Crystallization and preliminary X-ray crystallographic studies of the axin DIX domain

Axin is a negative regulator of the canonical Wnt signalling pathway that mediates the phosphorylation of β‐catenin by glycogen synthase kinase 3β. The DIX domain of rat axin, which is important for its homooligomerization and interactions with other regulators in the Wnt pathway, was purified and c...

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Veröffentlicht in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2007-06, Vol.63 (6), p.529-531
Hauptverfasser: Shibata, Naoki, Tomimoto, Yusuke, Hanamura, Toru, Yamamoto, Ryo, Ueda, Mai, Ueda, Yasufumi, Mizuno, Nobuhiro, Ogata, Hideaki, Komori, Hirofumi, Shomura, Yasuhito, Kataoka, Michihiko, Shimizu, Sakayu, Kondo, Jun, Yamamoto, Hideki, Kikuchi, Akira, Higuchi, Yoshiki
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Sprache:eng
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Zusammenfassung:Axin is a negative regulator of the canonical Wnt signalling pathway that mediates the phosphorylation of β‐catenin by glycogen synthase kinase 3β. The DIX domain of rat axin, which is important for its homooligomerization and interactions with other regulators in the Wnt pathway, was purified and crystallized by the sitting‐drop vapour‐diffusion technique using polyethylene glycol 6000 and lithium sulfate as crystallization agents. Crystals belong to space group P61 or P65, with unit‐cell parameters a = b = 91.49, c = 84.92 Å. An X‐ray diffraction data set has been collected to a nominal resolution of 2.9 Å.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309107022579