X-ray Diffraction: Single Crystal
Quick Specs
- Designed for protein structure determination
- Appropriate for analysis of small inorganic molecules
- Liquid nitrogen cooling stage allows temperature-dependent measurements
Environmental Spectroscopy and Biogeochemistry Facility has recently added a single crystal diffractometer to the capabilities available to EMSL Users. The diffractometer is a Bruker rotating anode with an image plate detector. Although designed for the determining the structure of protein molecules it is also appropriate for the analysis of problematic small inorganic molecules, such as twinning and lattice strain, due to high two theta resolution afforded by the Cu radiation.
Detection is by a large-format, charged-coupled device. This combination of source and detector makes the instrument ideal for determining the structure of very large biological molecules, small-molecule research (e.g., determining the structures of inorganic compounds). The instrument provides extremely high-resolution measurements of defect structures and lattice strain as a function of composition that would not be possible on a diffractometer with molybdenum radiation. It also has a liquid nitrogen cooling stage for temperature-dependent measurements.
All Related Publications Related Publications
- Antibody recognition force microscopy shows that outer membrane cytochromes OmcA and MtrC are expressed on the exterior surface of Shewanella oneidensis MR-1.
- Structural Transition of Gold Nanoclusters: From the Golden Cage to the Golden Pyramid .
- Characterization of Mg²⁺ Binding to the DNA Repair Protein Apurinic/Apyrimidic Endonuclease 1 via Solid-State ²⁵Mg NMR Spectroscopy.
- Kinetics of Reduction of Fe(III) Complexes by Outer Membrane Cytochromes MtrC and OmcA of Shewanella oneidensis MR-1.
- A Spectroscopic Study of the effect of Ligand Complexation on the Reduction of Uranium(VI) by Anthraquinone-2,6-disulfonate (AH2DS).
