Purification, crystallization and preliminary X-ray diffraction analysis of the plant Rho protein ROP5.
The small G protein ROP5 from the model plant Arabidopsis thaliana was purified and crystallized using the hanging-drop vapour-diffusion method. ROP5 crystals were obtained using PEG 3000 as precipitant and belong to space group P2(1). A data set was collected to 1.53 A resolution using synchrotron radiation at 100 K. A clear molecular-replacement solution was found using ROP4-GDP of the ROP4-GDP-PRONE8 complex as the search model.
Thomas
Christoph
C
Department of Structural Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany. cthomas@stanford.edu
Berken
Antje
A
D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics; D003460:Crystallization; D014961:X-Ray Diffraction; D020741:rho GTP-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D020741:rho GTP-Binding Proteins