
Our structural biology experts work with both X-ray-crystallography and cryogenic electron microscopy (Cryo-EM) to provide visual insight into macromolecular structure, binding interactions and mechanisms of action.
Extensive capabilities allow us to support all target classes, including specialist expertise in membrane proteins.
Structure-based drug design (SBDD) is a critical part of the drug discovery process, enabling the design of new molecules with increased potency. Using our in-house crystallography and cryo-EM microscopy expertise we will guide you through your structural biology project design, delivering high-quality structural data to help you:
Learn how collaboration enabled the successful progression of a client’s drug discovery program, read the case study:
Our structural biologists, biophysicists and protein scientists work as part of one integrated team. This collaborative approach combines elements of protein structure with protein design, ensuring suitability for structural enablement.
As standard we deliver crystallographic grade protein (95% pure), enabling a ‘fresh protein to dataset’ workflow to maximize success and accelerate workflow.
Cryo-EM is a powerful complementary technique to X-ray crystallography, as it can handle large, flexible complexes that do not readily crystallize. The samples are prepared in solution, making it possible to solve structures of multiple states in a single sample for investigation of protein dynamics.
Industry-leading Cryo-EM workflow timelines, delivered by novel approaches
Maximize success in minimal turnaround time:
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Our robust process includes:
2D Classification – classifies particles into groups of 2D classes and selection of 2D classes to progress
3D Classification – further refinement to high resolution structures
Uninterrupted access - Data acquisition performed at both UK and EU based synchrotron facilities
The key to X-ray crystallography success is the initial crystallization of the target protein. Our expert team work to produce:
High crystal hit rate - initial crystallization screening utilizes fresh protein
Optimal crystal quality - subsequent optimization rounds of crystallization screening may be employed
Versatile - co-crystallization and / or soaking experiments dependent on requirement
Uninterrupted access - Data acquisition performed at both UK and EU based synchrotron facilities
Our Structural Biologists support fragment-based drug discovery by providing: