Related Experiment Videos
Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis
Lisa Wright1, Elena Blagova, Vladimir M Levdikov
1Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England.
Acta Crystallographica. Section D, Biological Crystallography
|December 20, 2003
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 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 A spacing has been collected.