3bwd | pdb_00003bwd
From Proteopedia
Crystal structure of the plant Rho protein ROP5
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Purification, crystallization and preliminary X-ray diffraction analysis of the plant Rho protein ROP5.,Thomas C, Berken A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Dec 1;63(Pt, 12):1070-2. Epub 2007 Nov 30. PMID:18084097[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 09:30, 29 September 2014.