Abstract
NPC takes the next step beyond the folding structure and gives information about the hydrogen bonding, protonation states, and hydration configuration of the biomolecule—all of which are critical features for understanding how it actually functions. This unique information makes NPC a valuable tool for structural biology. The basic principles for analysis of the structure of the biomolecules are that the calculated structure factor, Fc, is subtracted from the observed structure, Fo, the result should include only the positions of the missing hydrogen atoms. One of the most difficult problems in NPC is to obtain a single crystal that is large enough to obtain diffraction results with the low flux of a neutron beam. A large single crystal can be grown in the metastable region in the crystallization phase diagram. The NPC of RNase A has been given as a walk-through example.
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