and conformational epitopes. X-ray co-crystallography allows for both linear and conformational epitope mappings. By co-crystallography the monoclonal antibody with its respective antigen, the epitope can be defined immediately with high accuracy.

CreMap™ Epitope Mapping Service by X-ray Crystallography

By far, X-ray crystallography is the most precise method for characterizing epitopes. The most significant and essential part of this method is crystallography. It is a process where atoms or molecules are highly organized into a structure called crystal. The principle of crystallization is the fact that solute should be soluble in a suitable solvent at high temperature. A change of these conditions to a state where the solubility is lower leads to the formation of a crystalline solid. One of the most efficient ways for crystallization is hanging drop crystallization. The samples and the reagents are in contact with a siliconized glass surface. This method is cost-effective and has easier access to crystals compared to other methods.

Workflow of X-ray crystallography mechanism.
Fig.1 Workflow of X-ray crystallography mechanism.

Key Features


Creative Biolabs has accumulated extensive experience in mapping epitopes recognized by the antibodies. If you are now doing research on antigen-antibody complex, trying to figure out epitopes on the antigen, or if you are particularly interested in our X-ray crystallization platform, please feel free to contact usand a formal feedback will be sent back as soon as possible.

References

  1. Abbott, W.M., M.M. Damschroder, and D.C. Lowe, Current approaches to fine mapping of antigen-antibody interactions. Immunology, 2014. 142(4): p. 526-35.
  2. Malito, E., A. Carfi, and M.J. Bottomley, Protein Crystallography in Vaccine Research and Development. Int J Mol Sci, 2015. 16(6): p. 13106-40.
  3. Lo Conte, L., C. Chothia, and J. Janin, The atomic structure of protein-protein recognition sites. J Mol Biol, 1999. 285(5): p. 2177-98.



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