My work in structural biology started with the crystallographic study of sugar
recognition by leguminous lectins, later extended to
include bacterial adhesins involved in establishing
infections. With a shift in focus to bacterial
toxin-antitoxin systems, biomolecular NMR became an increasingly important
- Crystallisation of biological macromolecules and complexes using vapour diffusion and microbatch techniques, using commercially available screens
and custom-optimised solutions.
- X-ray data collection on home X-ray sources, as well as synchrotron beam lines at DESY (Hamburg), ESRF (Grenoble) and
- De novo structure determination by multiwavelength anomalous dispersion (MAD).
- Analysis of protein-protein, protein-sugar and protein-DNA interactions
by means of isothermal titration calorimetry (ITC),
using Microcal Omega and VP-ITC instruments.
- Analysis of the thermodynamic stability of proteins and protein-ligand complexes by means
of differential scanning calorimetry (DSC), using a Microcal VP-DSC instrument.
Spectroscopy and optical methods
- Circular dichroism spectroscopy (CDS) for thermal unfolding studies and quality control of proteins.
Biomolecular NMR spectroscopy
- Data collection on Bruker and Varian instruments.