title: Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis.
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.
authors.affiliation: Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England.
authors.forename: Lisa
authors.initials: L
authors.lastname: Wright
authors.forename: Elena
authors.initials: E
authors.lastname: Blagova
authors.forename: Vladimir M
authors.initials: VM
authors.lastname: Levdikov
authors.forename: James A
authors.initials: JA
authors.lastname: Brannigan
authors.forename: Rebecca J
authors.initials: RJ
authors.lastname: Pattenden
authors.forename: Janet
authors.initials: J
authors.lastname: Chambers
authors.forename: Anthony J
authors.initials: AJ
authors.lastname: Wilkinson
mesh_terms: D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics; D002852:Chromatography, Ion Exchange; D003460:Crystallization; D018360:Crystallography, X-Ray; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D004269:DNA, Bacterial; D011994:Recombinant Proteins