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Updated: Apr 20, 2026

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Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
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[Purification of recombinant Bacillus cereus ResD-ResE proteins expressed in Escherichia coli strains]
Prikladnaia Biokhimiia I Mikrobiologiia
|December 2, 2014
Abstract:
Recombinant E. coli strains expressing the Bacillus cereus ATCC 14579T resD and resEgenes fused with the ubiquitin gene were constructed, and purification of the ResD and ResE proteins was performed. The approach used in the study allowed us to increase the protein yield of the electrophoretic homogeneous ResD andResE proteins without denaturation steps up to 150 mg per gram of wet cell weight.

