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Updated: Jul 6, 2026

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
Published on: November 1, 2012
Crystallization and preliminary X-ray analysis of human Brn-5 transcription factor in complex with DNA
Jose Henrique Pereira1, Sung Chul Ha, Sung-Hou Kim
1Department of Chemistry, University of California, Berkeley, California 94720, USA.
Abstract:
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 (POU(HD)) and the POU-specific domain (POU(S)). 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 POU(HD) and/or POU(S). 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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