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Macromolecular Diffraction at CHESS (MacCHESS)

Richard A. Cerione, Ph.D.
P41GM103485
Active

Center Overview

To understand how macromolecules such as proteins and DNA work, we need to know their structure. The "gold standard" for determining macromolecular structures at the atomic level is x-ray crystallography, and the premier source of x-rays is synchrotron radiation from a storage ring. The MacCHESS Research Resource supports structural biologists who use the Cornell High Energy Synchrotron Source (CHESS) to determine crystal structures of a broad range of biomedically relevant proteins and macromolecular complexes. MacCHESS provides the specialized equipment needed for state-of-the-art x-ray crystallography and training for structural biology users. Additionally, MacCHESS staff perform research on novel x-ray technology to determine biomolecular structure, the results of which benefit the entire structural biology community. Over the last three decades MacCHESS has been responsible for many of the seminal developments that have enabled the growth of x-ray methods as the foundation of biomolecular structure, including advances in x-ray optics, crystallographic detectors, cryoprotection procedures for x-ray crystals, solution scattering technology, methods to phase and analyze crystallographic data, and software tools. Technology developed and data collected at MacCHESS have led to two Nobel prizes on the structure of biomolecules.

Impact on Human Health

MacCHESS provides support which enables biomedical scientists who come to CHESS to obtain structural information that furthers understanding of a wealth of cellular processes at the molecular level. In addition, the facility emphasizes the development of new technology that will enable biomedical scientists to tackle more and more complex macromolecular structures in order to provide a better understanding of the molecular basis of disease. In keeping with the location of CHESS/MacCHESS on a major university research campus, we also have a strong commitment to training. Indeed, many of the leading synchrotron scientists and structural biologists who are now making important contributions at other academic institutions and facilities were trained here as graduate students or postdoctoral fellows. Research areas being investigated by MacCHESS scientists, collaborators, users, and former students include probing the structure and function of viruses (e.g. HIV), delineating the mechanisms by which DNA expression, RNA-splicing and translation are regulated, understanding how proteins are trafficked and bind to specific membranes within cells, and identifying the structural features of complex signaling assemblies that underlie the control of cell growth, differentiation, and development. When these processes are not properly regulated, breakdowns in normal cellular functions ensue resulting in a variety of pathological conditions and disease states including cancer and neurodegenerative disorders. Thus, an overriding goal of the research, and technology development, at MacCHESS is to obtain information that can be applied to the identification of new therapeutic targets and clinical strategies.