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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Purification and crystallization of ferric enterobactin receptor protein, FepA, from the outer membranes of Escherichia coli UT5600/pBB2.

The ferric enterobactin receptor protein, FepA, was isolated and purified from the outer membranes of a genetically transformed strain of Escherichia coli (UT5600/pBB2) using anion-exchange chromatography, chromatofocusing and gel filtration. The purified protein was found to crystallize from 25 mM sodium phosphate buffer in the presence of 0.8% beta-D-octylglucoside under a range of conditions. The protein formed mostly small rods and needle-shaped crystals in the hanging drop method.[1]

References

  1. Purification and crystallization of ferric enterobactin receptor protein, FepA, from the outer membranes of Escherichia coli UT5600/pBB2. Jalal, M.A., van der Helm, D. FEBS Lett. (1989) [Pubmed]
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