Vertebrate nuclear lamins exhibit polymerization properties that are remarkably different from those of vertebrate cytoplasmic intermediate filament (IF) proteins. Notably, under conditions where vertebrate cytoplasmic IF proteins form tetramers consisting of laterally associated dimers, nuclear lamin dimers associate longitudinally into head-to-tail polymers. Also, in vitro, nuclear lamins readily form paracrystalline fibers, rather than stable 10-nm filaments. To investigate whether these properties are also shared with invertebrate nuclear lamins, we analyzed in considerable detail the polymerization behavior of recombinant full-length lamin Dm0 from the invertebrate Drosophila melanogaster. This lamin differs substantially from vertebrate lamins in its primary structure. We also analyzed lamin Dm0-derived fragments lacking either the head domain (headless), the tail domain (tailless), or both (rod). Like vertebrate lamins, full-length Drosophila lamin Dm0 assembled into head-to-tail polymers, with little or no formation of tetramers by lateral association of dimers. This longitudinal assembly was severely inhibited by deletion of the head domain. Removal of the tail domain led to increased formation of filamentous polymers. Under appropriate conditions, full-length Drosophila lamin Dm0 as well as the three lamin Dm0-derived fragments assembled into paracrystalline fibers. No steady-state condition tested yielded assembly of 10-nm filaments resembling those formed by vertebrate cytoplasmic IF proteins. These findings indicate that the in vitro assembly behavior of nuclear lamins is highly conserved but distinct from that of cytoplasmic IF proteins, thus evidencing its functional importance.