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Biophysics, Structural Biology and Screening (BiSS)
molecular insights

Structural biology

To understand biomolecular function, as well as to be able to carry out structure-based experiments and drug design, it is mandatory to obtain high-resolution 3D structural information on the molecular system. BiSS carries significant expertise in protein X-ray crystallography and other structural biology techniques.

Macromolecular crystallization

The BiSS laboratory is well equipped with state-of-the-art equipment for high-throughput screening of crystallization conditions. The Mosquito LCP robot allows to set up nanoliter-scale crystallization experiments rapidly for both soluble and membrane proteins.

An automated imaging system for crystallization plates is available, which can be used for imaging with both visible and UV light. Images are centrally stored and can be accessed from an external computer. 

A number of microscopes, including a UV light source, and programmable incubators are also available for more manual screening and optimization. All necessary tools exist for preparing and transporting crystals to synchrotrons for high-resolution data collection. 

The crystallization laboratory is part of the NORCRYST national infrastructure network. 

Crystal testing and data collection

An X-ray diffractometer, also funded through NORCRYST, for crystal testing and data collection has been installed and will be in operation soon.

Crystallographic data collection is routinely carried out at various large European synchrotron infrastructures. The structural biology community at UiB has common block allocation group (BAG) beamtime at the DESY (Germany) and Diamond (UK) synchrotron light sources. In addition, a Norwegian national BAG operates at ESRF (France). Beamtime is frequently available for both X-ray crystallography and small-angle X-ray scattering (SAXS). 

Synchrotron data collection and structure determination are available on a case-by-case collaborative basis, depending on resources. 

Users interested in macromolecular crystallization at BiSS, structure determination, and/or use of the BAG beamtime should contact Petri Kursula