Crystallization and preliminary crystallographic analysis of a C2 protein from Arabidopsis thaliana

4 pags, 3 figs, 1 tab
An uncharacterized protein from Arabidopsis thaliana consisting of a single C2 domain (At3g17980) was cloned into the pETM11 vector and expressed in Escherichia coli, allowing purification to homogeneity in a single chromatographic step. Good-quality diffracting crystals were obtained using vapour-diffusion techniques. The crystals diffracted to 2.2 Å resolution and belonged to space group P212121, with unit-cell parameters a = 35.3, b = 88.9, c = 110.6 Å. A promising molecular-replacement solution has been found using the structure of the C2 domain of Munc13-C2b (PDB entry 3kwt) as the search model. © 2011 International Union of Crystallography. All rights reserved.
his work was funded by grants BFU2008-00368/BMC, BFU2011-25384 and CSD2006-00015 (Factoría de Cristalización) of the Spanish ‘Plan Nacional’ (MICINN) to AA. MD was supported by fellowship SENACYT-IFARHU of Panama–‘Programa de Investigadores’.