Crystallization of monodisperse maltoporin from wild-type and mutant strains of various Enterobacteriaceae.
Maltoporin has been purified by affinity chromatography on starch gel columns. This single-step procedure affords the rapid purification of active protein from wild-type and mutants of E. coli, and from other Gram-negative bacteria. The monodisperse protein was crystallized under various conditions. Several preparations have yielded crystals amendable to X-ray analysis, notably a single cysteine substitution, S57C.
Keller
T A
TA
Department of Microbiology, University of Basel, Switzerland.
Ferenci
T
T
Prilipov
A
A
Rosenbusch
J P
JP
D001425:Bacterial Outer Membrane Proteins / Q000302:isolation & purification; D002846:Chromatography, Affinity; D003460:Crystallization; D018360:Crystallography, X-Ray; D004755:Enterobacteriaceae / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D007711:Klebsiella pneumoniae / Q000378:metabolism*; D016296:Mutagenesis; D018272:Porins; D011991:Receptors, Virus / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification*; D013045:Species Specificity
D001425:Bacterial Outer Membrane Proteins; D018272:Porins; D011991:Receptors, Virus; C016532:maltoporins