Expression, purification and crystallization of an archaeal-type phosphoenolpyruvate carboxylase.
Acta crystallographica. Section F, Structural biology and crystallization communications(2009)
摘要
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.
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关键词
phosphoenolpyruvate carboxylase,recombinant proteins,isoenzymes,crystallization,x ray diffraction
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