The conformations of lysozyme in crystals and in aqueous solution are discussed and it is shown that the basic conformation is similar in the two states. Certain parts of the molecule have mobility. The reactions of lysozyme with protons, metal ions and some organic reagents are examined in the light of the conformations and their dynamics. The reactions considered are mainly those of tyrosyl, tryptophyl and carboxylate residues. The reactivity data are used in a discussion of the energy states of the reacting side-chains. In particular the reactivity of Glu-35 and its interaction with Trp-108 lead to suggestions for some new aspects in the hypothesis for the mechanism of action of lysozyme. In most respects the X-ray crystal diffraction and the nuclear magnetic resonance solution studies are in accord and complementary.