Open AccessCrystallization and preliminary X‐ray crystallographic studies of the axin DIX domain
Author(s) -
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
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107022579
Subject(s) - crystallization , crystallography , wnt signaling pathway , regulator , chemistry , polyethylene glycol , glycogen synthase , stereochemistry , phosphorylation , biochemistry , gene , organic chemistry
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 P 6 1 or P 6 5 , 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.