Crystallization and Preliminary X-Ray Crystallographic Studies on SICLP, a Novel Human Glyco_18 Domain-Containing Protein

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A novel human Glyco_18 domain-containing protein, SI-CLP, was detected recently in human bronchoalveolar lavage of patients with chronic inflammatory disorders of the respiratory tract and peripheral-blood leukocytes. The expression of SI-CLP is up-regulated by dexamethasone or IL-4 and involved in the Th2 cell pathway. To further investigate its structure and function will provide new insights into human immunity and related disorders. Here we provide a preliminary crystal image of SI-CLP using the hanging-drop vapor diffusion method. The crystals of SI-CLP diffracted Xrays to a resolution of 2.7 Å. The crystals belong to the space group P3221 with unit cell parameters a = b =99.79 Å, c =250.53 Å, α=β=90°, γ=120°. There are two molecules per asymmetry unit.

Keywords: Homo sapiens; SI-CLP; protein crystallography

Document Type: Research Article


Publication date: March 1, 2009

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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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