Info message
Ce contenu n'est pas disponible en français.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.
Expérience dans une goutte en lévitation
La structure exacte des protéines est normalement déterminée au PSI par la technique de diffraction des rayons X. Deux scientifiques du PSI viennent de l’améliorer de façon astucieuse: au lieu d’immobiliser les protéines, ils les ont étudiées dans une goutte de liquide en lévitation.
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.
L’union fait la force
Décrypter les molécules au SwissFEL et à la SLSLes protéines sont un objet de recherche convoité, mais récalcitrant. Leur étude est aujourd’hui facilitée par une nouvelle méthode développée à l’aide d’un laser à rayons X à électrons libres comme le futur SwissFEL du PSI. Elle consiste à exposer à intervalles rapprochés de petits échantillons identiques de protéines à de la lumière de type rayons X. On contourne ainsi un problème majeur auquel la recherche sur les protéines s’est heurtée jusqu’ici: produire des échantillons de taille suffisante.