The aim of our group is to determine three-dimensional structures of macromolecules with the single particle electron cryomicroscopy technique. Our work is mainly focused on spliceosomal components called snRNPs to obtain structural information about the eucaryotic pre-mRNA splicing. Apart from that we are working on ribosomal, viral and oxygen carrier projects. More detailed information is provided on our group website.
Press Releases & Research News
Holger Stark and his team have broken a crucial resolution barrier in cryo-electron microscopy. The scientists succeeded in observing single atoms in a protein structure and taking the sharpest images ever with this method. Such unprecedented details are essential to understand how proteins perform their work or cause diseases in the living cell. The technique can in future also be used to develop active compounds for new drugs.
Tuberculosis still represents the infectious disease with the highest fatality numbers and is caused by mycobacteria. The fatty acid biosynthetic factory is an important target in the fight against this infectious bacterium. Göttingen researchers have now discovered a protein that commands and controls FAS function. This finding not only opens up new therapeutic venues, particularly against tuberculosis. In biotechnological applications this new control unit enables the generation of tailor-made fatty acid synthases.
Macromolecular machines in 3D: The complex world of complexes
Tiny nano machines called macromolecular complexes participate in the most fundamental biological processes. The high-resolution three-dimensional (3D) structure of these complexes and their dynamic behavior can be studied by cryo electron microscopy. The molecular movies that can be obtained for these nano machines contribute tremendously to our understanding of molecular processes at a structural level. (in German)