@article { ISI:000297741100014,
	title = {Purification, crystallization and preliminary X-ray characterization of a haemagglutinin from the seeds of Jatropha curcas},
	journal = {Acta Crystallographica Section F-Structural Biology and Crystallization Communications},
	volume = {67},
	number = {12},
	year = {2011},
	month = {DEC},
	pages = {1534-1536},
	publisher = {WILEY-BLACKWELL},
	address = {COMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USA},
	abstract = {<p>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 P212121. The crystals diffracted to 2.8 angstrom resolution at 103 K.</p>},
	keywords = {haemagglutinins, Jatropha curcas},
	issn = {1744-3091},
	doi = {10.1107/S1744309111038218},
	author = {Nair, Divya N. and Suresh, C. G. and Singh, Desh Deepak}
}
