RNA is an incredibly diverse molecule, simultaneously encoding for proteins and adopting tertiary structures capable of recruiting macromolecular components, binding ligands and performing catalysis. The nature of RNA structure and how it performs these biologically essential functions is a rapidly advancing field in biochemistry. Of particular focus are the structures and mechanisms of viral RNA elements which support and propagate viral replication and proliferation. While RNAs are generally recalcitrant to Crystallization, Chaperone Assisted Crystallography is a new technology that enables rapid crystallization and resolution of pertinent structured viral RNAs. In this work I present the high-resolution structures of two viral RNA elements. Both represent the first structure of either element resolved using crystallography. They provide insights into a new RNA structural motif and the mechanisms these viruses employ to regulate translation of their genes. The Programmed Frameshifting element of SARS-CoV-2 adopts two conformations to induce a frameshifting event during translation of the SARS-CoV-2 gRNA. Here the first high resolution structure of the Programmed Frameshifting Element was solved to 2.09Å and reveals what may be a second linear conformation of this frameshifting element. The Pea Enation Mosaic Virus 2 Translation Enhancer is a cap-intendent translation enhancer found in the 3’ UTR of plant viruses. Presented here is the first crystal structure of this class of translation enhancers solved to 2.75Å. This structure reveals a new C-turn motif which creates a solvent exposed binding site for the eukaryotic initiation factor eIF4E. This work demonstrates the potential for chaperone assisted RNA crystallography to improve RNA crystallography and advance the study of viral RNA element structures.