Modern algorithms for de novo prediction of protein structures typically output multiple full-length models (decoys) rather than a single solution. Subsequent clustering of such decoys is used both to gauge the success of the modelling and to decide on the most native-like conformation. At the same time, partial protein models are sufficient for some applications such as crystallographic phasing by molecular replacement (MR) in particular, provided these models represent a certain part of the target structure with reasonable accuracy.