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Purification, crystallization and preliminary X-ray diffraction analysis of the plant Rho protein ROP5.

ABSTRACT: 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.

SUBMITTER: Thomas C

PROVIDER: S-EPMC2344096 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray diffraction analysis of the plant Rho protein ROP5.

Thomas Christoph C Berken Antje A

Acta crystallographica. Section F, Structural biology and crystallization communications 20071130 Pt 12

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. ...[more]

PMID: 18084097

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