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

Gabrielsen, M., Abdul-Rahman, P.S., Isaacs, N.W., Hashim, O.H. and Cogdell, R.J. (2010) Crystallization and initial X-ray diffraction analysis of a mannose-binding lectin from champedak. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 66(5), pp. 592-594. (doi:10.1107/S1744309110011760)

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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 P2(1)2(1)2(1) (unit-cell parameters a = 76.89, b = 86.22, c = 95.37 A) and the crystals diffracted to 2.0 A resolution.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Gabrielsen, Dr Mads and Cogdell, Professor Richard and Isaacs, Professor Neil
Authors: Gabrielsen, M., Abdul-Rahman, P.S., Isaacs, N.W., Hashim, O.H., and Cogdell, R.J.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
College of Science and Engineering > School of Chemistry
Journal Name:Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
Publisher:Wiley-Blackwell Publishing, Inc.
ISSN:1744-3091
ISSN (Online):1744-3091

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