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

N Manoj, Jeyaprakash Arulanandam, J V Pratap, S S Komath, R Kenoth, M J Swamy, M Vijayan

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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 Angstrom resolution. Molecular-replacement studies indicate that the lectin is homologous to type II ribosome-inactivating proteins. Partial refinement confirms this conclusion.

Original languageEnglish
Pages (from-to)912-914
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Publication statusPublished - Jun 2001


  • lectins

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