Antibodies are crucial to immune protection against SARS-CoV-2, with some in emergency use as therapeutics. In this article, the authors identified 377 human monoclonal antibodies (mAbs) recognising the virus spike, and focus mainly on 80 that bind the receptor binding domain (RBD). They devised a competition data-driven method to map RBD binding sites, finding that although antibody binding sites are widely dispersed, neutralising antibody binding is focused, with nearly all highly inhibitory mAbs (IC50<0.1μg/ml) blocking receptor interaction, except for one that bound a unique epitope in the N-terminal domain. Many of these neutralising mAbs use public V-genes and are close to germline. Dissection of the structural basis of recognition for this large panel of antibodies was performed through X-ray crystallography and cryo-electron microscopy of 19 Fab-antigen structures. The authors found find novel binding modes for some potently inhibitory antibodies and demonstrated that strongly neutralising mAbs protect, prophylactically or therapeutically, in animal models.