Automated plate sampling case study

An automated dynamic light scattering system from Malvern Instruments has become established as an essential part of the analytical toolkit used by SARomics Biostructures, a leading provider of protein 3D structure determination and structure-based drug design services. The Zetasizer APS automated plate sampling system is supporting the systematic study of the aggregation behaviour of proteins, a fundamental component of the services provided by SARomics Biostructures. The company, which is based in Lund, Sweden within the biotech cluster of the Medicon Valley, is a research-intensive organisation with clients around the world.

The Zetasizer APS is a robust, simple-to-operate system that uses laser light scattering to determine a number of parameters associated with protein conformation and stability. It integrates a plate sampling system and measurement unit into a single instrument, automating the measurement of samples in industry standard 96- or 384-well plates on as little as 20 μL of recoverable sample.

Dr Maria Håkansson is the MAX-lab Crystallization Facility Manager and Senior Scientist at SARomics Biostructures. She is one of a number of people within the company to use the system. “Our primary use of the Zetasizer APS is in screening protein preparations to ensure they are monodisperse and therefore suitable for crystallization,” said Dr Håkansson. “If we find aggregated proteins, then crystallization trials are unlikely to be successful and we know we need to adjust the preparation process. We’ve been running the Zetasizer APS continuously since 2012 and the real beauty is that we simply load the samples in multiwell plates, leave it to run, even overnight, and go back and pick up the results. The system is easy to use, requires little training and, most importantly, the measurements and data are excellent.”

The team at SARomics also uses the system in other protein screening applications. To screen protein constructs, for example, to check their size and aggregation status, with 20-30 duplicate samples being run routinely. Stability screening of single constructs in a range of buffers is also done to assist with selecting appropriate buffers for crystallization trials. In addition, the product is used in conjunction with differential scanning fluorimetry to determine protein melting points, the results of which can be correlated with light scattering.

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