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The serine acetyltransferase from Escherichia coli
Author(s) -
Wigley Dale B.,
Derrick Jeremy P.,
Shaw William V.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80862-d
Subject(s) - tetramer , polyethylene glycol , chemistry , escherichia coli , serine , affinity chromatography , cysteine , size exclusion chromatography , peg ratio , acetyltransferase , chromatography , periplasmic space , biochemistry , enzyme , stereochemistry , acetylation , finance , economics , gene
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 P4 1 2 1 2(or P4 3 2 1 2) 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 Å 3 /Da).