Crystallization and preliminary X-ray studies of snake gourd lectin: homology with type II ribosome-inactivating proteins

Manoj, N. ; Arockia Jeyaprakash, A. ; Pratap, J. V. ; Komath, Sneha Sudha ; Kenoth, Roopa ; Swamy, Musti J. ; Vijayan, M. (2001) Crystallization and preliminary X-ray studies of snake gourd lectin: homology with type II ribosome-inactivating proteins Acta Crystallographica Section D, 57 (6). pp. 912-914. ISSN 0907-4449

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Official URL: http://onlinelibrary.wiley.com/doi/10.1107/S090744...

Related URL: http://dx.doi.org/10.1107/S0907444901004620

Abstract

The lectin from the seeds of snake gourd (Trichosanthes anguina) has been crystallized in two forms using the hanging-drop method. Both the forms are hexagonal, with the asymmetric unit containing one subunit consisting of two polypeptide chains linked through disulfide bridges. Intensity data from one of the forms were collected at room temperature as well as at low temperature to 3 Å resolution. Molecular-replacement studies indicate that the lectin is homologous to type II ribosome-inactivating proteins. Partial refinement confirms this conclusion.

Item Type:Article
Source:Copyright of this article belongs to International Union of Crystallography.
Keywords:Lectins
ID Code:54246
Deposited On:11 Aug 2011 11:17
Last Modified:11 Aug 2011 11:17

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