Expression, purification and crystallization of the cell‐division protein YgfE from Escherichia coli
An open reading frame designated b2910 (ygfE) in the Escherichia coli K12‐MG1655 genome sequence, identified as a possible homologue to the cell‐division protein ZapA, was cloned into the high‐expression plasmid pETDuet‐1 and overexpressed in E. coli BL21 (DE3)‐AI. The protein was purified in three steps to 99% purity. Crystals were obtained by the hanging‐drop vapour‐diffusion method at 291 K from a wide range of screened conditions, but principally from solutions containing 0.1 M HEPES pH 7.0, 18% PEG 6000, 5 mM CaCl2. Diffraction data to 1.8 Å were collected at the European Synchrotron Radiation Facility (ESRF). The crystals belong to space group P6122 or P6522, with unit‐cell parameters a = 53.8, b = 53.8, c = 329.7 Å, α = β = 90, γ = 120°.
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