Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 1
pubmed:dateCreated
2001-12-25
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
143-4
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Crystallization and preliminary crystallographic study of an invertebrate C-type lectin, CEL-I, from the marine invertebrate Cucumaria echinata.
pubmed:affiliation
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan. thata@net.nagasaki-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't