Computational redesign of a fluorogen activating protein with Rosetta
Fig 4
DiB-RM crystal structures analysis.
Crystal structures of the full-length DiB-RM protein crystallized in the presence of DDM (A-C) or without it (D-E), and their comparison (F-G). Cartoon representation of the content of the asymmetric unit (A, D), the overlay of two protein chains from the asymmetric unit (B, E), and binding sites of the DDM molecules (C). The difference in the protein conformation between two crystals (F, DiB-RM protein structure obtained in the presence of DDM is colored blue, without DDM–colored orange) and in chain’s packing in the asymmetric unit (G). (H) Crystal structure of the DiB-RM-split protein. The N terminus part of the split protein is colored pink, the C terminus part of the split is colored blue. (I) The lipocalin fold is well preserved in DiB-RM-split protein as showed by the overlay of DiB-RM-split protein (both fragments colored pink) with the full-length DiB-RM (colored yellow).