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Circular dichroism (CD) measures the difference in the absorbance of left-handed circularly polarised light (L-CPL) and right-handed circularly polarised light (R-CPL), occurring in molecules with chiral chromophores (light-absorbing groups). it is primarily used to analyse the secondary structure or conformation of macromolecules, particularly proteins. Since secondary structure is sensitive to its environment, e.g. temperature or pH, CD can be used to observe how these structures change under different environmental conditions or when interacting with other molecules.

The Two MP mass photometer allows for simple and accurate mass measurements of single molecules in their native state in solution. It has a wide mass detection range suitable for studying proteins, DNA, RNA and large macromolecular complexes.

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The Nanotemper Prometheus is used to test protein stability and protein aggregation by either chemical or thermal denaturation. The instrument monitors the intrinsic fluorescence signal of a protein sample as a measure of its folding state. A ratio metric measurement of the fluorescent signal is plotted against either increasing concentration of a chemical denaturant or increasing temperature, to determine the Tm of a protein. Results are available within minutes.

The Formulatrix Rock Imager 54 is an advanced automated imaging system designed for protein crystallography. It features a temperature-controlled, automated hotel that securely stores protein crystallisation plates. The unit is able to automatically capture high-resolution images of each crystal-tray using visible light and cross-polarised imaging methods,all programmable using the Formulatrix software. Users can also log-in remotely to view the results of their crystallisation experiments and direct the imager to re-image individual plates as needed.

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