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 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.
Radzimanowski
Jens
J
Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
Ravaud
Stephanie
S
Schott
Andrea
A
Strahl
Sabine
S
Sinning
Irmgard
I
D017360:Arabidopsis / Q000235:genetics; D029681:Arabidopsis Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D003460:Crystallization; D056811:Unfolded Protein Response; D014961:X-Ray Diffraction
D029681:Arabidopsis Proteins