doi: 10.1016/0014-5793(89)80163-2.
Purification and crystallization of ferric enterobactin receptor protein, FepA, from the outer membranes of Escherichia coli UT5600/pBB2
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- PMID: 2645172
- DOI: 10.1016/0014-5793(89)80163-2
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Purification and crystallization of ferric enterobactin receptor protein, FepA, from the outer membranes of Escherichia coli UT5600/pBB2
FEBS Lett.
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Abstract
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.
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