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Prof. W. Saenger Institute of Chemistry / Crystallography
Freie Universität Berlin

Takustr. 6
D-14195 Berlin

Secretary's Office: Room

phone +49-30-838-53410
fax     +49-30-838-56702

E-Mail: saenger@chemie.fu-berlin.de



Protein X-ray crystallography, molecular biology, biochemistry, molecular dynamics, light scattering, DNA-binding proteins, photosystem I, oligosaccharides, hydrogen bonding, crystal nucleation.


The main emphasis of our research is the structure determination of biological macromolecules at atomic detail by crystallographic methods. Proteins under study are: tetracyclin repressor and its complex with operator DNA, a DNA helicase, DNA methyltransferases, purine nucleoside phosphorylase, arylsulfatase, peptide synthetases, and the membrane protein complex photosystem I. Molecular biology and biochemistry are used in the production, purification and functional characterization of several of these proteins, and their biological activity is monitored by absorption, fluorescence and circular dichroism spectroscopy. After successful structure determination, functional mechanisms are studied by genetically mutating amino acid residues located in strategic positions ("protein design") and by theoretical methods (molecular dynamics). Work is also in progress on cyclodextrin inclusion complexes to study non-covalent intermolecular interactions and hydrogen bonding and on oligosaccharides of the starch and cellulose type. Since the crystallization of proteins is only poorly understood, aggregation of molecules and crystal nucleation are investigated by static and dynamic light scattering.
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