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Acta Cryst. (2014). A70, C1215
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The research reactor Heinz Maier-Leibnitz (FRM II) is a modern high flux neutron source which feeds some 30 state of the art neutron beam instruments. Currently 24 are operational, others in commissioning or under construction. The newly built neutron single crystal diffractometer BIODIFF is especially designed to collect data from crystals with large unit cells. The main field of application is the structural analysis of proteins, especially the determination of hydrogen atom positions. BIODIFF is a joint project of the Jülich Centre for Neutron Science (JCNS) and the FRM II. Typical scientific questions addressed are the determination of protonation states of amino acid side chains (see e. g. [1,2]) and the characterization of the hydrogen bonding network between the protein active centre and an inhibitor or substrate. BIODIFF is designed as a monochromatic instrument. By using a highly orientated pyrolytic graphite monochromator (PG002) the diffractometer is able to operate in the wavelength range of 2.4 Å to about 5.6 Å. Contaminations of higher order wavelengths are removed by a neutron velocity selector. To cover a large solid angle the main detector of BIODIFF consists of a neutron imaging plate in a cylindrical geometry with online read-out capability. A fast Li/ZnS scintillator CCD camera is available for additional detection abilities. An optical CCD-camera pointing at the sample position is used to quickly align the crystal with respect to the neutron beam. The main advantage of BIODIFF is the possibility to adapt the wavelength to the size of the unit cell of the sample crystal while operating with a clean monochromatic beam that keeps the background level low. BIODIFF is equipped with a standard Oxford Cryosystem "Cryostream 700+" which allows measurements in the temperature regime from 90 K up to 500 K (see Figure underneath).
Keywords: neutron; protein; hydrogen.

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Acta Cryst. (2014). A70, C1279
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Modern crystallography makes intense use of large scale facilities: neutron reactors, synchrotron sources, free electron lasers, where sources, optics and detectors allow for a wide range of possible experiments putting forwards the limits of the analysis of the structure and dynamics of matter and materials. Giving the large scale facilities a major role in the teaching of crystallography and material science, allowing for intense practice, requires to gather different skills which is more often done through summer school or intensive programs at PhD or junior scientist level. The Erasmus Mundus Master Course MaMaSELF (Master in Material Science Exploring Large Scale Facilities) is a unique European master program focused on the use of large scale facilities to investigate intimate nature of matter and materials where the five consortium higher education institutions (University of Rennes 1, France; Technische Universität München and Ludwig Maximilian University in München, Germany; University of Torino, Italy and University of Montpellier 2, France) have managed, together with Large Scale Facilities partners (ESRF, ILL, FRMII, DESY, LLB, SOLEIL, PSI) and third country partners spread out all over the world (Brazil, India, Japan, Russia, Switzerland , USA), to offer to the students a two years program at the master level including large amount of crystallography and spectroscopy teaching and an intensive summer-school totally dedicated to large scale facilities and including a large proportion of lessons and labs taught by experts, as well as many internship and master thesis opportunities at the large scale facilities.
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