News & Scientific Highlights
Towards understanding of human betacoronavirus HKU1 life cycle
Researchers from China and USA join forces with Swiss Light Source (SLS) macromolecular crystallography (MX) beamline scientists in a study, which aims at understanding an important step in the life cycle of the human betacoronavirus HKU1.
1000 Structures solved at X06DA-PXIII
The macromolecular crystallography beamline X06DA-PXIII has reached 1,000 structures in the Protein Data Bank (PDB) on February 22, 2017.
First protein structure solved using the JUNGFRAU detector!
JUNGFRAU is a charge-integrating, two-dimensional pixel detector developed at the Paul Scherrer Institut for use at free-electron lasers, in particular SwissFEL, and synchrotron light sources. On the 10th October, the first protein crystallography experiment using the JUNGFRAU detector, was performed at the beamline X06SA (PXI) of the Swiss Light Source by the members of the Protein Crystallography and Detectors groups at PSI.
Call for expressions of interest: Beamline partners at the SLS for PX II and PX III
We invite companies and institutions to secure access to the beamlines X10SA/PX II and X06DA/PX III through a long term contract.
Experiment in a hovering droplet
At the PSI, the exact structure of proteins is deciphered in the standard way, with X-rays. Now two PSI researchers have used a clever trick to advance this method further: Instead of pinning down the proteins, they are studying them within a levitating drop of liquid.
First EIGER X 16M in operation at the Swiss Light Source
The macromolecular crystallography beamline X06SA at the Swiss Light Source, a synchrotron operated by Paul Scherrer Institute, is the first one in the world to upgrade its detector to an EIGER X 16M.
In Situ Serial Crystallography Workshop at the SLS
The Macromolecular Crystallography group at SLS is organizing a three days workshop on in situ serial crystallography (http://indico.psi.ch/event/issx) between November 17 and 19, 2015. It will be dedicated in the presentation of a novel method facilitating the structure determination of membrane proteins, which are highly important pharmaceutical targets but are difficult to handle using 'classical' crystallographic tools. Designed for 20 Ph.D. students, postdocs and young scientists from both academia and industry, the workshop will consist of introductory lectures, followed by hands-on practicals on in meso or lipidic cubic phase (LCP) crystallization, on in situ serial crystallography data collection using a micro-sized beam and on data processing.
New insight into receptor signalling
A team of 72 investigators across 25 institutions including researchers from the Paul Scherrer Institut obtained the X-ray structure of a rhodopsinàarrestin complex, which represents a major milestone in the area of G-protein-coupled-receptor (GPCR), a protein family recognized in the award of the 2012 Nobel Prize in Chemistry.
Together, not alone
Decoding biomolecules at SwissFEL and SLSProteins are a coveted but stubborn research object. A method developed for x-ray free-electron lasers and PSI’s future SwissFEL should now help researchers to make good headway in this field. It involves x-raying many small, identical protein samples consecutively at short intervals, thereby avoiding the main problem that protein research has faced thus far: producing samples in a sufficient size.