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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.

SUBMITTER: Gabrielsen M

PROVIDER: S-EPMC2864700 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature

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

Gabrielsen Mads M Abdul-Rahman Puteri Shafinaz PS Isaacs Neil W NW Hashim Onn Haji OH Cogdell Richard J RJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20100430 Pt 5

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 ...[more]

PMID: 20445267

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