HZB contributions to special edition on Ultrafast Dynamics with X-ray Methods
At the end of his contribution, Phillippe Wernet makes a great arch from the past (Opticae Thesaurus, 1572) of research with light to the future. © Wikimedia cc
In this theme issue leading researchers discuss
recent work on the ultrafast electronic and structural
dynamics of matter using a new generation of short
duration X-ray photon sources. © Royal Society
In the new special issue of the "Philosophical Transactions of the Royal Society of London", internationally renowned experts report on new developments in X-ray sources and ultrafast time-resolved experiments. HZB physicists have also been invited to contribute.
Almost 350 years after Isaac Newton's ground-breaking paper "Theory of Light and Colors (1671)", the world's oldest scientific journal “Philosophical Transactions” is now once again dedicated to light. The special issue on “Ultrafast Dynamics with X-ray Methods” is aimed at researchers who want to investigate biological, chemical or physical processes and obtain an overview of new developments in light sources and the methods available there. Dynamic processes in materials can be analyzed with high resolution and short pulses at X-ray light sources using ultrafast methods.
Femtoslicing and BESSY VSR
The special issue provides a comprehensive overview of current advances in the generation of ultra-short X-ray pulses by light sources such as Free Electron Lasers (FELs), High Harmonic Generation (HHG) laser sources and synchrotron radiation sources. An article in collaboration with Dr. Karsten Holldack, HZB, presents FEls and Laser sources but also classifies storage ring based methods such as “Femtoslicing” and BESSY VSR. These methods combine highly brilliant synchrotron light with a special time structure and thus allow to address unique experimental questions that cannot be answered at other sources. This complements and expands the portfolio of accelerator-based sources.
Ultra fast spectroscopy for photochemistry
An important contribution is dedicated to photochemistry, an area that focuses on processes such as photosynthesis, the dynamics of which are still largely unexplored. Using ultra-fast spectroscopy at FELs, HHG sources or at the synchrotron with BESSY VSR, methods are now available to measure in detail, for example, excitations of metallo-proteins and the subsequent reactions ; such experiments provide data that are indispensable, for example, for understanding photocatalysis of solar fuels. This article was written by Prof. Dr. Philippe Wernet, formerly a senior scientist at the HZB, and now a professor at Uppsala University, Sweden.
To the publications:
Measurement of ultrafast electronic and structural dynamics with X-rays; J. P. Marangos (ed.)
doi: 10.1098/rsta/377/2145
Recent Advances in Ultrafast X-ray Sources; Robert Schoenlein, Thomas Elsaesser, Karsten Holldack, Zhirong Huang, Henry Kapteyn, Margaret Murnane, Michael Woerner
doi: 10.1098/rsta.2018.0384
Chemical interactions and dynamics with femtosecond X-ray spectroscopy and the role of X-ray free-electron lasers; Philippe Wernet
doi: 10.1098/rsta.2017.0464
- Catalysis research at HZB gets new facilityAs part of the CatLab project, HZB has acquired a unique facility for measuring the catalytic performance of thin-film catalysts. Built by ILS in Adlershof, it has now been delivered. The facility consists of a total of eight chemical reactors in which catalytic systems can be tested. At over €2.5 million, this is the largest single investment in the CatLab project.
- Protein crystallography at BESSY II: faster, better and more and more automaticMany 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.
- 5000th protein structure at BESSY II: Starting point for a COVID drugMany 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.