THE SWISS -NORWEGIAN BEAM LINES  (General description)

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Synopsis

The mission of the SNBL is to provide scientists from both Norway and Switzerland, from both academia and industry, with increased access to synchrotron radiation. A user on SNBL has access to state-of-the-art, custom-designed instrumentation for diffraction and absorption experiments. Both partner countries have relatively large and exceptionally active scientific communities using X-ray diffraction and absorption as their main probes; for these groups the amount of public beamtime offered by ESRF was insufficient from day one, and this is the raison d’être of the Swiss-Norwegian Beam Lines at ESRF. Nowadays, it is fully understood by the  scientific community that many of the most challenging problems in structural crystallography can be solved only with the use of synchrotron radiation, and even  then, often enough, only by harnessing the combined power of two or more experimental techniques (such as, e.g., powder and single-crystal diffraction). The SNBL has four such different experimental techniques, which are distributed over two beamlines, and presently include:

• High-resolution single-crystal diffractometry

• Large-area diffraction imaging

• High-resolution powder diffractometry

• EXAFS spectrometry

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Events

1000 publications from SNBL!

 
Swiss-Norwegian workshop on Simultaneous Raman-X-ray diffraction/absorption studies for the in situ investigations (booklet)

High gas pressure meeting (program)

Swiss-Norwegian Seminar "Synchrotron Radiation in Studies of Nanoscaled Materials"

Highlights

Features of the secondary structure of a protein molecule from powder diffraction data

Protein powder diffraction is shown to be suitable for obtaining de novo solutions to the phase problem at low resolution via phasing methods such as the isomorphous replacement method. Two heavy-atom derivatives (a gadolinium derivative and a holmium derivative) of the tetragonal form of hen egg-white lysozyme were crystallized at room temperature. Acta Crystallographica Section D: Biological Crystallography, 2010

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