Purification, crystallization and preliminary X-ray crystallographic analysis of MIL, a glycosylated jacalin-related lectin from mulberry (Morus indica) latex.

2.50
Hdl Handle:
http://hdl.handle.net/10033/324483
Title:
Purification, crystallization and preliminary X-ray crystallographic analysis of MIL, a glycosylated jacalin-related lectin from mulberry (Morus indica) latex.
Authors:
Patel, Ashok K; Singh, Vijay K; Bergmann, Ulrich; Jagannadham, Medicherla V; Kursula, Petri ( 0000-0001-8529-3751 )
Abstract:
A quantitatively major protein has been purified from the latex of Morus indica. The purified previously uncharacterized protein, M. indica lectin (MIL), was further shown to be a glycosylated tetramer and belongs to the family of jacalin-related lectins. Crystallization of MIL was also accomplished and the tetragonal crystals diffracted synchrotron X-rays to a resolution of 2.8 Å.
Citation:
Purification, crystallization and preliminary X-ray crystallographic analysis of MIL, a glycosylated jacalin-related lectin from mulberry (Morus indica) latex. 2011, 67 (Pt 5):608-12 Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Journal:
Acta crystallographica. Section F, Structural biology and crystallization communications
Issue Date:
1-May-2011
URI:
http://hdl.handle.net/10033/324483
DOI:
10.1107/S174430911101013X
PubMed ID:
21543873
Type:
Article
Language:
en
ISSN:
1744-3091
Appears in Collections:
publications of the research group CSSB

Full metadata record

DC FieldValue Language
dc.contributor.authorPatel, Ashok Ken
dc.contributor.authorSingh, Vijay Ken
dc.contributor.authorBergmann, Ulrichen
dc.contributor.authorJagannadham, Medicherla Ven
dc.contributor.authorKursula, Petrien
dc.date.accessioned2014-08-08T10:42:32Zen
dc.date.available2014-08-08T10:42:32Zen
dc.date.issued2011-05-01en
dc.identifier.citationPurification, crystallization and preliminary X-ray crystallographic analysis of MIL, a glycosylated jacalin-related lectin from mulberry (Morus indica) latex. 2011, 67 (Pt 5):608-12 Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.en
dc.identifier.issn1744-3091en
dc.identifier.pmid21543873en
dc.identifier.doi10.1107/S174430911101013Xen
dc.identifier.urihttp://hdl.handle.net/10033/324483en
dc.description.abstractA quantitatively major protein has been purified from the latex of Morus indica. The purified previously uncharacterized protein, M. indica lectin (MIL), was further shown to be a glycosylated tetramer and belongs to the family of jacalin-related lectins. Crystallization of MIL was also accomplished and the tetragonal crystals diffracted synchrotron X-rays to a resolution of 2.8 Å.en
dc.language.isoenen
dc.rightsArchived with thanks to Acta crystallographica. Section F, Structural biology and crystallization communicationsen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshCrystallizationen
dc.subject.meshCrystallography, X-Rayen
dc.subject.meshGlycosylationen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshMorusen
dc.subject.meshPlant Lectinsen
dc.subject.meshSequence Alignmenten
dc.titlePurification, crystallization and preliminary X-ray crystallographic analysis of MIL, a glycosylated jacalin-related lectin from mulberry (Morus indica) latex.en
dc.typeArticleen
dc.identifier.journalActa crystallographica. Section F, Structural biology and crystallization communicationsen

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