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During its active period (1972-2005), the department of Structure Research witnessed and contributed to the preparation, crystallization and structural analysis of proteins. This work developed from a handful of small and stable proteins for protein crystallography to very large and fragile bio-molecular assemblies. The modern process comprises protein expression, purification, and refolding as well as gene cloning, crystal structure analysis, structure-guided mutational analysis to assist in functional interpretation, and activity and stability studies. During this 33 period, the focus of the department´s work moved to structural and functional analyses of large complex aggregates by crystallography with an emphasis on proteins relevant in medicine, pharma research, and crop science. The goal is to assist in design and development of functional ligands often in collaboration with external and internal academic and industrial partners.

Presently, the emeritus group has narrowed its in-house research activities to the preparation, crystallization, and structural and functional analysis of Ser-Thr kinases, of the Mdm2 E3 ubiquitin-protein ligase, the spire actin nucleator, the 20S proteasome structure from yeast and human sources, the human immunoproteasome, the human dipeptidyl peptidases 8 and 9 (DPP 8/9), yeast class II HADC complex, and further development of protein crystals annealing and improvement.

The research group consists of one postdoctoral fellow (“Nobel Laureate Fellowship” of the MPG), one doctoral student (promotion in May 2019), a part time postdoctoral fellow, and of a part time secretary (supported by the MPIB). The MPIB provides a spacious and comfortable space in which to conduct research. The laboratory space and equipment is rented from the TUM and the Proteros biostructures company located within walking distance from the MPIB. Scientific service is available at the MPIB and at Proteros. 


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 “Proteins are nice, crystals are nicer”  “Photosynthesis is the most important chemical reaction on Earth.” So proclaimed the Royal Swedish Academy of Sciences in 1988 in its announcement that Robert… more

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