In clinical practice it is well established that type O blood, which lacks A and B antigens on the red blood cells, can be safely used in universal blood transfusions for any ABO blood group. Serious or even fatal immune reactions may occur if one receives incompatible blood from a donor. How might we mitigate the risks for low donor supply or unusable blood in emergencies? Research groups from the Technical University of Denmark (DTU) and Lund University now report in Nature Microbiology, an enzymatic conversion method to create ABO-universal blood, a major leap towards human blood that could potentially enable live-saving blood donations to anyone, without negative immune response or the need for matched donor-recipient blood types. Data for the structural determination of key enzymes used in conversion of the ABO-universal blood was collected at MAX IV’s BioMAX beamline.
Kilohertz serial crystallography to film nature’s choreography
A collaborative work between MAX IV and Paul Scherrer Institute researchers investigated a setup to conduct serial and time-resolved macromolecular crystallography at MAX IV. The experiment shows that the setup, based on JUNGFRAU detector and Jungfraujoch data-acquisition system, can provide a molecular moving picture of up to 500 microseconds in resolution of protein dynamics – providing ten times finer details than the previously available method. The setup is in the works to be made available at MicroMAX beamline.
Bacterial biomass conversion for renewable fuels
Imagine this future. Vehicles and machinery primarily powered by renewable organic matter, a resource far better for the planet’s health than today’s predominate fossil fuels. What factors stand in the way for a global power transition to competitive, industrial-scale biomass conversion? A study in Nature Communications reveals one key piece of the puzzle using bacterial enzymes. At MAX IV’s BioMAX beamline, an international team of scientists has determined important rate-limiting steps of lignocellulose breakdown, a major hurdle in efficient biomass processing. The discovery holds promise for a significant reduction in manufacturing costs and faster adoption of new biomass-derived fuels to market.
Fragment-based research on potent, non-covalent inflammatory drugs goes forward
Researchers’ collaborative efforts from Denmark and Germany used BioMAX beamline to discover selective, non-covalent inhibitors of Keap1– a common target against oxidative stress and inflammation. The result is a potent antithesis of the currently available drugs acting as covalent inhibitors.
New potential drug for type 2 diabetes treatment explored at MAX IV
The drug discovery company Implexion Pharma and researchers from Lund University have explored new potential drug candidates for type 2 diabetes using X-ray crystallography research techniques at MAX IV.
MAX IV research contributes to the development of new cancer drugs
In the battle against cancer, scientists from the drug discovery company Sprint Bioscience and researchers from MAX IV have taken important steps together toward developing new and more efficient cancer drugs with the help of fragment screening by X-ray crystallography.
Mapping the genetic tools of fungi for fuel production
Fungal enzymes play an important role in the breakdown of plant cell walls during plant degradation. An international collaboration of researchers explored the auxiliary activities 7 (AA7) enzyme family, characterizing four fungal enzymes and uncovering a novel class of flavo-enzymes, exemplified by oligosaccharide dehydrogenase. The enzymes fuel the activity of lytic polysaccharide monooxygenases (LPMOs) in the challenging process of crystalline cellulose degradation. The study, published in Nature Communications, offers promise for tuning the efficiency of enzymatic breakdown processes of biomass feedstocks used in energy and biomaterial production.
Tackling SARS CoV-2 viral genome replication machinery using X-rays
An international collaboration between the UCL School of Pharmacy, the Lund Protein Production Platform (LP3) and ESS, through its DEMAX platform, have performed biophysical and structural studies of three non-structural proteins from the novel coronavirus, SARS CoV-2, the causative agent of COVID-19. In the spring of 2020, they managed to solve and started to analyse one of these proteins, Nsp10, by using the BioMAX beamline at MAX IV Laboratory. Early October published their results in the International Journal of Molecular Sciences.
Clues to block replication of SARS-CoV-2 found with FragMAX platform
An international collaboration of scientists identified four fragments that interact with the nsp10 protein of the SARS-CoV-2 virus using the FragMAX platform and BioMAX beamline. The fragments could be used to develop inhibitors that supplant key enzymes activated by the protein—an application which holds potential to block the viral replication process.
Scientists unlock secrets of surface receptor activation opening door to engineer plant-microbe interactions
In a study combining structural biology, biochemical and genetic approaches, scientists showed that plant cell-surface receptors employ a mechanism for error correction responsible for the control of receptor activation and signaling select bacterial symbionts. This demonstration opens the door to potentially manipulating such receptors’ binding sites in legumes and other organisms in the future.