Purification, crystallization and preliminary X-ray crystallographic analysis of MIL, a glycosylated jacalin-related lectin from mulberry (Morus indica) latex.
| dc.contributor.author | Patel, Ashok K | |
| dc.contributor.author | Singh, Vijay K | |
| dc.contributor.author | Bergmann, Ulrich | |
| dc.contributor.author | Jagannadham, Medicherla V | |
| dc.contributor.author | Kursula, Petri | |
| dc.date.accessioned | 2014-08-08T10:42:32Z | en |
| dc.date.available | 2014-08-08T10:42:32Z | en |
| dc.date.issued | 2011-05-01 | en |
| dc.identifier.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. | en |
| dc.identifier.issn | 1744-3091 | en |
| dc.identifier.pmid | 21543873 | en |
| dc.identifier.doi | 10.1107/S174430911101013X | en |
| dc.identifier.uri | http://hdl.handle.net/10033/324483 | en |
| dc.description.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. | |
| dc.language.iso | en | en |
| dc.rights | Archived with thanks to Acta crystallographica. Section F, Structural biology and crystallization communications | en |
| dc.subject.mesh | Amino Acid Sequence | en |
| dc.subject.mesh | Crystallization | en |
| dc.subject.mesh | Crystallography, X-Ray | en |
| dc.subject.mesh | Glycosylation | en |
| dc.subject.mesh | Molecular Sequence Data | en |
| dc.subject.mesh | Morus | en |
| dc.subject.mesh | Plant Lectins | en |
| dc.subject.mesh | Sequence Alignment | en |
| dc.title | Purification, crystallization and preliminary X-ray crystallographic analysis of MIL, a glycosylated jacalin-related lectin from mulberry (Morus indica) latex. | en |
| dc.type | Article | en |
| dc.identifier.journal | Acta crystallographica. Section F, Structural biology and crystallization communications | en |
| refterms.dateFOA | 2018-06-13T00:25:20Z | |
| html.description.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. |
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publications of the research group CSSB [12]
structural biology of the cytoskeleton