| Literature DB >> 19923749 |
Lakshmi Dharmarajan1, Jessica L Kraszewski, Biswarup Mukhopadhyay, Pete W Dunten.
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.Entities:
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Year: 2009 PMID: 19923749 PMCID: PMC2777057 DOI: 10.1107/S1744309109042663
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091