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. 2009 Jun 1;65(Pt 6):615-7.
doi: 10.1107/S1744309109016571. Epub 2009 May 22.

Crystallization and preliminary X-ray analysis of the V domain of human nectin-2

Xiaomin Qian  1 , Jianxun Qi, Fuliang Chu, Jun Liu, Qing Li, Jinghua Yan
Affiliations

Crystallization and preliminary X-ray analysis of the V domain of human nectin-2

Xiaomin Qian et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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 A resolution and belonged to space group P2(1), with unit-cell parameters a = 52.3, b = 43.9, c = 56.1 A, beta = 118.2 degrees .

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Figures

Figure 1
Figure 1
SDS–PAGE of the V domain of human nectin-2. Lanes 1, 2 and 3 represent different fractions after negative ion-exchange chromatography. Lane M, protein molecular-weight markers (kDa).
Figure 2
Figure 2
Crystals of the V domain of human nectin-2.
See this image and copyright information in PMC

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