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Crystallization and Preliminary X-Ray Crystallographic Analysis of Galectin LEC-1 from Caenorhabditis elegans

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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 Å, α = 108.73, β = 91.39, and γ = 98.45 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 P21, with unit-cell parameters a = 52.90, b = 47.01, c = 66.16 Å, and β = 113.30° and one protein molecule per asymmetric unit.

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Keywords: Caenorhabditis elegans; crystallization; preliminary X-ray crystallographic analysis; tandem-repeat-type galectin

Document Type: Research Article

Publication date: 2008-05-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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