Tailed phages transport their genomes into bacterial cells using their tail, whereas most tail-less phages use a host cell-encoded channel. One interesting exception is the icosahedral phage ΦX174, which is devoid of an external tail but instead uses the genome-associated DNA pilot protein H for DNA delivery. Sun et al. solved the crystal structure of protein H at 2.4 Å resolution and showed that its ten identical α-helical monomers are organized into a 170 Å-long α-barrel. This decameric coiled-coil contains transmembrane domains at each end, which may anchor the channel to the bacterial inner and outer cell membranes. The authors further found that H protein oligomerization is important for infectivity but not for particle formation. Using cryo-electon tomography, they went on to show that, following attachment of the ΦX174-like phage ST-1 to Escherichia coli mini cells, the virus extrudes a putative H tube for DNA transport across the periplasmic space. This tube is disassembled after DNA translocation.