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Sox9 is a fundamental sex-determining gene and the master regulator of chondrogenesis, involved in the development of various vital organs like testes, kidney, heart, brain and skeletal development. Like other known Sox transcription factors, Sox9 recognizes and binds DNA with consensus sequence C(T/A)TTG(T/A)(T/A) through the highly conserved HMG domain. Nonetheless, the molecular basis of Sox9 functional specificity in key developmental processes is still unclear. As a foremost step towards a mechanistic understanding of Sox9 transcriptional regulation, the current work describes the details of purification of mouse Sox9 HMG domain, its crystallization in complex with a ChIP-Seq identified 16-mer FOXP2 DNA and the preliminary X-ray diffraction data analysis of this complex. The mSox9HMGDNA complex was crystallized by the hanging-drop vapor diffusion method using 200 mM Sodium/potassium phosphate, 100 mM Bis Tris propane at pH 8.5, 20% (w/v) PEG 3350. The crystals belong to the tetragonal system, have space group P41212 with unit cell parameters a =b= 99.49, c = 45.89 and diffract X-rays to a resolution of 2.7 Å. Analysis of the diffraction data reveals a single molecule in the crystallographic asymmetric unit with an estimated solvent content of 64%.

Characterization of DNA binding and oligomerization domains of stem cell transcription factor Sox9 and Sox5