HIV-1 capsids enter the nucleus of infected macrophages through nuclear pores, where they interact with FG-repeat nucleoporins (FG-Nups). The study used super-resolution microscopy, cryo-electron tomography, and molecular simulations to investigate the nuclear entry of HIV-1 capsids. It was found that capsids entering the nuclear pore complex (NPC) lose their association with the cytosolic protein cyclophilin A (CypA), and the capsid hexagonal lattice remains largely intact. The NPC scaffold rings frequently crack during capsid passage, consistent with simulations indicating the need for NPC widening. The unique cone shape of the HIV-1 capsid facilitates its entry into NPCs and helps to crack their rings. The HIV-1 capsid is the main orchestrator of the early post-entry phase of viral replication. It interacts with the cytoplasmic protein CypA and with the Cyp domain of Nup358 at the cytoplasmic side of nuclear pores, potentially docking the capsid to the nuclear pore complex (NPC). The capsid lattice engages microtubular motors, facilitating its transport towards the nuclear envelope. The capsid also interacts with the cytoplasmic protein CypA and with the Cyp domain of Nup358 at the cytoplasmic side of nuclear pores, potentially docking the capsid to the nuclear pore complex (NPC). The study shows that HIV-1 capsids accumulate at nuclear pores in primary human macrophages. Subviral HIV-1 complexes were detected upon entry into, passage through, and exit from the NPC. The capsids were found to be cone-shaped and retained their morphology inside the NPC. The capsid binding site for CypA was occupied on cytosolic capsids, and CypA was stripped off capsids entering the NPC. The NPC scaffold rings frequently cracked during capsid passage, consistent with simulations indicating the need for NPC widening. The unique cone shape of the HIV-1 capsid facilitates its entry into NPCs and helps to crack their rings. The NPC scaffold in macrophages is wider than most capsids, allowing the capsid to pass through the central channel. The study found that the NPC scaffold in macrophages is wider than in previously analyzed SupT1 cells. The NPC scaffold in macrophages is wider than most capsids, allowing the capsid to pass through the central channel. The study also found that the NPC scaffold in macrophages is wider than most capsids, allowing the capsid to pass through the central channel. The study found that the NPC scaffold in macrophages is wider than most capsids, allowing the capsid to pass through the central channel. The study found that the NPC scaffold in macrophages is wider than most capsids, allowing the capsid to pass through the central channel. The study found that the NPC scaffold in macrophages is wider thanHIV-1 capsids enter the nucleus of infected macrophages through nuclear pores, where they interact with FG-repeat nucleoporins (FG-Nups). The study used super-resolution microscopy, cryo-electron tomography, and molecular simulations to investigate the nuclear entry of HIV-1 capsids. It was found that capsids entering the nuclear pore complex (NPC) lose their association with the cytosolic protein cyclophilin A (CypA), and the capsid hexagonal lattice remains largely intact. The NPC scaffold rings frequently crack during capsid passage, consistent with simulations indicating the need for NPC widening. The unique cone shape of the HIV-1 capsid facilitates its entry into NPCs and helps to crack their rings. The HIV-1 capsid is the main orchestrator of the early post-entry phase of viral replication. It interacts with the cytoplasmic protein CypA and with the Cyp domain of Nup358 at the cytoplasmic side of nuclear pores, potentially docking the capsid to the nuclear pore complex (NPC). The capsid lattice engages microtubular motors, facilitating its transport towards the nuclear envelope. The capsid also interacts with the cytoplasmic protein CypA and with the Cyp domain of Nup358 at the cytoplasmic side of nuclear pores, potentially docking the capsid to the nuclear pore complex (NPC). The study shows that HIV-1 capsids accumulate at nuclear pores in primary human macrophages. Subviral HIV-1 complexes were detected upon entry into, passage through, and exit from the NPC. The capsids were found to be cone-shaped and retained their morphology inside the NPC. The capsid binding site for CypA was occupied on cytosolic capsids, and CypA was stripped off capsids entering the NPC. The NPC scaffold rings frequently cracked during capsid passage, consistent with simulations indicating the need for NPC widening. The unique cone shape of the HIV-1 capsid facilitates its entry into NPCs and helps to crack their rings. The NPC scaffold in macrophages is wider than most capsids, allowing the capsid to pass through the central channel. The study found that the NPC scaffold in macrophages is wider than in previously analyzed SupT1 cells. The NPC scaffold in macrophages is wider than most capsids, allowing the capsid to pass through the central channel. The study also found that the NPC scaffold in macrophages is wider than most capsids, allowing the capsid to pass through the central channel. The study found that the NPC scaffold in macrophages is wider than most capsids, allowing the capsid to pass through the central channel. The study found that the NPC scaffold in macrophages is wider than most capsids, allowing the capsid to pass through the central channel. The study found that the NPC scaffold in macrophages is wider than