Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis.
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.
Wright
Lisa
L
Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, England.
Blagova
Elena
E
Levdikov
Vladimir M
VM
Brannigan
James A
JA
Pattenden
Rebecca J
RJ
Chambers
Janet
J
Wilkinson
Anthony J
AJ
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
D001426:Bacterial Proteins; D002352:Carrier Proteins; D004269:DNA, Bacterial; D011994:Recombinant Proteins