Open AccessCrystallization and preliminary crystallographic analysis of a C2 protein from Arabidopsis thaliana
Author(s) -
Diaz Maira,
Rodriguez Lesia,
GonzalezGuzman Miguel,
MartínezRipoll Martín,
Albert Armando
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111040541
Subject(s) - crystallization , arabidopsis thaliana , crystallography , protein data bank (rcsb pdb) , molecular replacement , escherichia coli , resolution (logic) , chemistry , arabidopsis , biology , crystal structure , stereochemistry , biochemistry , gene , computer science , organic chemistry , artificial intelligence , mutant
An uncharacterized protein from Arabidopsis thaliana consisting of a single C2 domain ( At 3g17980) 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 P 2 1 2 1 2 1 , 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.