Hydration structures in proteins and neutron diffraction experiment on dissimilatory sulfite reductase D (DsrD)
- 28 November 2003
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Journal of Synchrotron Radiation
- Vol. 11 (1) , 72-75
- https://doi.org/10.1107/s090904950302421x
Abstract
Neutron crystallography can provide a substantial amount of information about the hydration of proteins. The hydration patterns of three proteins, whose structures have been solved at 1.5 or 1.6 A resolution using our BIX-type diffractometers, show interesting features. The water molecules adopt a variety of shapes in the neutron Fourier maps, revealing details of intermolecular hydrogen-bond formation and dynamics of hydration. In addition, the neutron diffraction study of a DNA-binding protein, dissimilatory sulfite reductase D (DsrD) is briefly described, and some preliminary results are presented. This topic is of interest because it is well known that hydrogen bonds play important roles in DNA-protein recognition.Keywords
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