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. Author manuscript; available in PMC: 2021 Feb 25.
Published in final edited form as: Methods Mol Biol. 2016;1354:39–47. doi: 10.1007/978-1-4939-3046-3_3

Fig. 1.

Fig. 1

Diagram of the stabilization assay. In vitro-assembled HIV-1 CA-NC complexes, shown here as tubular structures, are formed by monomeric recombinant HIV-1 CA-NC fusion proteins under highly ionic conditions and recapitulate the surface of the HIV-1 core. When HIV-1 CA-NC complexes are incubated in destabilization buffer, they disassemble spontaneously. Disassembled capsids are layered on top of a 70 % sucrose cushion; however, the disassembled capsid does not cross the cushion after spinning at 100,000 × g for 1 h. In contrast, incubation of HIV-1 CA-NC in stabilization buffer preserves the assembled structures, which pellet when layered onto a 70 % sucrose cushion with spinning at 100,000 × g for 1 h. Input, a fraction of the sample layered onto the sucrose cushion before the centrifugation step. Pellet, a fraction of the capsid pelleted after the sample has been centrifuged at 100,000 × g for 1 h. Input and pellet samples were analyzed by Western blotting using anti-p24 antibodies.