@article{oai:repo.qst.go.jp:00083052,
 author = {Fumiaki, Kono and Taro, Tamada and Fumiaki, Kono and Taro, Tamada},
 journal = {Current Opinion in Structural Biology},
 month = {Jun},
 note = {Hydrogen atoms and hydration water molecules in proteins are indispensable for many biochemical processes, especially enzymatic catalysis. The locations of hydrogen atoms in proteins are usually predicted based on X-ray structures, but it is still very difficult to know the ionization states of the catalytic residues, the hydration structure of the protein, and the characteristics of hydrogen-bonding interactions. Neutron crystallography allows the direct observation of hydrogen atoms that play crucial roles in molecular recognition and the catalytic reactions of enzymes. In this review, we present the current status of neutron crystallography in structural biology and recent neutron structural analyses of three enzymes: ascorbate peroxidase, the main protease of severe acute respiratory syndrome coronavirus 2, and copper-containing nitrite reductase.},
 pages = {36--42},
 title = {Neutron crystallography for the elucidation of enzyme catalysis},
 volume = {71},
 year = {2021}
}