Open AccessCrystallization and preliminary X‐ray analysis of human Brn‐5 transcription factor in complex with DNA
Author(s) -
Pereira Jose Henrique,
Ha Sung Chul,
Kim SungHou
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108003370
Subject(s) - pou domain , transcription factor , crystallization , dna , transcription (linguistics) , crystallography , biology , computational biology , genetics , homeobox , chemistry , gene , linguistics , philosophy , organic chemistry
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.