title: Crystallization and preliminary crystallographic study of an invertebrate C-type lectin, CEL-I, from the marine invertebrate Cucumaria echinata.
abstract: 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.
authors.affiliation: Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan. thata@net.nagasaki-u.ac.jp
authors.forename: Tomomitsu
authors.initials: T
authors.lastname: Hatakeyama
authors.forename: Noriaki
authors.initials: N
authors.lastname: Matsuo
authors.forename: Haruhiko
authors.initials: H
authors.lastname: Aoyagi
authors.forename: Hajime
authors.initials: H
authors.lastname: Sugawara
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Uchida
authors.forename: Genji
authors.initials: G
authors.lastname: Kurisu
authors.forename: Masami
authors.initials: M
authors.lastname: Kusunoki
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004447:Echinodermata / Q000737:chemistry*; D011487:Protein Conformation