Open AccessPurification, crystallization and preliminary X‐ray characterization of a haemagglutinin from the seeds of Jatropha curcas
Author(s) -
Nair Divya N.,
Suresh C. G.,
Singh Desh Deepak
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111038218
Subject(s) - jatropha curcas , euphorbiaceae , crystallization , orthorhombic crystal system , chemistry , nuclear chemistry , chromatography , biology , botany , crystallography , crystal structure , organic chemistry
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 P 2 1 2 1 2 1 . The crystals diffracted to 2.8 Å resolution at 103 K.