The first diffraction experiment with a protein crystal has been performed at the BioMAX beamline at MAX IV Laboratory. After 5 years of designing, building and commissioning of this new beamline, crystals of the protein thaumatin were exposed to X-rays produced by the new MAX IV 3 GeV storage ring and diffraction patterns have been collected. This is a very important milestone for BioMAX and the entire MAX IV project as this shows that everything from the source to the detector is working. The instruments that prepare the beam (undulator, monochromator and focusing mirrors) produce a 40 x 20 μm2 X-ray beam that reaches the protein crystal in the diffractometer producing the diffraction patterns that the detector records. All these parts are not only working but are working together by careful control by the beamline control system. The first experiment was performed with preliminary settings and a lot of work remains to be done in order to achieve the final specifications.
To obtain these diffraction results early in the beamline commissioning phase is a crucial step. It gives confidence for the functioning of the beamline and it will greatly aid the remaining commissioning process. In the autumn of this year BioMAX will be supplemented with an automatic sample changer, the final detector will be installed and a first general call for proposals will be announced.
BioMAX is one of the first-phase beamlines at MAX IV Laboratory and will be a beamline dedicated to protein crystallography. Protein crystals are exposed to X-rays and diffraction patterns are collected. From the patterns the three dimensional structure of the proteins can be determined and this structure gives important information on the function of these molecules. One example of their use, is the way that structural information from proteins is used in modern rational drug discovery programs.