The Myc-Max heterodimer assembly is a central hub in cellular growth control, by regulating a wealth of biological functions. Increased Myc levels in the cell are caused by mutations disrupting ubiquitination and/or translocation, and result in an increment of Myc-Max heterodimer formation over the Max-Max homodimer. Uncontrolled Myc expression disturbs the balance of cell growth regulation, which turns the Myc-Max heterodimer into an oncoprotein and a key contributor to the development of many human cancers. To bind the DNA, the c-terminal region of Myc must form a heterodimer with the Max, but the Max is able to form a homodimer. Since X-Ray crystallography and NMR have failed to describe entire Max-Max or Myc-Max protein assemblies. Therefore, we intend to use SANS to investigate the structured envelope of DNA-bound complexes of Max-Max and Max-Myc.