Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of SDF2-like protein from Arabidopsis thaliana
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 a...
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| Main Authors: | , , , , |
|---|---|
| Format: | Article (Journal) |
| Language: | English |
| Published: |
January 2010
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| In: |
Acta crystallographica. Section F, Structural biology communications
Year: 2010, Volume: 66, Issue: 1, Pages: 12-14 |
| ISSN: | 2053-230X |
| DOI: | 10.1107/S1744309109042018 |
| Online Access: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1107/S1744309109042018 Verlag, kostenfrei, Volltext: http://scripts.iucr.org/cgi-bin/paper?bw5312 |
| Author Notes: | Jens Radzimanowski, Stephanie Ravaud, Andrea Schott, Sabine Strahl and Irmgard Sinning |
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| 520 | |a 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. | ||
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