Abstract
The contractile ability of active materials relies on the interplay of force-exerting and force-bearing structures. However, the complexity of interactions and limited parameter control of many model systems are major obstacles in advancing our understanding of the underlying fundamental principles. To shed light on these principles we introduce and analyse a minimal reconstituted system, consisting of highly concentrated actin filaments that are crosslinked by α-actinin and actively transported in the two-dimensional geometry of a motility assay. This minimal system actively compacts and evolves into highly compact fibres that exceed the length of the individual filaments by two orders of magnitude. We identify the interplay between active transport and crosslinking to be responsible for the observed active compaction. This enables us to control the structure and the length scale of active compaction.