Crystallization and preliminary x-ray crystallographic analysis of galectin LEC-1 from Caenorhabditis elegans.
Galectin LEC-1 isolated from the nematode Caenorhabditis elegans was the first galectin found in invertebrates and also the first tandem-repeat-type galectin identified, containing two homologous carbohydrate-binding sites. This galectin is localized most abundantly in the adult cuticle and possibly plays a role in the formation of epidermal layers. We succeeded in crystallizing LEC-1 composed of 279 amino acids with a calculated molecular weight of 31,809 Da under two independent sets of conditions as a result of extensive screening. The crystals grown under one set of conditions belong to the triclinic space group P1, with unit-cell parameters a = 48.44, b = 52.13, c = 64.24 A, alpha = 108.73, beta= 91.39, and gamma = 98.45 degrees and two protein molecules per unit cell. The crystals grown under the other set of conditions which included lactose belong to the monoclinic space group P2(1), with unit-cell parameters a = 52.90, b = 47.01, c = 66.16 A, and beta= 113.30 degrees and one protein molecule per asymmetric unit.
Itagaki
Takashi
T
Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan.
Nishizaki
Sachie
S
Sekihashi
Kaoru
K
Kobayashi
Hajime
H
Kidokoro
Shun-Ichi
S
Kezuka
Yuichiro
Y
Arata
Yoichiro
Y
Hirabayashi
Jun
J
Kasai
Ken-Ichi
K
Nonaka
Takamasa
T
D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000737:chemistry*; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D037161:Galectins / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D029742:Caenorhabditis elegans Proteins; D037161:Galectins; C525184:Lec-1 protein, C elegans