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 im schwebenden Tropfen
Der genaue Aufbau von Proteinen wird am PSI standardmässig mittels Röntgenstrahlung entschlüsselt. Nun haben zwei PSI-Wissenschaftler diese Methode trickreich weiterentwickelt: Anstatt die Proteine zu befestigen, untersuchten sie die Proteine in einem frei schwebenden Flüssigkeitstropfen.
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.
Gemeinsam statt einsam
An SwissFEL und SLS Biomoleküle entschlüsselnProteine sind ein begehrtes, aber widerspenstiges Forschungsobjekt. Eine für Freie-Elektronen-Röntgenlaser wie dem zukünftigen SwissFEL des PSI entwickelte Methode soll ihre Erforschung nun ein grosses Stück vorantreiben. Dabei werden viele identische, kleine Proteinproben in kurzen Abständen hintereinander mit einem Röntgenstrahl durchleuchtet. Damit wird ein bisheriges Hauptproblem der Erforschung von Proteinen umgangen: Proben in ausreichender Grösse herzustellen.