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

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

    Research output: Contribution to journalArticlepeer-review

    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 (Vm = 2.55 Å3/Da). © 1990.
    Original languageEnglish
    Pages (from-to)267-271
    Number of pages4
    JournalFEBS Letters
    Volume277
    Issue number1-2
    DOIs
    Publication statusPublished - 17 Dec 1990

    Keywords

    • Acetyltransferase
    • Crystallisation
    • cysE

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