Jan Lüning heads HZB Institute for Electronic Structure Dynamics
The HZB Institute for Electronic Structure Dynamics, newly founded on 1 May, develops experimental techniques and infrastructures to investigate the dynamics of elementary microscopic processes in novel material systems. This will help to optimise functional materials for sustainable technologies.
Prof. Dr. Jan Lüning is an internationally recognised expert in research with synchrotron radiation. Before joining HZB in 2018, he was a professor at Sorbonne University in Paris and worked at the French synchrotron SOLEIL.
Three groups belong to the institute: Dr Ulrich Schade's group operates the IRIS infrared beamline at the BESSY II synchrotron radiation source. He examines molecular processes in novel functional materials that enable, for example, energy conversion or catalytic water splitting.
The group "Ultra-Short-Time Laser Spectroscopy" led by Dr. Iain Wilkinson works in the laser laboratories ULLAS and LIDUX and investigates the dynamics of reactions in aqueous solutions and at aqueous interfaces on ultra-short time scales.
The third group, led by Dr. Christian Schüssler-Langeheine and Dr. Niko Pontius, operates the Femtoslicing Facility at BESSY II and conducts research on materials with complex phase transitions that have the potential to make electronic and magnetic devices smaller, faster and more energy efficient.
The institute's research activities are part of the Helmholtz Association's Programme-Oriented Funding (POF IV) in the Research Field Matter.
red.
https://www.helmholtz-berlin.de/pubbin/news_seite?nid=23708;sprache=en
- Copy link
-
Protein crystallography at BESSY II: faster, better and more and more automatic
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.
-
Humboldt-Fellow at HZB-Institute for Solar Fuels: Alexander R. Uhl
Alexander R. Uhl, UBC Okanagan School of Engineering in Kelowna, Canada, aims to develop with Roel van de Krol from the HZB Institute for Solar Fuels an efficient and inexpensive photoelectrolyser for producing hydrogen using sunlight. His stay is being funded by the Alexander von Humboldt Foundation.
-
5000th protein structure at BESSY II: Starting point for a COVID drug
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.