Severe Acute Respiratory Syndrome (SARS) CoV-1, SARS CoV-2 and the Middle East respiratory syndrome (MERS) are from the Betacoronavirus genera that have caused serious infectious respiratory diseases. Replication of the coronaviral genome is crucial for efficient synthesis of viral RNA in the host cells. Non-structural protein 9 (Nsp9) plays an important role in this replicative cycle as it has recently been shown to be vital for the capping of viral RNA. However, a largely unexplored feature of Nsp9 is the ability to recognise single stranded RNA (ssRNA). Across the homologs of the Coronavirus family, Nsp9 proteins exhibit moderate sequence similarities, however, the structural features are largely conserved. Our recent study on the SARS CoV-2 Nsp9 has revealed that the disruption of key residues in the binding interface of Nsp9 affects RNA binding. Although MERS emerged well before SARS CoV-2, the structure of MERS Nsp9 has not been determined and little is known about its RNA binding properties. In this study, nuclear magnetic resonance (NMR and X-ray crystallography in combination with Biolayer interferometry (BLI) were utilised to characterise the structure and details of RNA binding of MERS Nsp9. These data will allow for a direct comparison between Nsp9 proteins within the Coronavirus family, thus shedding light onto the molecular details of RNA replication which will ultimately aid in the development of new antiviral drugs for this devastating disease.