Crystallization and preliminary crystallographic study of an invertebrate C-type lectin, CEL-I, from the marine invertebrate Cucumaria echinata.
CEL-I is a GalNAc-specific carbohydrate-binding protein (lectin) isolated from the sea cucumber Cucumaria echinata. This protein belongs to the widely distributed C-type lectin family of animal lectins, which require Ca(2+) for their carbohydrate-binding ability and play important roles in various molecular-recognition processes in organisms. CEL-I was crystallized with 2-methyl-2,4-pentanediol using the hanging-drop vapour-diffusion technique. The CEL-I crystals belong to the monoclinic space group C2, with unit-cell parameters a = 92.38 (3), b = 69.94 (3), c = 76.69 (3) A, beta = 136.46 (2) degrees. Diffraction data were collected to 2.0 A resolution using synchrotron radiation. The asymmetric unit contains one CEL-I molecule.
Hatakeyama
Tomomitsu
T
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan. thata@net.nagasaki-u.ac.jp
Matsuo
Noriaki
N
Aoyagi
Haruhiko
H
Sugawara
Hajime
H
Uchida
Tatsuya
T
Kurisu
Genji
G
Kusunoki
Masami
M
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004447:Echinodermata / Q000737:chemistry*; D011487:Protein Conformation