ArticleActa crystallographica. Section D, Biological crystallography2003
Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY.
Article in Acta crystallographica. Section D, Biological crystallography, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Article
- Nucleotide-binding flexibility in ultrahigh-resolution structures of the SRP GTPase Ffh.Acta crystallographica. Section D, Biological crystallography · 2008Article
- Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY.Journal of structural biology · 2007Article
- X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases.Proteins · 2007Article
- SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting.RNA (New York, N.Y.) · 2007Article
- Analysis of protein hydration in ultrahigh-resolution structures of the SRP GTPase Ffh.Acta crystallographica. Section D, Biological crystallography · 2006Article
- Structure of a GDP:AlF4 complex of the SRP GTPases Ffh and FtsY, and identification of a peripheral nucleotide interaction site.Journal of molecular biology · 2006Article
- Heterodimeric GTPase core of the SRP targeting complex.Science (New York, N.Y.) · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The GTPases Ffh and FtsY are components of the prokaryotic signal recognition particle protein-targeting pathway. The two proteins interact in a GTP-dependent manner, forming a complex that can be stabilized by use of the non-hydrolyzable GTP analog GMPPCP. Crystals of the complex of the NG GTPase domains of the two proteins have been obtained from ammonium sulfate solutions. Crystals grow with several different morphologies, predominately as poorly diffracting plates and needle clusters, but occasionally as well diffracting rods. It has been demonstrated that all forms of the crystals observed contain an intact complex. Diffraction data to 2.0 A resolution have been measured.
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Registered trials
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