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. 1995 May;177(9):2564–2566. doi: 10.1128/jb.177.9.2564-2566.1995

High-level expression of soluble recombinant RNase P protein from Escherichia coli.

R Rivera-León 1, C J Green 1, B S Vold 1
PMCID: PMC176919  PMID: 7730292

Abstract

We have expressed recombinant RNase P protein from Escherichia coli in high yield. A hexahistidine sequence at the amino terminus allowed protein purification in a single step. Mass spectrometry confirmed the molecular weight of the purified protein and indicated a purity of > 95%. Protein functionality was demonstrated by reconstitution of active holoenzyme.

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Selected References

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