Vapor Diffusion Crystallography of the Polymerase Acidic Protein
Current treatments of an Influenza infection target frequently mutating surface proteins. This causes increased variability in the effectiveness of modern treatment methods, as a single mutation in the protein could cause the antiviral to be ineffective. A component of the RNA-dependent-RNA-polymerase (RdRp) of the Influenza A virus, the Polymerase Acidic (PA) protein, is a promising antiviral target for a new generation of Influenza treatments because of its highly conserved nature. PA has been shown to have a similar structure and sequence across known strains of Influenza. Drug design research utilizes crystal structures to synthetically improve viral inhibitors through in silico analysis that can prevent the binding of PA to an additional protein, Polymerase Basic 1 (PB1). Years of research to make a soluble and pure PA sample that is binding-pocket solvent-exposed has led to the culmination of crystalizing the protein construct as the final step to capturing an image using X-ray crystallography. Various techniques involving a pure PA sample and many different thermodynamic conditions make forming a structure difficult and time-consuming. A large “shotgun” approach over a broad spectrum of reagents, concentration, pH, buffers, and the occasional additive help to narrow in on the highly specific mother liquor necessary to grow PA crystals. The presentation will discuss the current methodologies and chemical types and how they played a role in the vapor diffusion of PA Crystallography.
Primary Advisor's Department
Stander Symposium, College of Arts and Sciences
"Vapor Diffusion Crystallography of the Polymerase Acidic Protein" (2023). Stander Symposium Projects. 2926.
Presentation: 11:00-11:20 a.m., Kennedy Union 312