Purification, characterization, and crystallization of an N-hydroxyarylamine O-acetyltransferase from Salmonella typhimurium

Protein Expression and Purification
John SinclairEdith Sim

Abstract

The N-hydroxyarylamine O-acetyltransferase from Salmonella typhimurium has been expressed as a histidine-tagged fusion protein in Escherichia coli and purified to apparent homogeneity using single-step immobilized metal ion chromatography. Sufficient quantities of the purified protein have been obtained to allow its characterization by physical methods including dynamic light scattering and electrospray mass spectrometry. The substrate specificity and temperature sensitivity of the enzymatic activity have also been assessed. The enzyme has been crystallized from sodium, potassium tartrate and X-ray diffraction data have been obtained to allow the identification of an orthorhombic unit cell, point group P21212, with dimensions a = 137 A, b = 223 A, and c = 105 A. These crystals will provide a route to a crystallographic determination of the structure of the protein.

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Citations

Jun 24, 2008·Journal of Toxicology and Environmental Health. Part a·Jutta LichterBrunhilde Blomeke
Mar 22, 2007·BMC Biochemistry·Isaac M Westwood, Edith Sim
Apr 23, 2002·Pharmacogenomics·Frédérique PompeoEdith Sim
Mar 12, 2003·Bioorganic & Medicinal Chemistry·Edward W BrookeRichard J Vickers
May 6, 2005·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·Larissa WakefieldEdith Sim
Jan 19, 2002·The Journal of Biological Chemistry·Adeel MushtaqEdith Sim
Jul 5, 2017·Molecular Pharmacology·Ximing XuFernando Rodrigues-Lima
Apr 22, 2010·The Journal of Pharmacology and Experimental Therapeutics·Jutta BonifasBrunhilde Blömeke
Jun 17, 2010·Toxicology Mechanisms and Methods·Malika KhelilBouchentouf Tayebi

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