Crystallization and preliminary X-ray analysis of human Brn-5 transcription factor in complex with DNA.
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.
Pereira
Jose Henrique
JH
Department of Chemistry, University of California, Berkeley, California 94720, USA.
Ha
Sung Chul
SC
Kim
Sung-Hou
SH
D001483:Base Sequence; D003460:Crystallization; D004247:DNA / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D050809:POU Domain Factors / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D011485:Protein Binding; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014961:X-Ray Diffraction
D050809:POU Domain Factors; C082703:POU6F1 protein, human; D014157:Transcription Factors; D004247:DNA