2013 年 23 巻 1 号 p. 81-86
Hydrogen (H) atoms and proton (H+) of biomacromolecules are important for various biological phenomena. H atoms of functional groups such as -OH and -NH2 make hydrogen bonds to contribute to folding and assembly of biomacromolecules. H+ ions are used for chemical reaction, electron transfer, and H+ concentration gradient is an energy source in cells.
X-ray crystallography is the most popular technique for structure determination of biomacromolecules, however it is very difficult to determine H atoms and almost impossible to identify H+ ions, because X-ray diffracts by electron cloud. On the other hand, neutron scattering length of H, H+, and its isotope (deuterium: D and D+) are comparable to those of non-hydrogen atoms in biomacromolecules. Therefore, the complementary use of X-ray and neutron crystallography provides detailed structural information of biomacromolecules including H and H+. So far, protein has been the main subject of biomacromolecular neutron crystallography; this technique is also called neutron protein crystallography (NPC). In this report, the basic principles of NPC are described.