The Ebola virus, one of the most feared of pathogens, causes a severe haemorrhagic fever with up to 90% human mortality. Since 1994, outbreaks of the virus have increased fourfold. Although initial vaccine trials in primates have shown promise, no vaccines or post-exposure treatments are yet available. And it is still not clear why the virus is so pathogenic or why the immune response is so weak in fatal cases. A team from The Scripps Research Institute has now determined the crystal structure of the trimeric Ebola virus glycoprotein bound to a neutralizing antibody isolated from a human survivor. The structure reveals a putative receptor-binding site sequestered in a bowl of a chalice formed by three GP1 viral attachment subunits (in shades blue in the molecular surface model on the cover), cradled by three GP2 fusion subunits (coloured white). Access to the site is restricted by a glycan cap and a protruding mucin-like domain. The antibody (in yellow) bridges the GP1 and GP2 subunits and is specific for the prefusion, viral surface conformation of GP2. [Article p. 177] Cover grapics by Christina Corbaci & Michael Pique.