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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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Bibliographic Details
Main Authors: Radzimanowski, Jens (Author) , Ravaud, Stéphanie (Author) , Schott, Andrea (Author) , Strahl, Sabine (Author) , Sinning, Irmgard (Author)
Format: Article (Journal)
Language:English
Published: January 2010
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
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Author Notes:Jens Radzimanowski, Stephanie Ravaud, Andrea Schott, Sabine Strahl and Irmgard Sinning
Description
Summary: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.
Item Description:Gesehen am 23.05.2017
Physical Description:Online Resource
ISSN:2053-230X
DOI:10.1107/S1744309109042018

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