Antibody:antigen complex structures
A three-dimensional X-ray crystallographic structure is essential for elucidating the details of epitope-parartope interactions in antigen-antibody complexes, and for optimizing the binding interactions within a complex. The structure will accelerate your therapeutics program and will also provide clear and indisputable data for patent application. SARomics Biostructures team has gathered extensive experience in the crystallization of antibody:antigen complex structures (see our case study below). Our crystallography services platform includes all necessary equipment and tools for handling projects of this type.
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LukGH (LukAB) is a potent leukocidin of Staphylococcus aureus that lyses human phagocytic cells and is thought to contribute to immune evasion. Unlike the other bi-component leukocidins of S. aureus, LukGH forms a heterodimer before binding to its receptor, CD11b expressed on professional phagocytic cells, and displays significant sequence variation.
In a project we performed X-ray crystallography analysis of the complex between the LukGH dimer and the antigen-binding fragment of a very potent mAb (PDB code 5K59). The complex clearly indicated that the epitope is located in the predicted cell binding region (rim domain) of LukGH.
Details can be found in the publication:
Badarau A, Rouha H, Malafa S, Battles MB, Walker L, Nielson N, Dolezilkova I, Teubenbacher A, Banerjee S, Maierhofer B, Weber S, Stulik L, Logan DT, Welin M, Mirkina I, Pleban C, Zauner G, Gross K, Jägerhofer M, Magyarics Z & Nagy E (2016). Context matters: The importance of dimerization-induced conformation of the LukGH leukocidin of Staphylococcus aureus for the generation of neutralizing antibodies. MAbs. 8, 1347-1360.
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