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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 33, Number 1
BKCSDE 33(1)
January 20, 2012 

Biophysical Feature, Crystallization and X-ray Crystallographic Studies of Toxascaris leonina Galectin
Minkyung Sung, Mi Suk Jeong, Woo Chul Lee, Jeong Hyun Song, Hye Yeon Kim, Min Kyoung Cho, Hak Sun Yu, Se Bok Jang*
Crystallization, X-ray analysis, Toxascaris leonina, Galectin
Galectins are generally believed to be potential candidates for use in the development of novel antiinflammatory agents or as selective modulators of the immune response. In particular, galectin-9 exhibits some of the extracellular functions, including cell aggregation, adhesion, chemoattraction, activation, and apoptosis. Tl-galectin (Tl-gal, galectin-9 homologue gene) was isolated from an adult worm of the Toxascaris leonina. The full-length Tl-gal gene, which was incorporated into pET-28a, was overexpressed in E. coli and purified by nickel affinity and gel filtration chromatographies. The purified Tl-gal was crystallized using the hangingdrop vapor-diffusion method. The crystal belonged to the tetragonal space group P41, with unit-cell parameters of a = b = 75.7 Å and c = 248.4 Å. The crystals were obtained at 20 oC and diffracted to a resolution of 3.0 Å. The asymmetric unit contained four molecules of Tl-gal, which gave a crystal volume per protein mass (Vm) of 2.8 Å3 Da−1 and a solvent content of 54.1%.
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