The long term goal of this research is to understand the mechanisms by which ordered assemblies of biological macromolecules are formed. These symmetrical structures are made up of molecules having specific, repeated interactions with each other. They include both extended structures, such as cytoskeletal filaments and membrane photoreceptor arrays, and compact ones, such as nuclear pore complexes and viruses. They play crucial roles in cell morphology, motility, and other areas of cell function. The question to be investigated is: how do such ordered structures assemble themselves, i.e. how do the component molecules find their way to, recognize, and attach to specific sites? The more immediate aim is to apply the emerging technique of atomic force microscopy to a model self-assembling system, a three-dimensional protein crystal. Besides constituting a simple case of ordered assembly crystallization is generally the rate-limiting step in determining protein structure by X-ray diffraction. To develop rational guidelines for optimizing crystal growth, Dr. Durbin proposes to study the fundamental process of crystallization. Protein crystals have unique advantages for developing and applying methods of atomic force microscopy to imaging biological molecules and structures.
