Incorporation of impurity to a tetragonal lysozyme crystal

Abstract

Concentration of a phosphor-labeled impurity (ovalbumin) incorporated into protein (lysozyme) crystals during growth was measured by fluorescence. Impurity concentration increased with growth rate, which could not be explained by two conventional models. Impurity concentration also increased with the pH of the solution. This result is discussed considering the electrostatic interaction between the impurity and the crystallizing species.