Expression, purification and crystallization of an archaeal-type phosphoenolpyruvate carboxylase.
An archaeal-type phosphoenolpyruvate carboxylase (PepcA) from Clostridium perfringens has been expressed in Escherichia coli in a soluble form with an amino-terminal His tag. The recombinant protein is enzymatically active and two crystal forms have been obtained. Complete diffraction data extending to 3.13 angstrom resolution have been measured from a crystal soaked in KAu(CN)(2), using radiation at a wavelength just above the Au L(III) edge. The asymmetric unit contains two tetramers of PepcA.
Dharmarajan
Lakshmi
L
Virginia Bioinformatics Institute, USA.
Kraszewski
Jessica L
JL
Mukhopadhyay
Biswarup
B
Dunten
Pete W
PW
D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003016:Clostridium perfringens / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D010730:Phosphoenolpyruvate Carboxylase / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D014961:X-Ray Diffraction
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D007527:Isoenzymes; D011994:Recombinant Proteins; D010730:Phosphoenolpyruvate Carboxylase