ArticleActa crystallographica. Section F, Structural biology and crystallization communications2007
Crystallization and preliminary X-ray analysis of the complex between a Bacillus subtilis alpha/beta-type small acid-soluble spore protein and DNA.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- Photochemistry and Photobiology of the Spore Photoproduct: A 50-Year Journey.Photochemistry and photobiology · 2015Review
- The enzyme-mediated direct reversal of a dithymine photoproduct in germinating endospores.International journal of molecular sciences · 2013Article
- Mechanistic studies of the radical SAM enzyme spore photoproduct lyase (SPL).Biochimica et biophysica acta · 2012Review
- Mechanistic studies of the spore photoproduct lyase via a single cysteine mutation.Biochemistry · 2012Article
- Structure of a protein-DNA complex essential for DNA protection in spores of Bacillus species.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Effect of a small, acid-soluble spore protein from Clostridium perfringens on the resistance properties of Bacillus subtilis spores.Journal of bacteriology · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
An engineered variant of an alpha/beta-type small acid-soluble spore protein (SASP) from Bacillus subtilis was crystallized in a complex with a ten-base-pair double-stranded DNA by the hanging-drop vapor-diffusion method using ammonium sulfate as a precipitating agent. Crystals grew at 281 K using sodium cacodylate buffer pH 5.5 and these crystals diffracted X-rays to beyond 2.4 A resolution using synchrotron radiation. The crystallized complex contains two or three SASP molecules bound to one DNA molecule. The crystals belong to the hexagonal space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 87.0, c = 145.4 A, alpha = beta = 90.0, gamma = 120.0 degrees. Diffraction data were 96.6% complete to 2.4 A resolution, with an R(sym) of 8.5%. Structure solution by the multiwavelength/single-wavelength anomalous dispersion method using isomorphous crystals of selenomethionine-labeled protein is in progress.
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Registered trials
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