Abstract
Nectin-2 belongs to a family of immunoglobulin-like cell adhesion molecules that are characterized by the presence of three immunoglobulin-like domains (V, C2 and C2) in the extracellular region. The V domain plays important roles in cell adhesion, NK cell activation and the entry of some herpesvirus. In this study, the V domain of human nectin-2 was expressed in Escherichia coli in the form of inclusion bodies, which were subsequently denatured and refolded. The soluble protein was crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to 1.85 Å resolution and belonged to space group P21, with unit-cell parameters a = 52.3, b = 43.9, c = 56.1 Å, β = 118.2°. © 2009 International Union of Crystallography. All rights reserved.
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Qian, X., Qi, J., Chu, F., Liu, J., Li, Q., & Yan, J. (2009). Crystallization and preliminary X-ray analysis of the v domain of human nectin-2. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(6), 615–617. https://doi.org/10.1107/S1744309109016571
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