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Updated: Jun 18, 2026
Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
Published on: December 17, 2016
Expression, purification and crystallization of an archaeal-type phosphoenolpyruvate carboxylase
Lakshmi Dharmarajan1, Jessica L Kraszewski, Biswarup Mukhopadhyay
1Virginia Bioinformatics Institute, USA.
Abstract:
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.
