Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 3 (March 2008)

crystallization communications

Acta Cryst. (2008). F64, 175-178 [ 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 and S.-H. Kim

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.

Keywords: transcription factors; protein-DNA crystallization; POU family; Brn-5 protein.