Current work is focused on the structure determination of a number of protein binary complexes formed from disulfide-rich parasitic signaling proteins that mimic mammalian TGF-beta and mammalian TGF-beta receptors and co-receptors. I use mainly mammalian cell expression systems and tandem purification to enable the isolation of native stoichiometric complexes. I also use cryo-electron microscopy (CryoEM) to determine structures of larger complexes and other projects. Previously, At Rutgers University, my role as a Research Associate in Structural Biology involves the characterization of viral proteins, focusing on polymerases from pathogens such as HIV-1 and SARS-CoV-2. Our team is dedicated to advancing the understanding of these proteins' mechanisms, which is vital for the development of antiviral therapeutics. As a Postdoctoral Researcher at Oak Ridge National Laboratory, I contributed to groundbreaking research using neutron diffraction to probe enzyme interactions and reactions. Mastery of neutron diffraction, membrane proteins, and biochemistry underpins our efforts to elucidate protein structures, aiding the scientific community's response to viral threats.