title: Crystallization and preliminary X-ray diffraction analysis of the TetR-family transcriptional repressor YhgD from Bacillus halodurans.
abstract: YhgD is a member of the TetR-family transcription factors, which regulate genes encoding proteins involved in multidrug resistance, virulence, osmotic stress and pathogenicity. YhgD from the alkaliphilic bacterium Bacillus halodurans was cloned and overexpressed in Escherichia coli. YhgD (Bh2145) from B. halodurans is composed of 193 amino-acid residues with a molecular mass of 21 853 Da. YhgD was crystallized at 296 K using ethylene glycol as a precipitant by the sitting-drop vapour-diffusion method. The crystal diffracted to 1.9 Å resolution and belonged to the apparent triclinic space group P1, with unit-cell parameters a = 37.22, b = 47.85, c = 54.15 Å, α = 92.75, β = 107.9, γ = 90.27°. The asymmetric unit is likely to contain two molecules of monomeric YhgD, giving a crystal volume per mass (VM) of 2.05 Å(3) Da(-1) and a solvent content of 40.2%.
authors.affiliation: Department of Life Science, Dongguk University-Seoul, 26 Pil-dong 3-ga, Jung-gu, Seoul 100-715, Republic of Korea.
authors.forename: Hyun Ku
authors.initials: HK
authors.lastname: Yeo
authors.forename: Young Woo
authors.initials: YW
authors.lastname: Park
authors.forename: Jina
authors.initials: J
authors.lastname: Kang
authors.forename: Jae Young
authors.initials: JY
authors.lastname: Lee
mesh_terms: D001407:Bacillus; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D012097:Repressor Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D012097:Repressor Proteins
keywords: TetR family; YhgD; transcriptional regulators