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- 4000th protein structure decoded at BESSY IIThe 4000th structure is the molecule FKBP51, which is linked to stress-induced diseases such as depression, chronic pain and diabetes. The team led by Prof. Felix Hausch, TU Darmstadt, is using the knowledge of the three-dimensional structure to develop new strategies for the design of suitable drugs.
- Fine particles back into the raw material cycleIndustrial processes always produce fine-grained residues. These rarely find their way back into the industrial value chain, but are usually disposed of and represent a potential environmental risk. The FINEST project records and investigates various of these fine-grained material flows with the aim of developing new concepts to keep them in the cycle and safely dispose of remaining residues.
FINEST was successful in the Helmholtz Association's sustainability competition and will now receive 5 million euros in funding.
- Deputy Prime Minister of Singapore visits HZBOn Friday, 17 June, a delegation from Singapore visited HZB. Heng Swee Keat, Deputy Prime Minister of Singapore, was accompanied by the Ambassador to Singapore in Germany, Laurence Bay, as well as representatives from research and industry.
- HZB coordinates European collaboration to develop active agents against CoronaX-ray structure analysis at BESSY II enables the systematic testing of many thousands of molecules that could inhibit the reproduction and virulence of SARS-CoV2 viruses. Now, a team at HZB with partners from Austria and the Czech Republic has set up the NECESSITY project to investigate more than 8000 compounds in a high-throughput procedure and develop active agents against COVID-19.
- BESSY II: universal mechanism of regulation in plant cells discoveredIn pioneering work, a German-Japanese research team at BESSY II has been able to determine the 3D structure of a metalloprotein that plays an important role as a catalyst in all plant cells. This involves the DYW deaminase domain of what is referred to as the RNA editosome. The DYW domain alters messenger RNA nucleotides in chloroplasts and mitochondria and contains a zinc ion whose activity is controlled by a very unusual mechanism. The team has now been able to describe this mechanism in detail for the first time. Their study, published in Nature Catalysis, is considered a breakthrough in the field of plant molecular biology and has far-reaching implications for bioengineering.
- BESSY II: New insights into switchable MOF structures at the MX beamlinesMetal-organic framework compounds (MOFs) are widely used in gas storage, material separation, sensor technology or catalysis. A team led by Prof. Dr. Stefan Kaskel, TU Dresden, has now investigated a special class of these MOFs at the MX beamlines of BESSY II. These are "switchable" MOFs that can react to external stimuli. Their analysis shows how the behaviour of the material is related to transitions between ordered and disordered phases. The results have now been published in Nature Chemistry.
- “The gain in insights for structural biology has continued for five decades”
Prof. Dr. Udo Heinemann works at the Max Delbrück Center for Molecular Medicine, where he has been researching in structural biology for 40 years. From 2008 to 2012, he was a member of the Advisory Board for the Protein Data Bank in Europe. In an interview, he speaks of the value added by the Protein Data Bank for research today, and why it is important that there are specialised beamlines for structural biology analysis in Berlin.
- New substance library to accelerate the search for active compoundsIn order to accelerate the systematic development of drugs, the MX team at the Helmholtz-Zentrum Berlin (HZB) and the Drug Design Group at the University of Marburg have established a new substance library. It consists of 1103 organic molecules that could be used as building blocks for new drugs. The MX team has now validated this library in collaboration with the FragMAX group at MAX IV. The substance library of the HZB is available for research worldwide and also plays a role in the search for substances active against SARS-CoV-2.
- User research at BESSY II: Insights into the visual perception of plantsPlants use light not only for photosynthesis. Although the plant cell does not have eyes, it can still perceive light and thus its environment. Phytochromes, certain turquoise proteins, play the central role in this process. How exactly they function is still unclear. Now a team led by plant physiologist Jon Hughes (Justus Liebig University Gießen) has been able to decipher the three-dimensional architecture of various plant phytochrome molecules at BESSY II. Their results demonstrate how light alters the structure of the phytochrome so that the cell transmits a signal to control the development of the plant accordingly.
- Coronavirus SARS-CoV2: BESSY II data accelerate drug developmentA coronavirus is keeping the world in suspense. SARS-CoV-2 is highly infectious and can cause severe pneumonia with respiratory distress (COVID-19). Scientists are doing research in order to prevent the viruses from multiplying. A team from the University of Lübeck and from Helmholtz Centre for Infection Research (HZI) has now found a promising approach. Using the high-intensity X-ray light from the Berlin synchrotron source BESSY II, they have decoded the three-dimensional architecture of the main protease of SARS-CoV-2. This protein is involved in the reproduction of the virus. Analysing its 3D architecture allows the systematic development of drugs which inhibit the reproduction of the virus.
