Determination of an accurate atomic model of the phi1026b capsid protein to compare to the established HK97 fold leading to isolation of structural elements that dictate capsid size. By utilizing the FEI Krios microscope, Falcon II camera, and EPU data acquisition software, a high-resolution structure was generated with visible alpha helices, beta sheets, and bulky side chains. The application of molecular dynamics flexible fitting (MDFF) and Phenix software packages has led to an initial atomic model of the phi1026b capsid protein. Compared to icosahedral capsid structural work, tail fiber structural research is relatively slim so I am also working on the structure of the tail tip complex and tail tube of Lambda bacteriophage.
Columbus State University, 2011
PhD Advisors: Dr. James Conway and Dr. Roger Hendrix
Biomedical Science Tower 3, Room 2047
Department of Structural Biology