LBR is exceptionally well equipped for biophysics studies. Our biophysical instrumentation includes a number of instruments for characterisation of protein stability, their molecular weight and stoichiometry of proteins complexes, and affinity of biological interactions. These include a qPCR instrument suitable for protein stability measurements, a circular dichroism (CD) spectrometer, isothermal titration calorimeter (ITC), bench top fluorimeter equipped with polarisers and automated titrators, multimode plate readers, multi angle light scattering instrument (SEC-MALS), absorbance spectrometers and analytical ultracentrifuge (Beckman XLI) equipped with absorbance, interference and fluorescence detection systems.
A distinctive advantage of LBR as a research environment is the presence, on campus, of the Swiss Light Source (SLS). The macromolecular crystallography (MX) beamlines perfectly complement the excellent infrastructure of LBR for protein preparation, crystallization, crystallographic computing and structure analysis. We work in close collaboration with the MX group at the SLS in several areas, especially crystallization, in situ diffraction screening and data acquisition.
In LBR there is a state-of-art cryo-EM facility for structural analysis of biological macromolecules and organelles. Cryo-EM provides images of biological macromolecules and organelles in intact hydrated states. Computational image analysis enables three-dimensional reconstruction.
LBR is very well equipped for the imaging of fixed and living eukaryotic cells. Our microscopes are mainly used to monitor subcellular localization of heterologously expressed proteins and to analyze cellular processes.