Crystallization and initial X-ray diffraction analysis of a mannose-binding lectin from champedak.
نویسندگان
چکیده
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.
منابع مشابه
Crystallization and preliminary structural studies of champedak galactose-binding lectin.
Galactose-binding lectin from champedak (Artocarpus integer) consists of two chains: alpha and beta (133 and 21 amino acids, respectively). It has been shown to recognize and bind to carbohydrates involved in IgA and C1 inhibitor molecules. The protein was purified and crystallized at 293 K. Crystals were observed in two space groups, P2(1) and P2(1)2(1)2, and diffracted to 1.65 and 2.6 A, resp...
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عنوان ژورنال:
- Acta crystallographica. Section F, Structural biology and crystallization communications
دوره 66 Pt 5 شماره
صفحات -
تاریخ انتشار 2010