Pseudomonas aeruginosa is an opportunistic human pathogen that causes acute and chronic infections, which can lead to life-threating septic shock. Treatment of these infections is further complicated by the ability of these bacteria to form biofilm. Biofilm serves as a shield through which the antibiotics cannot pass. Unlike antibiotics, bacteriophages are able to penetrate throug h biofilm, infect and kill bacterial cells. Here we present the structure of a bacteriophage JBD30 virion resolved by cryo- electron microscopy. Bacteriophage JBD30 belongs to the family Siphoviridae, order Caudovirales. Its virion is composed of non-enveloped icosahedral head of 60 nm in diameter connected via dodecameric portal with a non-contractile 180 nm long flexible tail. JBD30 tail is terminated with a baseplate embellished with side-tail fibres. Bacteriophage head is built from 415 copies of HK -97 l ike major capsid protein and further decorated on three-fold and quasi-three-fold axis with trimers of minor capsid protein. Data from cryo-electron tomography revealed that bacteriophage JBD30 uses the baseplate side-tail fibers for the attachment to its prey – bacterium Pseudomonas aeruginosa. P. aeruginosa pili type IV, that grow only from bacterial cell pole, serve as a primary receptor for the bacteriophage JBD30. After binding to pili, phage is pulled towards the cell surface by pili retraction, injects its nucleic acid into the bacterium and starts its replication cycle.