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Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of SDF2-like protein from Arabidopsis thaliana.

ABSTRACT: The stromal-cell-derived factor 2-like protein of Arabidopsis thaliana (AtSDL) has been shown to be highly up-regulated in response to unfolded protein response (UPR) inducing reagents, suggesting that it plays a crucial role in the plant UPR pathway. AtSDL has been cloned, overexpressed, purified and crystallized using the vapour-diffusion method. Two crystal forms have been obtained under very similar conditions. The needle-shaped crystals did not diffract X-rays, while the other form diffracted to 1.95 A resolution using a synchrotron-radiation source and belonged to the hexagonal space group P6(1), with unit-cell parameters a = b = 96.1, c = 69.3 A.

SUBMITTER: Radzimanowski J

PROVIDER: S-EPMC2805525 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature

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Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of SDF2-like protein from Arabidopsis thaliana.

Radzimanowski Jens J Ravaud Stephanie S Schott Andrea A Strahl Sabine S Sinning Irmgard I

Acta crystallographica. Section F, Structural biology and crystallization communications 20091225 Pt 1

The stromal-cell-derived factor 2-like protein of Arabidopsis thaliana (AtSDL) has been shown to be highly up-regulated in response to unfolded protein response (UPR) inducing reagents, suggesting that it plays a crucial role in the plant UPR pathway. AtSDL has been cloned, overexpressed, purified and crystallized using the vapour-diffusion method. Two crystal forms have been obtained under very similar conditions. The needle-shaped crystals did not diffract X-rays, while the other form diffract ...[more]

PMID: 20057059

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