Crystallization of the oligopeptide‐binding protein AppA from  Bacillus subtilis | Zendy

Wright Lisa | Zendy; Blagova Elena | Zendy; Levdikov Vladimir M. | Zendy; Brannigan James A. | Zendy; Pattenden Rebecca J. | Zendy; Chambers Janet | Zendy; Wilkinson Anthony J. | Zendy

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Crystallization of the oligopeptide‐binding protein AppA from Bacillus subtilis

Author(s) -

Wright Lisa,

Blagova Elena,

Levdikov Vladimir M.,

Brannigan James A.,

Pattenden Rebecca J.,

Chambers Janet,

Wilkinson Anthony J.

Publication year - 2004

Publication title -

acta crystallographica section d

Language(s) - English

Resource type - Journals

ISSN - 1399-0047

DOI - 10.1107/s0907444903025320

Subject(s) - bacillus subtilis , oligopeptide , escherichia coli , chemistry , polyethylene glycol , extracellular , fusion protein , biochemistry , maltose binding protein , crystallization , transporter , maltose , zinc , enzyme , biology , bacteria , peptide , organic chemistry , gene , recombinant dna , genetics

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 morpholinoethanesulfonic acid‐buffered solutions at pH 6.5 containing polyethylene glycol and zinc acetate. A complete X‐ray diffraction data set extending to 2.3 Å spacing has been collected.

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