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The research interests of the structural biology laboratory are centered around the analysis of the atomic-resolution structure of biological molecules. The main technique is macromolecular X-ray crystallography. Our staff currently includes three permanently employed scientists, one technician, 2 postdocs, and about 10 PhD and MsC (Diploma) students. The laboratory has an excellent biocrystallographic infrastructure. We are also regular users of the synchrotron facilities in Hamburg, Grenoble and Trieste.

The laboratory started with protein crystallography in the early 90th. Previously, we were concerned with chemical crystallography of biologically significant small molecules, such as porphyrins and B12 cofactors.

Besides macromolecular X-ray crystallography, we also use other complementary techniques for structure analysis, such as neutron crystallography and X-ray absorption spectroscopy (XAS). For functional studies on biological molecules, we apply a full range of biophysical techniques (UV/VIS, Fluorescence and CD spectroscopy, DSC and ITC microcalorimetry, stopped-flow kinetic equipment) to probe protein stability, enzyme activity, and the interaction of proteins with other proteins, nucleic acids or small molecules. For the production, purification and biochemical analysis of recombinant proteins, we run a fully equipped biochemical laboratory. Our scientific interests include the following topics:

Proteins with a B12 cofactor
Enzymes for industrial biocatalysis
Bacterial conjugation and Plazmid stabilisation
Allergens
S-layer proteins
Xenon for protein crystallography
Enzymes for industrial biocatalysis
Proteins with a B12 cofactor
Xenon for protein crystallography
Allergens
S-layer proteins
Bacterial conjugation and Plazmid stabilisation
 
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Nov.15, 2004         Christoph.Kratky@uni-graz.at                                                                      HOME              UNI GRAZ