Co-crystallization defines the epitope
The epitope binding site can be represented by multiple domains or residues not closely aligned in the primary sequence, making it difficult to define the epitope binding site. A variety of technologies (peptide array mapping, mutagenesis studies, etc.) can be used to define epitopes. The most unambiguous method, however, is to co-crystallize the mAb (or corresponding Fragment Antigen Binding region, Fab) with its respective antigen. These co-crystal structures immediately define the epitope and can be used to rationally alter and improve the binding interactions.
Leverage Emerald experience in antibody crystallization
The proteins for crystallization trials can be supplied by the client or we can leverage our experience in protein engineering, expression, and purification to generate the Fab and a wide range of different antigens for crystallization trials.
At Emerald BioStructures, we generate hundreds of structures for drug discovery projects and structural genomics initiatives. The Protein Maker™ workstation, innovated by our sister company Emerald BioSystems, performs high throughput protein purification running 24 chromatography columns (1-5 ml) in parallel. This instrument allows us to evaluate expression levels, study different isotypes or clones, and determine the best purification method for scaling up.