The SLS Group for Macromolecular Crystallography
MX in a nutshell
The Macromolecular Crystallography group at the SLS is active in the study of large molecule structures, such as proteins, DNA, RNA, which in cristalline form can be investigated using X-ray diffraction techniques. In particular, the group is responsible for the operation of three beamlines, two undulator ones (X06SA and X10SA), and a superbend beamline (X06DA).
Scientists decode the structure of the enzyme responsible for the ethane fixation by – beside others – using the SLS.
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.