Explanation for the supersaturation dependence of the morphology of lysozyme crystals

In this paper the growth morphology of crystals of the protein lysozyme and its experimentally observed dependence on the supersaturation is explained by the presence of multiple connected nets or surface configurations. The F-forms found by a connected net analysis are {1 1 0}, {1 0 1} and {1 1 1}. From the connected nets, besides the attachment energies, also the step energies are estimated. The results of the morphological analysis are compared with recently published Monte Carlo simulation data on lysozyme and related crystal structures. The results show that the presence of multiple connected nets has major implications for the growth morphology and explains the different growth rates as a function of supersaturation of the crystal faces. (C) 1999 Elsevier Science B.V. All rights reserved.