Crystallization and preliminary X-ray crystallographic studies of the oxidative-stress sensor SoxR and its complex with DNA.
SoxR, a member of the MerR family of transcriptional activators, functions as a sensor of oxidative stress. The redox states of the 2Fe-2S cluster of SoxR regulate the activity of SoxR. Here, the crystallization and preliminary crystallographic analysis of SoxR and its complex with DNA are reported. Crystals of SoxR were obtained using PEG 10,000 and glycerol as precipitants. The crystals of SoxR belong to space group P6(2) or P6(4), with unit-cell parameters a = b = 80.0, c = 88.1 A. Crystals of the SoxR-DNA complex were obtained using a 20 bp DNA fragment from a condition containing PEG 10,000 and sodium/potassium tartrate. The crystals of the SoxR-DNA complex belong to space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 53.5, c = 355.6 A. Diffraction data were collected to a maximum resolution of 3.2 and 2.7 A for SoxR and the SoxR-DNA complex, respectively.
Watanabe
Satoshi
S
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Kita
Akiko
A
Kobayashi
Kazuo
K
Takahashi
Yasuhiro
Y
Miki
Kunio
K
D001426:Bacterial Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D004269:DNA, Bacterial / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D018384:Oxidative Stress; D014157:Transcription Factors / Q000737:chemistry*
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; D007506:Iron-Sulfur Proteins; D014157:Transcription Factors; C070724:SoxR protein, Bacteria