The Filoviridae family, including the Ebolavirus and Marburgvirus genera, cause haemorrhagic fevers with high mortality in humans, and no effective treatments are currently approved [5] , although candidate vaccines are promising [6] . The 18.9 kb single-stranded negative-sense non-segmented RNA genome of Ebola virus (EBOV) codes for at least eight proteins. The ribonucleoprotein complex is composed of the nucleoprotein (NP), polymerase protein (L), VP24, VP30, and VP35. The trimeric transmembrane glycoprotein (GP) forms surface spikes on the virion envelope and also has a soluble form, while the matrix protein, VP40, is associated with the inner surface. [5, [7] [8] [9] . The GP spike, a class I fusion protein, mediates cellular attachment and entry and is extensively glycosylated, especially in the glycan-rich mucin-like domain [10] [11] [12] [13] . Three proteins, VP24, VP35 and NP are essential for nucleocapsid formation [14] . Although some of the major protein interactions that occur during EBOV morphogenesis have been characterised [14, 15] , the three-dimensional (3D) structure and molecular arrangements have not been previously determined. Structural details are essential to understand how protection of the genome, cell binding, entry, and immune evasion are achieved in a filamentous animal virus, and to determine how this unique morphology plays a role in pathogenesis.