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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.

SUBMITTER: Diaz M

PROVIDER: S-EPMC3232143 | biostudies-other | 2011 Dec

REPOSITORIES: biostudies-other

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

Diaz Maira M Rodriguez Lesia L Gonzalez-Guzman Miguel M Martínez-Ripoll Martín M Albert Armando A

Acta crystallographica. Section F, Structural biology and crystallization communications 20111126 Pt 12

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 ...[more]

PMID: 22139170

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