Purification and crystallization of fumarase C from Escherichia coli.
Fumarase C purified from Escherichia coli has been crystallized in the presence of polyethylene glycol in both a citrate buffer at pH 5.3 and a 3-(4-morpholino)-propanesulfonic acid buffer at pH 7.5 yielding two crystal forms. An orthorhombic C222(1) form was obtained in citrate at pH 5.3 and an orthorhombic I222 form was obtained in 3-(4-morpholino)-propanesulfonic acid (pH 7.5). Complete native data sets have been collected on both crystal forms: the C222(1) form is complete to 2.10 A and the I222 form is complete to 2.20 A.
Department of Biochemistry, University of Minnesota, Minneapolis 55455.
T M
TM
Weaver
D G
DG
Levitt
L J
LJ
Banaszak
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005649:Fumarate Hydratase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D005798:Genes, Bacterial; D007527:Isoenzymes / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D007700:Kinetics; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014961:X-Ray Diffraction
D007527:Isoenzymes; D005649:Fumarate Hydratase