Protein synthesis (translation) consumes a significant portion of cellular resources, necessitating specialized mechanisms to modulate translation during adverse conditions. Ribosome inactivation often involves ribosome-interacting proteins that enable ribosome dimerization, hibernation, or subunit anti-association, allowing organisms to adapt to stress. While such mechanisms are well-characterized in bacteria and eukaryotes, factor-mediated ribosome dimerization or anti-association in archaea has remained largely unexplored. Here, we present cryo-electron microscopy (cryo-EM) structures of an archaeal 30S dimer complexed with an archaeal ribosome dimerization factor (aRDF) from Pyrococcus furiosus. The aRDF-stabilized 30S dimer adopts a unique head-to-body architecture, distinct from the disome conformation observed during bacterial1,2 and eukaryotic ribosome hibernation4. aRDF interacts directly with the eS32 ribosomal protein, a critical component for subunit association, revealing its anti-association properties that inhibit the formation of archaeal 70S ribosomes. The archaeal system employs a unique strategy, offering valuable insights into ribosome inactivation and uncovering distinct mechanisms of ribosomal regulation across domains of life.