We are studying the crystal structures of various amino acids, peptides and proteins, either alone or in complexes with other compounds.
Above is an artistic impression of the model enzyme chorismate mutase in action. Yellow colored chorismate molecules coming in from the left are transmuted via a bicyclic transition state (here depicted with a light orange transition state analog) to prephenate, shown in orange. There was a decade-long debate on how this enzyme achieves its catalytic efficiency, which has now been resolved experimentally.
What we do
Single crystals are used as X-ray diffraction analysis to determine molecular 3-D structure, such as products related to potential drugs.
But first and foremost we make fundamental investigations of the properties of natural substances such as amino acids and peptides and targeted design of new types of organic materials with useful properties.
Closely tailored molecules works as building blocks in the so-called super molecular synthesis ("crystal engineering").
Protein crystallography is the major technique for the structure elucidation of proteins and other macromolecules. Our main interest is in medically relevant systems, such as anti-cancer antibodies and bacterial toxins, in particular those involving protein-carbohydrate interactions.
In several projects we are involved in developing drugs (structure-based drug design).