The aim of our collaboration is to solve the structures of proteins and protein complexes for exploring the relationship between structure, interaction-patterns and protein function. Diffraction quality crystals were grown of activated and proenzyme MASP-2 in complex with peptide inhibitors, human and Plasmodium falciparum calmodulin in complex with a target peptide, and porcine acylaminoacyl peptidase. X-ray diffraction experiments on these crystals using the diffractometer greatly facilitated crystal optimization and collection of good quality diffraction data at synchrotron sources. In new collaborations with research groups of the HAS-RCNS we started crystallizing the Dj-1 and DAAO proteins. X-ray diffraction data collected from crystals of S100 protein complexes and solving the structures helped to identify undesired crystal forms containing the uncomplexed protein.

Péter Gál - Veronika Harmat - Károly Liliom - Gábor Mező - László Nyitray - Gábor Pál - Attila Reményi - Kálmán Tory - Beáta Vértessy G.


Report I. 2015. november