Crystallization and preliminary X-ray analysis of human Brn-5 transcription factor in complex with DNA

J.H. Pereira; S.C. Ha; S.-H. Kim

doi:10.1107/S1744309108003370

Crystallization and preliminary X-ray analysis of human Brn-5 transcription factor in complex with DNA

J.H. Pereira, S.C. Ha, S.-H. Kim

Norwich Medical School

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

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) and the POU-specific domain (POU). 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 and/or POU. 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.

Original language	English
Pages (from-to)	175-178
Number of pages	4
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volume	64
Issue number	3
DOIs	https://doi.org/10.1107/S1744309108003370
Publication status	Published - 1 Jan 2008

Keywords

transcription factors
protein-DNA crystallization
POU family
Brn-5 protein

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Crystallization and preliminary X-ray analysis of human Brn-5 transcription factor in complex with DNA

Abstract

Keywords

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