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Crystallization and preliminary X‐ray analysis of the complex between a Bacillus subtilis α/β‐type small acid‐soluble spore protein and DNA

Crystallization and preliminary X‐ray analysis of the complex between a Bacillus subtilis... An engineered variant of an α/β‐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 Å 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 P6122 or P6522, with unit‐cell parameters a = b = 87.0, c = 145.4 Å, α = β = 90.0, γ = 120.0°. Diffraction data were 96.6% complete to 2.4 Å resolution, with an Rsym of 8.5%. Structure solution by the multiwavelength/single‐wavelength anomalous dispersion method using isomorphous crystals of selenomethionine‐labeled protein is in progress. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary X‐ray analysis of the complex between a Bacillus subtilis α/β‐type small acid‐soluble spore protein and DNA

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References (17)

Publisher
Wiley
Copyright
Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309107022750
pmid
17554173
Publisher site
See Article on Publisher Site

Abstract

An engineered variant of an α/β‐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 Å 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 P6122 or P6522, with unit‐cell parameters a = b = 87.0, c = 145.4 Å, α = β = 90.0, γ = 120.0°. Diffraction data were 96.6% complete to 2.4 Å resolution, with an Rsym of 8.5%. Structure solution by the multiwavelength/single‐wavelength anomalous dispersion method using isomorphous crystals of selenomethionine‐labeled protein is in progress.

Journal

Acta Crystallographica Section FWiley

Published: Jun 1, 2007

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