title: Crystallization and initial X-ray diffraction analysis of a mannose-binding lectin from champedak.
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.
authors.affiliation: Glasgow Biomedical Research Centre, Faculty of Biomedical and Life Sciences, Glasgow G12 8QQ, Scotland. m.gabrielsen@bio.gla.ac.uk
authors.forename: Mads
authors.initials: M
authors.lastname: Gabrielsen
authors.forename: Puteri Shafinaz
authors.initials: PS
authors.lastname: Abdul-Rahman
authors.forename: Neil W
authors.initials: NW
authors.lastname: Isaacs
authors.forename: Onn Haji
authors.initials: OH
authors.lastname: Hashim
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Cogdell
mesh_terms: D031622:Artocarpus / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D037601:Mannose-Binding Lectin / Q000737:chemistry*
chemical_list: D037601:Mannose-Binding Lectin
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