AI Article Synopsis
- An engineered variant of a small acid-soluble spore protein from Bacillus subtilis was crystallized with DNA using the hanging-drop vapor-diffusion method.
- The resulting crystals, grown at 281 K in sodium cacodylate buffer, diffracted X-rays to a resolution better than 2.4 A and contained multiple SASP molecules bound to a single DNA strand.
- The crystals belong to a specific hexagonal space group and the structure determination is currently underway using advanced techniques involving selenomethionine-labeled protein.
Article 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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2335083 | PMC |
| http://dx.doi.org/10.1107/S1744309107022750 | DOI Listing |
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