title: Crystallization and preliminary crystallographic analysis of a C2 protein from Arabidopsis thaliana.
abstract: 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 P2(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.
authors.affiliation: Departamento de Cristalografía y Biología Estructural, Instituto de Química Física Rocasolano, CSIC, Madrid, Spain.
authors.forename: Maira
authors.initials: M
authors.lastname: Diaz
authors.forename: Lesia
authors.initials: L
authors.lastname: Rodriguez
authors.forename: Miguel
authors.initials: M
authors.lastname: Gonzalez-Guzman
authors.forename: Martín
authors.initials: M
authors.lastname: Martínez-Ripoll
authors.forename: Armando
authors.initials: A
authors.lastname: Albert
mesh_terms: D017360:Arabidopsis / Q000737:chemistry*; D029681:Arabidopsis Proteins / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray
chemical_list: D029681:Arabidopsis Proteins; D002352:Carrier Proteins