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

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2007-06, Vol.63 (6), p.529-531
• Main Authors: 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
• Format: Article
• Language: English
• Subjects: Animals; axin; Axin Protein; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; Crystallization Communications; Crystallography, X-Ray; CRYSTALS; DIFFUSION; DIX domain; INTERACTIONS; Intracellular Signaling Peptides and Proteins - chemistry; Intracellular Signaling Peptides and Proteins - metabolism; Microfilament Proteins - chemistry; Microfilament Proteins - metabolism; Protein Structure, Tertiary; RATS; Repressor Proteins - chemistry; Repressor Proteins - physiology; RESOLUTION; Signal Transduction - physiology; SPACE GROUPS; SYNCHROTRON RADIATION; Wnt Proteins - chemistry; Wnt Proteins - physiology; Wnt signal; X-RAY DIFFRACTION; β-catenin
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309107022579

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.