Abstract
Neutron diffraction provides different information from
X-ray diffraction, because neutrons are scattered by
atomic nuclei, whereas X-rays are scattered by electrons.
One of the key advantages of neutron crystallography is
the ability to visualize hydrogen and deuterium atoms,
making it possible to observe the protonation state of
amino acid residues, hydrogen bonds, networks of water
molecules and proton relay pathways in enzymes. But,
because of technical difficulties, less than 100 enzyme
structures have been evaluated by neutron crystallography
to date. In this review, we discuss the advantages and
disadvantages of neutron crystallography as a tool to
investigate the functional structure of glycoside
hydrolases, with some examples.
| Original language | English |
|---|---|
| Pages (from-to) | 54-61 |
| Journal | Current Opinion in Structural Biology |
| Volume | 40 |
| DOIs | |
| Publication status | Published - 2016 |
| MoE publication type | A1 Journal article-refereed |
Keywords
- glycosidase
- proton