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Expression, purification and crystallization of the cell-division protein YgfE from Escherichia coli
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Dr Stephen Addinall
Addinall SG, Johnson KA, Dafforn T, Smith C, Rodger A, Gomez RP, Sloan K, Blewett A, Scott DJ, Roper DI
Acta Crystallographica Section F Structural Biology and Crystallization Communications
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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 A were collected at the European Synchrotron Radiation Facility (ESRF). The crystals belong to space group P6(1)22 or P6(5)22, with unit-cell parameters a = 53.8, b = 53.8, c = 329.7 A, alpha = beta = 90, gamma = 120 degrees.
Wiley-Blackwell Publishing, Inc.
Addinall, Stephen G Johnson, Kenneth A Dafforn, Timothy Smith, Corinne Rodger, Alison Gomez, Raul Paco Sloan, Katherine Blewett, Anne Scott, David J Roper, David I United Kingdom Wellcome Trust Research Support, Non-U.S. Gov't England Acta crystallographica. Section F, Structural biology and crystallization communications Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Mar 1;61(Pt 3):305-7. Epub 2005 Feb 24.
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