Rapid visualization of hydrogen positions in protein neutron crystallographic structures

Authors: Munshi, Parthapratim; Chung, Shang-Lin; Blakeley, Matthew P.; Weiss, Kevin L.; Myles, Dean A. A.; Meilleur, Flora

Source: Acta Crystallographica Section D, Volume 68, Number 1, 1 January 2012 , pp. 35-41(7)

Publisher: Wiley-Blackwell

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Abstract:

Neutron crystallography is a powerful technique for experimental visualization of the positions of light atoms, including hydrogen and its isotope deuterium. In recent years, structural biologists have shown increasing interest in the technique as it uniquely complements X-ray crystallographic data by revealing the positions of D atoms in macromolecules. With this regained interest, access to macromolecular neutron crystallography beamlines is becoming a limiting step. In this report, it is shown that a rapid data-collection strategy can be a valuable alternative to longer data-collection times in appropriate cases. Comparison of perdeuterated rubredoxin structures refined against neutron data sets collected over hours and up to 5 d shows that rapid neutron data collection in just 14 h is sufficient to provide the positions of 269 D atoms without ambiguity.

Document Type: Research article

DOI: http://dx.doi.org/10.1107/S0907444911048402

Publication date: 2012-01-01