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

Journal Article · Sat Dec 01 00:00:00 EST 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309107059672· OSTI ID:22360442

Thomas, Christoph; Berken, Antje ^[1]

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1. Department of Structural Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund (Germany)

Crystals of the plant Rho protein ROP5 from A. thaliana have been obtained that diffract to 1.53 Å resolution. 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{sub 1}. A data set was collected to 1.53 Å 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.

• OSTI ID: 22360442
• Journal Information: Acta Crystallographica. Section F, Vol. 63, Issue Pt 12; Other Information: PMCID: PMC2344096; PMID: 18084097; PUBLISHER-ID: en5269; OAI: oai:pubmedcentral.nih.gov:2344096; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
DIFFUSION
MATHEMATICAL SOLUTIONS
RESOLUTION
SOLUTIONS
SPACE GROUPS
SYNCHROTRON RADIATION
X-RAY DIFFRACTION