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strategies for high-throughput ligand screening -automated co-crystallisation and soaking
Poster Title: strategies for high-throughput ligand screening -automated co-crystallisation and soaking
Submitted on 10 Jan 2020
Author(s): Paul Thaw1, David Hargreaves2, JörgBenz3, Joby Jenkins1
Affiliations: SPT Labtech Ltd, Melbourn Science Park, Melbourn, Rosyton, Hertfordshire, SG8 6HB, UK. 2Biochemistry Dept.,2Astra Zeneca, Cambridge Biomedical Campus, Cambridge , UK, 3F.Hoffman-La Roche AG, Switzerland
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Abstract: Growing protein-ligand complex crystals can be challenging, especially in cases where the affinity is poor and the solubility of the ligand in the crystallisation condition is low. Various methodologies are often trialled before obtaining a diffraction-quality protein-ligand crystal.
Co-crystallisation is a common method for producing protein-ligand complex structures. It is especially useful when drug-like compounds trigger conformational changes in proteins. This can result in variations in the growing conditions or crystal forms, and may necessitate wider screening strategies for co-crystallisation in general.
Alternatively, soakingprotein crystals with ligands is the fastest route to produce high-throughput structures, as long as the starting crystal form is easy to grow reproducibly, able to accommodate the desired ligand and, is robust to physical and chemical changes.
This poster will describe automated low-volume, high-throughput techniques for both types of crystallisation methods. These methods were developed by Dr.David Hargreaves (AstraZeneca, UK) and Dr.JörgBenz, F.Hoffman-La Roche AG, Switzerland.
SPTLabtech’s mosquito®crystal enabled fast and accurate miniaturisation of the crystallisation set-up for both techniques.
Summary: This poster demonstrates how the methods of co-crystallisation and soaking can both be automated for high-throughput screening using very low volumes of both protein and ligand solutionReport abuse »
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