SDU: Software for high throughput automated data collection at SLS MX
The Smart Digital User (SDU) software for unattended data collection has been deployed at the macromolecular crystallography beamlines at the Swiss Light Source.
A new spin on sample delivery for membrane proteins
Proteins hover in front of the X-ray beam at a Swiss Light Source beamline. Now, spinning thin films bring on board these trickiest of proteins.
Lighting up the appealing world of hybrid perovskites
Researchers from Italy, in collaboration with the Paul Scherrer Institut, successfully used the macromolecular crystallography beamline X06DA-PXIII at the Swiss Light Source to characterize promising perovkites materials used in solar cells and other photodetector devices.
How to get chloride ions into the cell
A molecular movie shot at PSI reveals the mechanism of a light-driven chloride pump
PSI researchers have developed a new method to attach proteins to the surface of virus-like particles.
Nanobodies against SARS-CoV-2
In a study published in EMBO Journal, researchers at the Max Planck Institute for Biophysical Chemistry, Göttingen, Germany, developed nanobodies that efficiently block the coronavirus SARS-CoV-2 and its variants. The high resolution structural characterization was performed at the X10SA crystallography beamline at the Swiss Light Source.
How ethane-consuming archaea pick up their favorite dish
Scientists decode the structure of the enzyme responsible for the ethane fixation by – beside others – using the SLS.
On-demand sample delivery article highlighted in "Applied Physics Letters"
An article on the on-demand sample delivery and protein crystallography using acoustic levitation has been selected in an Applied Physics Letters collection of papers on technology and application of acoustic tweezers.
Crystal structure of SARS-CoV-2 Orf9b in complex with human TOM70 suggests unusual virus-host interactions
In a study published in Nature Communications, researchers at the NHC Key Laboratory of Systems Biology of Pathogens in Beijing, China, in collaboration with the Paul Scherrer Institut characterize the interactions of SARS-CoV-2 orf9b and human TOM70 biochemically, and they determine the 2.2 Å crystal structure of the TOM70 cytosolic domain with a bound SARS-CoV-2 orf9b peptide.