Neutron diffraction
X-ray structure of perdeuterated DFPase – perdeuteration of enzymes for neutron diffraction
Perdeuteration of proteins is a much discussed strategy to overcome the problems of incoherent scattering caused by hydrogen in neutron diffraction experiments because deuterium displays a significantly lower incoherent scattering cross section compared to the normal hydrogen isotope. Expression of the protein in perdeuterated media is required for this. We report the X-ray structure of perdeuterated DFPase, which displays practically no differences to the hydrogenous structure. B-factors and RMSD values are reported. Even though a very big perdeuterated DFPase crystal was grown, it did not diffract neutrons. Reasons for this unexpected behaviour are discussed. The structure is presented in a new publication in Acta Cryst. F.
Bundeswehr Medical Service Writes About DFPase
The Bundeswehr Medical Service (Sanitätsdienst der Bundeswehr) writes about DFPase and our neutron structure on its web page. The article (in German) can be found here.
The Fish and the Venom
The German newspaper “Frankfurter Rundschau” published an article about DFPase and our neutron structure with the title “Der Fisch und das Gift” (The Fish and the Venom). The article can be found here.
Neutron Structure of the Enzyme DFPase
A new publication in the journal Proceedings of the National Academy of Sciences of the USA (PNAS) describes the neutron diffraction structure of the enzyme DFPase. Neutron diffraction allows the visualization of hydrogen atoms in protein structures and thus the determination of protonation states and orientations of solvent water molecules. The results of the study confirm the proposed reaction mechanism for DFPase and permit the directed introduction of modifications to the enzyme by mutagenesis to enhance both turnover rates and substrate diversity.
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