Research reports

The serine acetyltransferase from Escherichia coli Over-expression, purification and preliminary crystallographic analysis

Dale B. Wigley, Jeremy P. Derrick and William V. Shaw

Department of Biochemistry, University of Leicester, Leicester LE1 7RH, UK
Received 11 October 1990;  revised 25 October 1990.  Available online 21 November 2001.

Volume 277, Issues 1-2, 17 December 1990, Pages 267-271

Abstract

An expression vector has been constructed which increases the expression of serine acetyltransferase (SAT) from E. coli to 17% of the soluble cell protein. A novel purification procedure, using dye-affinity chromatography, allows purification of SAT to homogeneity. The enzyme has been crystallised from polyethylene glycol, in the presence of L-cysteine (an inhibitor of SAT). The crystals which diffract to beyond 3.0 Å resolution are of the tetragonal spacegroup P4₁2₁2(or P4₃2₁2) with cell dimensions a = b = 123 Å, c = 79 Å. Since ultracentrifugation and gel-filtration experiments indicate that purified SAT is a tetramer, there appears to be one-half tetramer in the asymmetric unit (V_m = 2.55 ų/Da).

 fulltext: The serine acetyltransferase from E. coli

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