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Title
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Crystallization and preliminary crystallographic study of an invertebrate C-type lectin, CEL-I, from the marine invertebrate Cucumaria echinata.
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Authors
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T.Hatakeyama,
N.Matsuo,
H.Aoyagi,
H.Sugawara,
T.Uchida,
G.Kurisu,
M.Kusunoki.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2002,
58,
143-144.
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PubMed id
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Abstract
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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.
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