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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 12(67), p. 1575-1578, 2011

DOI: 10.1107/s1744309111040541

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Crystallization and preliminary crystallographic analysis of a C2 protein fromArabidopsis thaliana

Journal article published in 2011 by Maira Diaz, Lesia Rodriguez, Miguel Gonzalez-Guzman ORCID, Martín Martínez-Ripoll, Armando Albert
This paper is available in a repository.
This paper is available in a repository.

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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 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.