Crystallography is a biophysical method to measure the structure of a protein in its crystallized form. After protein crystals are successfully produced (for more information please see Protein Purification and Crystallization), the protein structure can be recorded by shooting the crystals with radiation. When the radiation beam hits the crystal, a diffraction pattern can be monitored which is essential to model the complete structure of the protein inside the crystal at an atomic resolution. Our group is using different techniques to measure the crystal structure of our proteins.
XFEL
XFEL
XFEL crystallography gives us the chance to measure time-resolved and steady state protein structures under more physiological conditions namely under room temperature and without radiation damage (see XFEL). For this approach we are using four XFEL facilities worldwide which are LCLS (USA) , SwissFEL (Switzerland), PAL (Korea) and SACLA (Japan).
Synchrotron
Synchrotron
Synchrotron facilities are used in our group to conduct single-crystal X-ray experiments under cryo conditions and room temperature. We are closely working together with the Berkeley Center for Structural Biology and are users of ALS (USA), SSRL (USA) and diamond (UK).
Neutron diffraction
Neutron diffraction
Neutron diffraction, also called neutron scattering, is the third method in our group used to record protein structures. With this method we have the chance to measure nuclei of the atoms in our structure enabling to actually detect protons as well.
We are using the neutron scattering facility of ORNL (USA).
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