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Crystallization and preliminary X-ray analysis of the Pax6 paired domain bound to the Pax6 gene enhancer.

ABSTRACT: 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 A resolution and belongs to the monoclinic space group P2(1), with unit-cell parameters a = 62.21, b = 70.69, c = 176.03 A, beta = 90.54 degrees. Diffraction data were collected to 3.7 A resolution.

SUBMITTER: Ito M

PROVIDER: S-EPMC1978128 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of the Pax6 paired domain bound to the Pax6 gene enhancer.

Ito Makoto M Oyama Takuji T Okazaki Kenji K Morikawa Kosuke K

Acta crystallographica. Section F, Structural biology and crystallization communications 20051025 Pt 11

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 ...[more]

PMID: 16511221

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