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Rapid visualization of hydrogen positions in protein neutron crystallographic structures
Acta Cryst. (2012). D68, 35–41 (http://doi.org/d49jgc)
![[Rubredoxin]](https://www.iucr.org/__data/assets/image/0006/66291/ActaD.jpg)
Although hydrogen atoms are difficult to locate using X-ray crystallography, with neutron crystallography the deuterium isotope can be readily visualized. Neutron analysis, however, has been limited by a number of technical challenges, such as prohibitively long data-collection times. Recent developments in instrumentation and deuterium labeling have dramatically increased the speed of data collection, as illustrated here by the structure of rubredoxin to 1.75 Å resolution, refined against neutron data collected in 14 h and revealing over 70% of deuteron positions without ambiguity.
P. Munshi, S.-L. Chung, M. P. Blakeley, K. L. Weiss, D. A. A. Myles and F. Meilleur