Open AccessCrystallization and preliminary X‐ray analysis of the Pax6 paired domain bound to the Pax6 gene enhancer
Author(s) -
Ito Makoto,
Oyama Takuji,
Okazaki Kenji,
Morikawa Kosuke
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105033506
Subject(s) - pax6 , enhancer , crystallization , gene , crystallography , dna , microbiology and biotechnology , biology , transcription factor , chemistry , genetics , organic chemistry
Pax6 is a member of the Pax family of transcription factors and is essential for eye development. Pax6 has two DNA‐binding domains: the paired domain and the homeodomain. The Pax6 paired domain is involved in Pax6 gene autoregulation by binding to its enhancer. In this study, crystallization and preliminary X‐ray diffraction analysis of the mammalian Pax6 paired domain in complex with the Pax6 gene enhancer was attempted. The Pax6 paired domain complexed with an optimized 25 bp DNA fragment was crystallized by the hanging‐drop vapour‐diffusion method. The crystal diffracted synchrotron radiation to 3.0/3.7 Å resolution and belongs to the monoclinic space group P 2 1 , with unit‐cell parameters a = 62.21, b = 70.69, c = 176.03 Å, β = 90.54°. Diffraction data were collected to 3.7 Å resolution.