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Charles F. Zukoski Professor of Chemical and Biomolecular Engineering and Biophysics Ph.D. 1984, Princeton University Protein crystallization and structural genomics Charles F. Zukoski 420 Swanlund, MC-304 601 E. John Champaign, IL 61820 217-333-0034 czukoski@uiuc.edu

With the delineation of the genomes of several species, biological research is entering a new state of activity where intellectual challenges revolve around the functions of sequences of proteins linked in the metabolic pathways that generate biological function. Manipulating and controlling true functions to catalyze production of desired molecules or core desire states requires understanding the structure of proteins and how small molecules bind to and interact with the proteins. In addition, many biological functions are mediated by large macromolecular complexes such as those important in ion transport across membranes or in DNA transcription. Understanding how small molecules bind to proteins or how macromolecular complexes function requires a knowledge of macromolecule structure. The work horse method of biological macromolecule structural determination is x-ray crystallography. With the advent of robust expression systems and high intensity, synchrotron x-ray sources and computer based methods of solving diffraction patterns, the rate limiting step in structural studies lies in rapidly growing x-ray quality crystals from small quantities of biomolecule. The research carried out in Professor Zukoski's group focuses at eliminating this bottleneck in advances of structural genomics. Treating proteins as nanoparticles and applying experimental and modeling methods developed for suspensions of weakly attractive particles, Prof. Zukoski's group are developing general methods for reducing the size of screens required to locate crystallization conditions. These studies involve development of microfluidic methods for characterizing rates of protein crystal nucleation and growth as well as developing the methods for characterizing the influences of solution conditions on nanoparticle interactions. These methods are applied to variety of novel proteins developed through collaboration with biochemists here on campus.