Crystallization and initial X‐ray diffraction analysis of a mannose‐binding lectin from champedak | Zendy

Gabrielsen Mads | Zendy; AbdulRahman Puteri Shafinaz | Zendy; Isaacs Neil W. | Zendy; Hashim Onn Haji | Zendy; Cogdell Richard J. | Zendy

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

Author(s) -

Gabrielsen Mads,

AbdulRahman Puteri Shafinaz,

Isaacs Neil W.,

Hashim Onn Haji,

Cogdell Richard J.

Publication year - 2010

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

ISSN - 1744-3091

DOI - 10.1107/s1744309110011760

Subject(s) - lectin , mannose , mannan binding lectin , concanavalin a , monomer , glycosylation , resolution (logic) , chemistry , crystallization , crystallography , biochemistry , in vitro , organic chemistry , artificial intelligence , computer science , polymer

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 P 2 1 2 1 2 1 (unit‐cell parameters a = 76.89, b = 86.22, c = 95.37 Å) and the crystals diffracted to 2.0 Å resolution.

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