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

FEBS Letters

van der Helm, D.¹  Jalal, M.A.F.¹ 

[1] Department of Chemistry, University of Oklahoma, Norman, OK 73019, USA

关键词: Ferric enterobactin protein;    Purification;    Crystallization;    Outer membrane protein;    (E. coli);    Tris;    trihydroxymethylaminomethane;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    PEG;    polyethylene glycol;   

DOI  :  10.1016/0014-5793(89)80163-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown