Here we investigate how these mAbs target the B.1.351 spike protein using cryo-electron microscopy (cryo-EM).We assembled three ternary complexes containing Fab pairs of these mAbs bound to a prefusion-stabilized B.1.351 spike variant, namely BD-812/BD-836/S6P(B.1.351), BD-821/BD-771/S6P(B.1.351), and BD-813/BD-744/S6P(B.1.351), and obtained cryo-EM d. maps at overall resolutions of 3.0, 3.7, and 3.0 Å, resp.In addition, local refinements were performed to further improve the densities around the Fab and RBD regions, yielding local maps of 3.3, 3.4, and 3.2 Å, resp., which enabled us to construct the structure models unambiguously.We also solved the cryo-EM structures of two binary complexes: BD-667/S6P(B.1.351) and BD-804/S6P(B.1.351).Together, these cryo-EM structures provide detailed structural information for eight SARS-CoV-2 B.1.351 neutralizing antibodies.