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Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis

By L Wright, E Blagova, V M Levdikov, J A Brannigan, R J Pattenden, J Chambers and A J Wilkinson

Abstract

AppA is the membrane-anchored extracellular receptor component of an ABC transporter responsible for the uptake of oligopeptides into Bacillus subtilis. AppA has been overexpressed as a cleavable maltose-binding protein fusion in Escherichia coli. Following removal of the fusion portion, AppA has been crystallized from morpholino-ethanesulfonic acid-buffered solutions at pH 6.5 containing polyethylene glycol and zinc acetate. A complete X-ray diffraction data set extending to 2.3 Angstrom spacing has been collected

Year: 2004
OAI identifier: oai:eprints.whiterose.ac.uk:457

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