Direct observation of hydronium and Zundel ions in proteins by neutron crystallography: a reverse labelling approach.
We request beamtime on D19 for cryogenic and ambient temperature neutron crystallographic studies of perdeuterated rubredoxin (Rb) in hydrogenated water. Previous neutron work on perdeuterated rubredoxin has revealed, at atomic resolution, a remarkable network of ordered water that includes hydronium ions. These observations prompted ultra-high resolution studies on D19 using cryo-cooled samples at 100K. The results, which were obtained to a resolution of 0.88A, were striking: the visibility of the water-hydronium network was greatly enhanced, and exotic species such as Zundel ions [seen as D5O2]+ were observed. Given the significance of these results we wish to carry out a crucial crystallographic verification of this network by reverse labelling the water around the protein with H2O. The key aspect of this study is that the hydrogen atoms will appear as negative peaks in the Fourier maps and allow an unambiguous verification of the water, hydrogen, hydronium and Zundel features that have been found using perdeuterated protein hydrated with D2O. This experiment will also allow an ultra-high resolution analysis of the subtle differences between H and D analogues of these species.
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CUYPERS Maxime; Juliette M. Devos; FORSYTH Victor Trevor; HAERTLEIN Michael; MASON, Sax A.; MITCHELL Edward; MOSSOU Estelle and ROMOLI Filippo. (2016). Direct observation of hydronium and Zundel ions in proteins by neutron crystallography: a reverse labelling approach.. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-01-458
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