Structure/function relationship of enzymes, metallo-enzymes and metallo-proteins. The mechanism of action of enzymes is probed by determining the structure of the native molecule and of its adducts with substrate or substrate-analogues, intermediates or transition-state analogues  by X-ray crystallography (kinetic crystallography is also used) and by X-ray absorption spectroscopy (XAS). Metalloproteins involved in metal trafficking in prokaryotic organisms are investigated by the same techniques.

The available crystallographic facilities include:

Oxford Xcalibur PX Ultra diffractometer equipped with an Onix CCD detector system mounted on a four circle goniometer using a Enhance Cu source. An Oxford Cryosystem cryogenic apparatus is available for data collection at liquid nitrogen temperatures.

Computer facilities consist on several dedicated workstations.

Synchrotron radiation for XAS, MAD or ultra-high resolution structure determination is yearly available on a group basis at the Elettra (Trieste), Hamburg EMBL outstation c/o DESY and the ESRF in Grenoble.

The laboratory is fully equipped for protein crystallization screening techniques and crystal growth optimization.

Molecular biology techniques are also used for protein expression mutagenesis studies.

The Laboratory of Protein Crystallography and X-ray Absorption Spectroscopy of the University of Siena is a dedicated center for structure-function studies of proteins and enzymes, with particular emphasis on metallo-proteins and metallo-enzymes.

The main research interest is to elucidate the reaction mechanisms of enzymes and the function of metal transport proteins. Major tools are protein crystallography, X-ray absorption spectroscopy (XAS) on metallo-proteins to gain insight into the chemistry involved in enzymatic catalysis and other biochemical reactions.