Extended Data Fig. 5: Crystal packing interactions suggest ClbP forms a dimer.
From: Structural basis of colibactin activation by the ClbP peptidase

a, The ClbP dimer (left) and the dimer in context of the crystal packing arrangement (right), with the asymmetric units containing each subunit in yellow or green and other symmetry mates in gray. b, The same dimeric arrangement observed in our full-length ClbP structure is also present as a crystallographic dimer interface in the published structure of the isolated periplasmic domain (top), as seen in the interaction between two trimeric asymmetric units (bottom). c, 2D representation of the ClbP dimer interface detailing the molecular interactions stabilizing the assembly as well as distances (in Ã…) between interacting polar groups.