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Dr. Tobias Schrader

Knowing the three dimensional structure of a protein is a pre-requisite for understanding its function.

Protein x-ray crystallography is a well established tool to obtain structural information on proteins. However, with x-rays as probes the position of hydrogen atoms can hardly be seen.

Here, neutron scattering on protein crystals opens up the possibility to locate hydrogen atoms even at moderate resolutions of 2 Å. Therefore, in collaboration with the FRM II in Garching the BIODIFF, a dedicated instrument for neutron protein crystallography is being built.


The first measurement of Bragg-reflections from a sperm whale myoglobin crystal with the CCD-detector of the BIODIFF instrument is shown above in the first picture on the left. The resulting protein structure is depicted in the picture on the right.

The additional information gained with neutron protein crystallography is for example the identification of unusual hydrogen bonds, the protonation state of side chains and the solvent structure around the protein, just to name a few.

Unfortunately, large protein crystals are required for this method. In order to grow these large crystals, detailed knowledge on the phase diagram of the corresponding protein is required. Also, more understanding of the processes involved in crystallization is desired.

Among other techniques, neutron small angle scattering in combination with in-situ dynamic light scattering and quasi-in-situ static light scattering is especially well suited to follow the crystallization process in real time.

Dedicated effort is put into the development of such techniques to provide more information on the crystal nucleation and growth process.