Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase

@article{Ogata2015HydrogensDB,
  title={Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase},
  author={Hideaki Ogata and Koji Nishikawa and Wolfgang Lubitz},
  journal={Nature},
  year={2015},
  volume={520},
  pages={571-574}
}
The enzyme hydrogenase reversibly converts dihydrogen to protons and electrons at a metal catalyst. The location of the abundant hydrogens is of key importance for understanding structure and function of the protein. However, in protein X-ray crystallography the detection of hydrogen atoms is one of the major problems, since they display only weak contributions to diffraction and the quality of the single crystals is often insufficient to obtain sub-ångström resolution. Here we report the… CONTINUE READING
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