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The Brn-5 protein plays an important role in the control of cellular development and belongs to a class of transcription factors that usually contain two domains: the POU homeodomain (POUHD) and the POU-specific domain (POUS). Since high-quality crystals suitable for crystallographic studies of the proteins of this class are difficult to obtain, all the known structural information available is for POUHD and/or POUS. This paper describes several critical steps that allowed the production of high-quality crystals of the full-length Brn-5 protein complexed with its cognate DNA.

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