01624nas a2200193   4500008004100000022001400041245012700055210006900182260007600251300001400327490000700341520084900348653002001197653002001217100002001237700001901257700002401276856013001300       2011                        eng d  a1744-309100aPurification, crystallization and preliminary X-ray characterization of a haemagglutinin from the seeds of Jatropha curcas0 aPurification crystallization and preliminary Xray characterizati  aCOMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USAbWILEY-BLACKWELLcDEC  a1534-15360 v673 a<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>10ahaemagglutinins10aJatropha curcas1 aNair, Divya, N.1 aSuresh, C., G.1 aSingh, Desh, Deepak  uhttps://library.ncl.res.in/content/purification-crystallization-and-preliminary-x-ray-characterization-haemagglutinin-seeds-0