Crystallization and initial X-ray diffraction analysis of a mannose-binding lectin from champedak
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 alt...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | en |
| Published: |
2010
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| Subjects: | |
| Online Access: | http://eprints.um.edu.my/3434/1/Crystallization_and_initial_X-ray_diffraction_analysis_of_a_mannose-binding_lectin_from_champedak.pdf http://eprints.um.edu.my/3434/ http://scripts.iucr.org/cgi-bin/paper?hc5104 |
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| Summary: | 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. |
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