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 Å resolution using a synchrotron-radiation source and belonged to the hexagonal space group P61, with unit-cell parameters a = b = 96.1, c = 69.3 Å. © 2010.
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CITATION STYLE
Radzimanowski, J., Ravaud, S., Schott, A., Strahl, S., & Sinning, I. (2009). Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of SDF2-like protein from Arabidopsis thaliana. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(1), 12–14. https://doi.org/10.1107/S1744309109042018
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