Growth and Characterization of Lysozyme Crystals in Varying Precipitants

X-ray crystallography is a method used in determining the arrangement of atoms within a crystal. This method of examining a molecular structure can be applied to biological compounds, such as proteins and enzymes. By allowing researchers to know the structure of an enzyme, the function of such a molecule can be fully understood. Often, chemical properties may be known of an enzyme, but how such an enzyme truly functions is dependent upon its structure and how it interacts with its substrate and environment. Specifically, the chicken-egg white lysozyme under investigation was crystallized in order to undergo x-ray diffraction, as well as analyzed with a circular dichroism spectrometer. The growth of lysozyme crystals using varying precipitant solutions provided a study on the effects of growth and crystal lattice formation as a result of differing solutions. Concentrations were a factor changed but so were ions, which provided us with a study of the Hofmeister Series, which “ranks the relative influence of ions on the physical behavior of a wide variety of aqueous processes” (Zhang). The data collected validated the Hofmeister Series and provided the conclusion that the precipitant present in the buffer solution does affect the size and shape of the crystal grown.