Open AccessCrystallization and preliminary X‐ray analysis of the complex between a Bacillus subtilis α/β‐type small acid‐soluble spore protein and DNA
Author(s) -
Bumbaca Daniela,
Kosman Jeffrey,
Setlow Peter,
Henderson R. Keith,
Jedrzejas Mark J.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107022750
Subject(s) - bacillus subtilis , crystallization , spore , dna , microbiology and biotechnology , biology , chemistry , crystallography , biochemistry , bacteria , genetics , organic chemistry
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 P 6 1 22 or P 6 5 22, 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 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.