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

dc.contributor.author	Manoj, N.
dc.contributor.author	Jeyaprakash, A. A.
dc.contributor.author	Pratap, J. V.
dc.contributor.author	Komath, S. S.
dc.contributor.author	Kenoth, R.
dc.contributor.author	Swamy, M. J.
dc.contributor.author	Vijayan, M.
dc.date.accessioned	2022-03-27T08:35:05Z
dc.date.available	2022-03-27T08:35:05Z
dc.date.issued	2001-07-04
dc.description.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.
dc.identifier.citation	Acta Crystallographica Section D: Biological Crystallography. v.57(6)
dc.identifier.issn	09074449
dc.identifier.uri	10.1107/S0907444901004620
dc.identifier.uri	http://scripts.iucr.org/cgi-bin/paper?S0907444901004620
dc.identifier.uri	https://dspace.uohyd.ac.in/handle/1/11028
dc.title	Crystallization and preliminary X-ray studies of snake gourd lectin: Homology with type II ribosome-inactivating proteins
dc.type	Journal. Article
dspace.entity.type

Now showing 1 - 1 of 1