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used to determine the crystal structures of proteins up to resolution limits of 1.5-2.5 Å. Results relating to hydrogen positions and hydration patterns in proteins have been obtained from these studies. Examples include the geometrical details of hydrogen bonds, the role of hydrogen atoms in enzymatic activity, CH3 configuration, H/D exchange in proteins and oligonucleotides, and the dynamical behavior of hydration structures, all of which have been extracted from these structural results. These will open the new field beyond the folding structure of biological macromolecules such as: 1) Recognition of proteins and nucleic acids through the network structure of water molecules surrounding bio-macromolecules, and 2) The nature of chemical bond in proteins and nucleic acids elucidated by the accumulation of accurate structural information of hydrogen atoms. Other techniques, such as the growth of large single crystals and a database of hydrogen and hydration in proteins, will be given. Reference: 1) Nobuo Niimura and Robert Bau, Acta Cryst. A64 (2008) 12-22

Crystallography and mechanisms of structural phase transitions: the use of symmetry-adapted modes