PMID:2125278
| Citation |
No author listed (1990) The serine acetyltransferase from Escherichia coli. Over-expression, purification and preliminary crystallographic analysis. FEBS Lett. 277:267-71 |
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| 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 A resolution are of the tetragonal spacegroup P4(1)2(1)2 (or P4(3)2(1)2) with cell dimensions a = b = 123 A, c = 79 A. Since ultracentrifugation and gel-filtration experiment indicate that purified SAT is a tetramer, there appears to be one-half tetramer in the asymmetric unit (Vm = 2.55 A3/Da). |
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| Keywords |
Acetyltransferases/genetics; Acetyltransferases/isolation & purification; Acetyltransferases/ultrastructure; Chromatography, Gel; Cloning, Molecular; Crystallography; Escherichia coli/enzymology; Gene Expression; Molecular Structure; Serine; Serine O-Acetyltransferase |
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