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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 May 1;66(Pt 5):592-4. doi: 10.1107/S1744309110011760. Epub 2010 Apr 30.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Artocarpus / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Mannose-Binding Lectin / chemistry*

Substances

  • Mannose-Binding Lectin