My lab is one of the few in the world that directly links deep-sequencing to structural biology in an effort to advance discoveries in precision medicine. Our approach uses interdisciplinary techniques to elucidate mechanisms of genomic maintenance and regulation in diseases, such as cancer. Our challenge is to understand how genomic and proteomic variations affect health, disease and drug response. To address this, we seek to define protein-protein interaction networks in patient data and model these observations in cell systems to determine the best course of therapy. Our aim is to determine the three-dimensional structural details of dynamic protein assemblies known to influence tumorigenesis. This understanding is crucial for more effective detection, treatment and prevention of disease. As a postdoctoral scholar at the National Cancer Institute, I discovered a novel truncation product of the DNA damage mediator protein, Pax transactivation domain-interacting protein (PTIP/PAXIP1), which has an important role in preserving genomic stability and is essential for cell survival following DNA damage. I have worked on the structural characterization of PTIP constructs and have obtained protein crystals that deteriorate due to radiation damage. I have been the sole person responsible for moving this project forward, which has affected my publication record. As an Early Stage Investigator, I have the experience and resources necessary to successfully carry out the proposed work. My laboratory’s work extends on the discovery of this PTIP neoform to further our understanding how DNA damage mediator proteins work together to protect the cellular genome. Currently, we are characterizing the changes in the levels of DNA damage mediator proteins across breast cancer subtypes. Our central hypothesis is that the expression levels of DNA damage mediators, like PTIP, are important indicators of the cells DNA repair capacity and ultimately tumorigenesis. Our future plans will include characterizing the proteinprotein interactions that mediate the assembly of functional DNA repair complexes.