- New detector accelerates protein crystallography
Last week a new detector was installed at one of the three MX beamlines at HZB. Compared to the old detector the new one is better, faster and more sensitive. It allows to acquire complete data sets of complex proteins within a very short time.
- Cancer research at BESSY II: Binding Mechanisms of Therapeutic Substances DecipheredIn tumor cells, the DNA is altered in comparison to normal body cells. How such changes can be prevented or inhibited is an exciting field of research with great relevance for the development of cancer treatments. An interdisciplinary team has now analysed the possible binding mechanisms in certain therapeutic substances from the tetrazole hydrazide group using protein crystallography at BESSY II.
- New sample holder for protein crystallographyAn HZB research team has developed a novel sample holder that considerably facilitates the preparation of protein crystals for structural analysis. A short video by the team shows how proteins in solution can be crystallised directly onto the new sample holders themselves, then analysed using the MX beamlines at BESSY II. A patent has already been granted and a manufacturer found.
- "Molecular scissors" for plastic wasteA research team from the University of Greifswald and Helmholtz-Zentrum-Berlin (HZB) has solved the molecular structure of the important enzyme MHETase at BESSY II. MHETase was discovered in bacteria and together with a second enzyme - PETase - is able to break down the widely used plastic PET into its basic building blocks. This 3D structure already allowed the researchers to produce a MHETase variant with optimized activity in order to use it, together with PETase, for a sustainable recycling of PET. The results have been published in the research journal Nature Communications.
- HZB and Freie Universität Berlin are establishing the joint research group “Macromolecular Crystallography”For eight years, HZB’s “Macromolecular Crystallography” workgroup has been successfully cooperating with the “Structural Biochemistry” research group headed by Prof. Markus Wahl at the Freie Universität Berlin. They are about to intensify this cooperation. The two institutes are establishing a joint research group dedicated to studying the biochemistry of genetic information processing. This research group benefits in particular from access to the three MX beamlines, where it can study protein crystals using the synchrotron light from BESSY II.
- Advancing methodology at BESSY II: Automated evaluation speeds up the search for new active substanceThe macromolecular crystallography (MX) beamlines at the BESSY II X-ray source are specially designed to highly automated structural analyses of protein crystals. With up to now more than 2000 solved structures of protein molecules, these beamlines are by far the most productive ones in Germany and are in vigorous demand by groups from either an academic and industrial research area. Now teams from HZB and Philipps-Universität Marburg in Germany have automated the evaluation of data records as well. The newly developed expert system identifies small molecule fragments bound to proteins in the raw X-ray diffraction data. These fragments represent suitable starting points for the development of an active substance. Using a series of 364 samples, the collaborating partners demonstrated that the expert system works reliably and can speed up the search for a suitable active agents.
- 1000th protein structure decoded at BESSY IIIn July of this year, the 1000th protein structure based on measurements obtained at BESSY II was published. The molecule in question belongs to a class of proteins called sirtuins, which are involved in aging, stress, and metabolic processes within the human organism. Bayreuth University’s Prof. Clemens Steegborn and his team uncovered a clever mechanism used by active substances to inhibit sirtuin activity. The results have been published in the renowned scientific journal Proceedings of the National Academy of Sciences, USA, and could potentially point the way to new cancer therapies.
- Proteinstrukturen besser erforschenFeierlich eingeweiht: Der neue Pilatus-Detektor für die Kristallographie ist nun einsatzbereit
- Von 1 auf 500… - 500ste Protein-Struktur an BESSY II entschlüsseltHaare, Haut, Blutkreislauf und Nervensystem – alles wird von winzigen biologischen Bausteinen gesteuert. Wer nach diesen kleinsten Bausteinen des Lebens forscht, landet automatisch bei ihnen: den Proteinen. Um diese Grundbausteine des Lebens und die Vorgänge, die sie bewirken, besser zu verstehen, archivieren Wissenschaftler in aller Welt ihre Erkenntnisse über Proteine in einer gemeinsamen Datenbank. Die HZB-Forschungsgruppe Makromolekulare Kristallografie (MX) stellt Nutzern am BESSY II die Technik zur Verfügung, mit der sie Protein-Strukturen entschlüsseln können. Vor kurzem wurde die bereits 500ste Struktur an diesen MX-Strahlrohren des HZB von Wissenschaftlern der Bayer Healthcare Pharmaceuticals Berlin entschlüsselt.