Principal Investigator: Marjolein Thunnissen
Others: Derek Logan, Yngve Cerenius, Thomas Ursby, Maria Håkansson

The ideal setting for diffraction experiments is a synchrotron capable of producing X-rays. In Lund we are fortunate enough to have a synchrotron, MAX-lab, in which members of the Dept. of Molecular Biophysics have always participated actively. One of the veterans of the MAX II synchrotron is the station for protein X-ray crystallography, called BLI711, based around a so-called multipole wiggler that produces intense X-ray radiation. The wavelength is tuneable from 0.9 Å to 1.5 Å, but too slowly for the implementation of the multiple wavelength anomalous dispersion (MAD) method. Thus in general only single wavelength experiments are performed.

Beam time at I711 is shared between the protein crystallography and chemical crystallography communities. Work done at the beamline has featured in more than 300 publications (see the beamline web page for details) since 1998, the vast majority of which are in the protein crystallography field and a good number of which are in high profile journals.

Protein crystallography at MAX-lab is in a significant and exciting expansion phase. A new beamline has being constructed under the name Cassiopeia (more prosaically BLI911) which will eventually feature five experimental stations. One of these is optimized for the MAD method, providing Scandinavia's first resource of this type. The MAD station has been open for users since May 2005 and will be opened for full MAD data collection in the autumn of 2005. This central user station is complemented by four monochromatic stations at fixed wavelengths chosen to be useful for common heavy atoms used in phase determination by protein crystallography. Two of these monochromatic experimental stations are currently in operation.

The beamline has recently been complemented by a medium-throughput facility for protein crystallization. The use of robotic pipetting technology has enabled the reduction of the volume of protein crystallization drops by a factor of 10, to around 100 nanolitres. Thus experiments can be done with a much more modest supply of protein than was previously required. The lab has been equipped with a Mosquito pipetting robot and a CrystalPro robot for automatic inspection of the crystallization plates. For further details contact Derek Logan, or Maria Håkansson at MAX-lab.

This project is a Swedish-Danish cooperation that has been made possible due to generous funding from the Knut and Alice Wallenberg Foundation, and from the Danish Biotechnology Instrumentation Center DABIC. The participation of our industrial partners, Astra Zeneca and Novo Nordisk is also of fundamental importance for the project.

Please consult the Cassopieia Web page, for more details and updates.