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Macromolecular structure phasing by neutron anomalous diffraction.

Macromolecular structure phasing by neutron anomalous diffraction. Thumbnail


Abstract

In this report we show for the first time that neutron anomalous dispersion can be used in a practical manner to determine experimental phases of a protein crystal structure, providing a new tool for structural biologists. The approach is demonstrated through the use of a state-of-the-art monochromatic neutron diffractometer at the Institut Laue-Langevin (ILL) in combination with crystals of perdeuterated protein that minimise the level of hydrogen incoherent scattering and enhance the visibility of the anomalous signal. The protein used was rubredoxin in which cadmium replaced the iron at the iron-sulphur site. While this study was carried out using a steady-state neutron beam source, the results will be of major interest for capabilities at existing and emerging spallation neutron sources where time-of-flight instruments provide inherent energy discrimination. In particular this capability may be expected to offer unique opportunities to a rapidly developing structural biology community where there is increasing interest in the identification of protonation states, protein/water interactions and protein-ligand interactions - all of which are of central importance to a wide range of fundamental and applied areas in the biosciences.

Acceptance Date Jul 20, 2016
Publication Date Aug 11, 2016
Publicly Available Date Mar 28, 2024
Journal Scientific Reports
Print ISSN 2045-2322
Publisher Nature Publishing Group
Pages 31487 - ?
DOI https://doi.org/10.1038/srep31487
Keywords biophysics; structural biology
Publisher URL http://www.nature.com/articles/srep31487

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