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Crystallization and preliminary X‐ray diffraction of the ZO‐binding domain of human occludin

Crystallization and preliminary X‐ray diffraction of the ZO‐binding domain of human occludin Occludin is a tight‐junction protein controlling the integrity of endothelial and epithelial cell layers. It forms complexes with the cytoplasmic proteins ZO‐1, ZO‐2 and ZO‐3. The ZO‐binding domain in the C‐terminal cytoplasmic region of human occludin has previously been isolated and identified. This domain, as expressed in a bacterial system or isolated from native cellular occludin, maintains its ability to bind ZO‐1 and ZO‐2. The crystallization conditions of the human ZO‐binding domain are reported here. The crystals diffract to 2.3 Å resolution and were shown to belong to the orthorhombic space group P212121, with unit‐cell parameters a = 33.3, b = 35.4, c = 107.3 Å. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary X‐ray diffraction of the ZO‐binding domain of human occludin

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References (30)

Publisher
Wiley
Copyright
Copyright © 2005 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309105007475
pmid
16511043
Publisher site
See Article on Publisher Site

Abstract

Occludin is a tight‐junction protein controlling the integrity of endothelial and epithelial cell layers. It forms complexes with the cytoplasmic proteins ZO‐1, ZO‐2 and ZO‐3. The ZO‐binding domain in the C‐terminal cytoplasmic region of human occludin has previously been isolated and identified. This domain, as expressed in a bacterial system or isolated from native cellular occludin, maintains its ability to bind ZO‐1 and ZO‐2. The crystallization conditions of the human ZO‐binding domain are reported here. The crystals diffract to 2.3 Å resolution and were shown to belong to the orthorhombic space group P212121, with unit‐cell parameters a = 33.3, b = 35.4, c = 107.3 Å.

Journal

Acta Crystallographica Section F – Wiley

Published: Apr 1, 2005

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