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

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

Volume: 16 Issue: 3

Author(s): Geng Meng, Xiaoyun Bai, Todd J. Green, Ming Luo and Xiaofeng Zheng

Affiliation:

Keywords: Homo sapiens, protein crystallography, SI-CLP

Abstract: 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.

Cite this article as:

Meng Geng, Bai Xiaoyun, Green J. Todd, Luo Ming and Zheng Xiaofeng, Crystallization and Preliminary X-Ray Crystallographic Studies on SICLP, a Novel Human Glyco_18 Domain – Containing Protein, Protein & Peptide Letters 2009; 16 (3) . https://dx.doi.org/10.2174/092986609787601660