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.; 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. ISSN 1744-3091

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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 angstrom) and the crystals diffracted to 2.0 angstrom resolution.

    Item Type: Article
    Creators:
    1. Gabrielsen, M.
    2. Abdul-Rahman, P.S.
    3. Isaacs, N.W.
    4. Hashim, O.H.(Department of Molecular Medicine, Faculty of Medicine Building, University of Malaya, 50603 Kuala Lumpur, MALAYSIA)
    5. Cogdell, R.J.
    Journal or Publication Title: Acta Crystallographica Section F-Structural Biology and Crystallization Communications
    Additional Information: Gabrielsen, Mads Abdul-Rahman, Puteri Shafinaz Isaacs, Neil W. Hashim, Onn Haji Cogdell, Richard J. Part 5
    Uncontrolled Keywords: lectins; Artocarpus integer; champedak; mannose binding.
    Subjects: R Medicine
    Divisions: Faculty of Medicine
    Depositing User: Ms Haslinda Lahuddin
    Date Deposited: 10 Jul 2012 09:12
    Last Modified: 10 Jul 2012 09:12
    URI: http://eprints.um.edu.my/id/eprint/3434

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