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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt 12):1534-6. doi: 10.1107/S1744309111038218. Epub 2011 Nov 25.

Purification, crystallization and preliminary X-ray characterization of a haemagglutinin from the seeds of Jatropha curcas.

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1
Bioinformatics and Structural Biology, Indian Institute of Advanced Research, Koba, Gandhinagar, India.

Abstract

The plant Jatropha curcas (Euphorbiaceae) is an important source of biofuel from the inedible oil present in its toxic seeds. The toxicity arises from the presence of curcin, a ribosome-inactivating protein showing haemagglutination activity. In this communication, the purification, crystallization and preliminary X-ray characterization are reported of a small protein isolated from J. curcas seeds with a molecular mass of ~10 kDa that agglutinates rabbit erythrocytes. The protein was crystallized using the hanging-drop vapour-diffusion method and also by the microbatch method in 72-well HLA plates, using PEG 8000 as the precipitant in both conditions. X-ray diffraction data collected from the rod-shaped crystals were processed in the orthorhombic space group P2(1)2(1)2(1). The crystals diffracted to 2.8 Å resolution at 103 K.

PMID:
22139159
PMCID:
PMC3232132
DOI:
10.1107/S1744309111038218
[Indexed for MEDLINE]
Free PMC Article

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