MX-Posterprize to Bartosz Sekula, Lodz

Many diseases are linked to malfunctions of proteins in the organism. The three-dimensional architecture of these molecules is often highly complex, but it can provide valuable insights into biological processes and the development of drugs. X-ray diffraction at the MX beamlines of BESSY II can be used to decipher the 3D structure of proteins. To date, more than 5000 structures have been solved at the three MX beamlines. Here, we present a review and an outlook with  Manfred Weiss, head of the research group for macromolecular crystallography. 

Many proteins have a complex architecture that enables biological functions. Molecules can bind to specific sites on a protein and alter its function. A team at HZB has now investigated the Nsp1 protein, which plays a role in infection with the SARS-CoV-2 virus. They analysed protein crystals, previously mixed with molecules from a fragment library, and discovered a total of 21 candidates as starting points for drug development. At the same time, they also decoded the 5000th structure at BESSY II.

Teeth are composites of mineral and protein, with a bulk of bony dentin that is highly porous. This structure is allows teeth to be both strong and sensitive. Besides calcium and phosphate, teeth contain trace elements such as zinc. Using complementary microscopy imaging techniques, a team from Charité Berlin, TU Berlin and HZB has quantified the distribution of natural zinc along and across teeth in 3 dimensions. The team found that, as porosity in dentine increases towards the pulp, zinc concentration increases 5~10 fold. These results help to understand the influence of widely-used zinc-containing biomaterials (e.g. filling) and could inspire improvements in dental medicine.