Study conducted by scientist at The Hormel Institute, University of Minnesota revealed the 2.9-Å cryo-electron microscopy structure of the Nipah virus L–P polymerase complexes. The L protein complex consists of conserved N-terminal domain, RNA-dependent RNA polymerase (RdRp), and GDP poly ribonucleotidyltransferase while the P protein complex consists of central oligomerization domain and the C-terminal X domain. These interact using the flexible antiparallel β-sheets domain of the P protomers and the fingers subdomain of RdRp forming a tetrameric organization crucial for replication and transcription mechanisms of the virus.