Extended Data Fig. 3: Electron density maps of P-Rex1 ΔN40DH-PH-DEP1T4L.
From: Structure of the metastatic factor P-Rex1 reveals a two-layered autoinhibitory mechanism
a-d. 2Fo-Fc maps of the P-Rex1 DH-PH-DEP1 structure contoured between 1-1.5σ. Inset regions highlighting the density in the b. DEP1 domain, c. the DH hinge helix, and d. the PH domain. Electron density for T4L was diffuse, preventing the confident placement and refinement of a T4L model. As such, no contacts between T4L and P-Rex1 (either within the P-Rex1 chain or across the crystal lattice) were observed that could affect the conformation of the crystal structure. The T4L domain appears to be positioned within a solvent cavity in the crystal, enabling a high degree of mobility. Regardless, T4L was essential for crystal formation.
