Details

Autor(en) / Beteiligte

• MA14ller, Alexandra
• Schlicker, Christine
• Fehringer, Maria
• Masepohl, Bernd
• Hofmann, Eckhard

Titel

Expression, purification, crystallization and preliminary Xaray analysis of the DNAabinding domain of Rhodobacter capsulatus MopB

Ist Teil von

• Acta crystallographica. Section F, Structural biology and crystallization communications, 2011-03, Vol.67 (3), p.377-379

Erscheinungsjahr

2011

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• The LysR-type regulator MopB represses transcription of several target genes (including the nitrogen-fixation gene anfA) in Rhodobacter capsulatus at high molybdenum concentrations. In this study, the isolated DNA-binding domain of MopB (MopBHTH) was overexpressed in Escherichia coli. Purified MopBHTH bound the anfA promoter as shown by DNA mobility-shift assays, demonstrating the function of the isolated regulator domain. MopBHTH was crystallized using the sitting-drop vapour-diffusion method in the presence of 0.2M lithium sulfate, 0.1M phosphate/citrate pH 4.2, 20%(w/v) PEG 1000 at 291K. The crystal belonged to space group P3121 or P3221, with unit-cell parameters a = b = 61.84, c = 139.64Aa, alpha = beta = 90, gamma = 120 degree , and diffracted to 3.3Aa resolution at a synchrotron source.