Expression, purification and crystallization of penicillin G acylase from Escherichia coli ATCC 11105
- 1 July 1990
- journal article
- research article
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 3 (7) , 635-639
- https://doi.org/10.1093/protein/3.7.635
Abstract
The penicillin acylase gene (pac) from Escherichia coli ATCC 11105 was cloned into pUC 9 and the resulting vector (pUPA-9), when transformed into E.coli strain 5K, allowed the constitutive overproduction of mature penicillin acylase when grown at 28°C. The enzyme ws purified from the periplasmic fraction of E.coli pUPA-9 by hydrophobic interaction chromatography and anion exchange. Crystals of penicillin acylase were grown in batch using polyethylene glycol 8000 as a precipitant. The crystals (space group P1) diffracted to beyond 2.3 Å.This publication has 6 references indexed in Scilit:
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