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Crystallization and initial X-ray diffraction analysis of a mannose-binding lectin from champedak.
- Source :
-
Acta Crystallographica: Section F (Wiley-Blackwell) . May2010, Vol. 66 Issue 5, p592-594. 3p. - Publication Year :
- 2010
-
Abstract
- Mannose-binding lectin from champedak ( Artocarpus integer) is a homotetramer with a single-monomer molecular weight of 16 800 Da. Previous work has shown it to bind IgE and IgM, as well as being a mitogen of T cells in humans. Champedak mannose-binding lectin has successfully been used to detect altered glycosylation states of serum proteins. The protein was crystallized at 293 K in space group P212121 (unit-cell parameters a = 76.89, b = 86.22, c = 95.37 Å) and the crystals diffracted to 2.0 Å resolution. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 66
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 111657260
- Full Text :
- https://doi.org/10.1107/S1744309110011760