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The transcription factor p53 acts as major tumor suppressor and is inactivated by mutation in more than 50% of all human tumors. We have established an efficient procedure for the  in vitro  folding and purification of the p53 DNA binding domain (p53DBD) using a modified factorial matrix approach that supplies large amounts of homogeneous (isotope-labeled) p53DBD for application in biochemical, crystallographic and NMR spectroscopic studies. We further show with biophysical methods that  in vitro  folded p53DBD is fully functional and that its conformation is identical to that obtained from the soluble fraction.

In vitro folding and characterization of the p53 DNA binding domain