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

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|66|1|12-14

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.66, Iss.1, 2010-01, pp. : 12-14

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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.

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