Influence of the Inner Channels in Tetragonal Lysozyme Crystals on the Dissolution Shapes Formation

Abstract Protein molecules, although big and complicated structures, arrange into ordered crystal formations, but at specific only conditions, related to pH, additives and temperature. Truly, their crystallization is still more art than science and conditions relating their behavior to the known rules of crystal growth and dissolution are under investigation. This study is devoted to dissolution and more precise - the influence of undersaturation on the habitus of the dissolving tetragonal lysozyme crystals. Experiments described reveal that the morphologies of the dissolving crystals at low and high levels of undersaturations go through wholly different habitus. Rounding and diminishing the crystal happens at low undersaturation. Dissolution at higher undersaturation revealed development of ribbed crystal habitus, never noticed for dissolving low molecular weight crystals. Its formation could be explained with specific distribution of energetic places on the crystal surface. Existence of such energetic places is conditioned by inner channels passing through the crystal. A model relating these channels distribution and shapes observed during dissolving is presented.