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Purification and crystallization of ferric enterobactin receptor protein, FepA, from the outer membranes of Escherichia coli UT5600/pBB2
Author(s) -
Jalal M.A.F.,
van der Helm D.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80163-2
Subject(s) - enterobactin , escherichia coli , bacterial outer membrane , chromatography , size exclusion chromatography , chemistry , membrane , ultrafiltration (renal) , fast protein liquid chromatography , chromatofocusing , ferric , phosphate , sodium , biochemistry , high performance liquid chromatography , inorganic chemistry , organic chemistry , gene , enzyme
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% β‐D‐octylglucoside under a range of conditions. The protein formed mostly small rods and needle‐shaped crystals in the hanging drop method.