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Crystallization and initial X-ray diffraction analysis of a mannose-binding lectin from champedak.

Authors :
Gabrielsen, Mads
Abdul-Rahman, Puteri Shafinaz
Isaacs, Neil W.
Hashim, Onn Haji
Cogdell, Richard J.
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