Open AccessCrystallization 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.