TY - JOUR
T1 - Crystallization and preliminary X-ray analysis of human Brn-5 transcription factor in complex with DNA
AU - Pereira, J.H.
AU - Ha, S.C.
AU - Kim, S.-H.
PY - 2008/1/1
Y1 - 2008/1/1
N2 - 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.
AB - 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.
KW - transcription factors
KW - protein-DNA crystallization
KW - POU family
KW - Brn-5 protein
UR - http://www.scopus.com/inward/record.url?scp=40449139952&partnerID=8YFLogxK
U2 - 10.1107/S1744309108003370
DO - 10.1107/S1744309108003370
M3 - Article
AN - SCOPUS:40449139952
SN - 1744-3091
VL - 64
SP - 175
EP - 178
JO - Acta Crystallographica Section F Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F Structural Biology and Crystallization Communications
IS - 3
ER -