The quest for tastier, more sustainable vegan cheese has led Swedish food company Cassius AB to take a closer look at cheese protein structures. Using synchrotron X-rays at MAX IV, Cassius are searching for the perfect scientific recipe for plant-based cheese.
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.
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.
A group of researchers have successfully soaked proteins into large protein crystals, marking a hitherto never reported achievement. The X-ray diffraction data, which were collected on MAX IV’s BioMAX beamline, indicate that the guest proteins could follow at least some of the hosts’ structures signifying a so far unparalleled step towards using crystallographic methods to solve guest protein structures. Such insights could pave the way for major advances in biotechnology, material science, and structural studies.