Available Services

Many workflows available in other Infrastructural Units of the National Facility for Structural Biology may require a rapid sample quality control verification (if not performed by the users) or a step of sample optimisation, for instance via size-exclusion chromatography just prior to experiments. These services, which differ from the full characterisation of the macromolecular sample because of their ancillary role with respect to other IU workflows, may only be requested in combination with such workflows.

We offer access to expert support in isolating and purifying proteins from a variety of biological sources. We offer customisable workflows, including cell lysis via sonication or homogenization, depending on any given sample’s specific requirements. The service can accommodate both purification from standard small and medium-volume lysates, or isolation from large-volume sample preparations, ensuring flexibility for different experimental needs. Our purification techniques include affinity, ion exchange, and size-exclusion chromatography, delivering (when possible) high-quality proteins suitable for downstream applications such as structural analysis or functional assays.

The Biophysics Unit is equipped with instruments designed to determine the strength and biophysical properties of macromolecular or protein-ligand interactions, including association and dissociation constants, as well as stoichiometry of binding. Available techniques include isothermal titration calorimetry, microscale thermophoresis, and bio-layer interferometry (which can also be utilized for quantifying known components in complex mixtures).

Structural biology and biochemical assays often require sample optimization to achieve stability and homogeneity, while understanding the oligomerisation state and precise composition of macromolecular complexes is crucial for unravelling their architecture. To address these needs, the Biophysics Unit offers a service leveraging various instruments to determine the molecular weights of species in solution and their thermal stability parameters. Techniques utilized include mass photometry, SEC-MALS, dynamic light scattering, and nanoDSF.