Fast and accurate data collection for macromolecular crystallography using the JUNGFRAU detector.
On the 7th to 12th of August 2018, a collaborative group of scientists from the Paul Scherrer Institute and members of the LeadXpro and Heptares pharmaceutical companies led by Karol Nass (PSI macromolecular crystallography MX-SLS group) performed the first serial femtosecond crystallography (SFX) pilot user experiment at the SwissFEL X-ray free electron laser (XFEL).
Since it was first established in 1987, the annual Regio-Meeting has been instrumental in facilitating interactions in the structural biology community in southwestern Germany, the eastern region of France and an expanding area of Switzerland. It is set as an informal event to foster young scientists to discuss their research results in an international context. The 2018 edition will take place in the heart of Switzerland in Emmetten from September 26 to 28, 2018. Registration and abstract submission deadline: September 7, 2018.
A workshop dedicated to the presentation of the in meso in situ serial crystallography (IMISX) method (Huang et al. 2015, 2016 ActaD) for the X-ray structure determination of membrane proteins is organised at the Swiss Light Source at PSI for the second time. It will be held between November 27 and 29, 2017.
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.
The macromolecular crystallography beamline X06DA-PXIII has reached 1,000 structures in the Protein Data Bank (PDB) on February 22, 2017.
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.
We invite companies and institutions to secure access to the beamlines X10SA/PX II and X06DA/PX III through a long term contract.
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.