title: Purification, crystallization and preliminary X-ray characterization of a haemagglutinin from the seeds of Jatropha curcas.
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.
authors.affiliation: Bioinformatics and Structural Biology, Indian Institute of Advanced Research, Koba, Gandhinagar, India.
authors.forename: Divya N
authors.initials: DN
authors.lastname: Nair
authors.forename: C G
authors.initials: CG
authors.lastname: Suresh
authors.forename: Desh Deepak
authors.initials: DD
authors.lastname: Singh
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006388:Hemagglutinins / Q000737:chemistry* / Q000302:isolation & purification; D031286:Jatropha / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry
chemical_list: D006388:Hemagglutinins