The Durham Osmolyte Screen MD1-120
Harness the power of intracellular compounds to improve your crystallisations.
The new Durham Osmolyte screen allows you to test which of a broad range of cell components help stabilise your protein, improving the results of structural and functional studies. The developers of the screen describe the importance of stability screening for protein structural and functional studies in this JoVE article:
Osmolytes are uncharged, highly soluble organic molecules that act in cells to balance high external salt concentrations without disturbing intracellular ionic strength. This makes osmolytes the ideal additives for stabilising your protein during structural and functional studies as they are usually present in high concentrations in native cell environments without affecting protein behaviour.
Easily identify which osmolytes are most beneficial to your research with The Durham Osmolyte screen, a 96-well screen that scans more than 50 different osmolytes, available exclusively from Molecular Dimensions.
Osmolytes such as sugars, polyols, amino-acids, NDSBs and many other chemical classes are included in the screen, for example:
To optimise your protein’s complete environment, we recommend using the Osmolyte screen together with the Durham pH and Salt screens. All three screens were developed at Durham University by Ehmke Pohl, Daniel Bruce, Morten Grøftehauge and Emily Cardew.The Durham Screens are designed to work with NAMI* the free to download software for easy interpretation of thermal shift assay results.
Reference: Bruce, D. et al.J. Vis. Exp.144: e58666 (2019).
The Durham Osmolyte Screen is presented as 96 x 0.5 mL conditions in a deep-well block. They are preservative free and it is recommended that they are stored at 4°C, however they can be used at room temperature for screen set-up.
*NAMI can generate waterfall plots of thermal shift data at multiple concentrations or plots of melting temperature against concentration. These differentiate a sudden increase in protein stability indicating a specific interaction and steady increases in stability due to the changing protein environment. In addition, it produces a useful colour gradient plate diagram to make identifying particularly stabilising or destabilising conditions simple.
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