Abstract
The morphology (growth habit) of a crystal depends on the relative growth rates of different crystal faces which are determined by both structural and environmental factors. In protein crystals, where the constituent molecules are large and contain considerable amount of water, molecules form intermolecular contacts (macrobond) of various strength depending on the nature of protein molecules and their crystal forms. The at first sight complex structure of intermolecular contact in protein crystals can be reduced in a simple periodic bond chain of macrobonds. We estimated the strength of intermolecular contact in protein crystals and studied their correlation to the crystal morphology.
