Structural basis for binding of RILPL1 to TMEM55B reveals a lysosomal platform for adaptor assembly through a conserved TBM motif

Multi-angle light scattering, coupled to FPLC datasets for TMEM55B. TMEM55B 80-166 2CysMUT crystallized with 2 subunits in the unit cell of the crystal. The complex of the TMEM construct and a RILPL1 C-terminal peptide also showed 2 subunits of TMEM but only one RILPL1 peptide. Therefore we addressed the question what oligomeric state the constructs are in solution and whether there is a difference between the TMEM construct alone and the complex. We used static light scattering (SEC-MALS) to answer these questions by injecting either the TMEM55B construct alone or a complex with the RILPL1 peptide. The data we provide here was recorded and processed with the ASTRA 4.9 software. The additional excel file contains the extracted molecular weights (Mn) for each dataset and calculations done with them.