Insulin receptor (IR) signaling is critical to controlling nutrient uptake and metabolism. However, only a low-resolution (3.8 Å) structure currently exists for the IR ectodomain, with some segments ill-defined or unmodeled due to disorder. Here, we revise this structure using new diffraction data to 3.3 Å resolution that allow improved modeling of the N-linked glycans, the first and third fibronectin type III domains, and the insert domain. A novel haptic interactive molecular dynamics strategy was used to aid fitting to low-resolution electron density maps. The resulting model provides a foundation for investigation of structural transitions in IR upon ligand binding. Display omitted •The structure of the insulin receptor ectodomain is improved to 3.3 Å resolution•The structure reveals new features within the receptor insert domain•The structure corrects errors in the first and third fibronectin type III domains•A new low-resolution crystallographic model-building strategy, iMDFF, is presented Croll et al. describe a revised structure of the human insulin receptor ectodomain using diffraction data to 3.3 Å resolution. The revised structure allows improved resolution of the insert domain, an element critical to ligand binding and signal transduction.