STRUCTURAL BIOLOGY SHARED RESOURCE The Structural Biology Shared Resource (STRBIO) provides a comprehensive platform of expertise, education, and infrastructure that enables LCCC researchers to perform cutting-edge structural biological studies. LCCC members have all the resources needed to determine macromolecular structures using X-ray crystallography, biomolecular NMR, and single-particle cryo-electron microscopy (cryoEM). This mission is accomplished through seven complementary components: 1) macromolecular X-ray crystallography, 2) multi-dimensional nuclear magnetic resonance (NMR) spectroscopy, 3) cryo-electron microscopy, 4) structural bioinformatics, 5) protein expression and purification, 6) synthesis of peptides and peptidomimetics, and 7) biophysical measurements of macromolecular properties in solution and their interactions. Each component of STRBIO is managed by an on-site director with a Ph.D. and years of relevant scientific and managerial experience. All core directors hold ranks of Assistant Research Professor or higher and most teach graduate-level classes in their respective disciplines. John Sondek (MT) continues as faculty director of STRBIO and leads this team of experienced directors. Dr. Sondek has over 20 years of experience in structural biology and drug discovery and meets bimonthly with core directors as a group to coordinate efforts and develop strategic plans. The STRBIO was used by 131 users last year. LCCC members accounted for 34% of the use. There are no alternatives to STRBIO on campus or at nearby academic institutions. In fact, STRBIO attracts numerous users from outside the UNC system due to its competitive rates and extensive services. STRBIO requests $119,631 for this SR, approximately 6% of the total operating budget of $1.9M. To accomplish its mission STRBIO will continue to expand services into areas of high demand, areas that take advantage of the inherent synergies embodied among the STRBIO components, and areas predicted to provide major advances in cancer biology including new fragment-based drug discovery and expanding capacity to label proteins isotopically.
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