Details

Autor(en) / Beteiligte

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

Titel

Expression, purification, crystallization and preliminary X-ray analysis of the DNA-binding 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

Ort / Verlag

5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography

Erscheinungsjahr

2011

Quelle

Wiley Online Library All Journals

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 0.2 M lithium sulfate, 0.1 M phosphate/citrate pH 4.2, 20%(w/v) PEG 1000 at 291 K. The crystal belonged to space group P3121 or P3221, with unit‐cell parameters a = b = 61.84, c = 139.64 Å, α = β = 90, γ = 120°, and diffracted to 3.3 Å resolution at a synchrotron source.