PMID:2125278: Difference between revisions

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<span style = 'font-size: large'> '''Wigley, DB, Derrick, JP and Shaw, WV'''  (1990) The serine acetyltransferase from Escherichia coli. Over-expression, purification and preliminary crystallographic analysis.''FEBS Lett.'' '''277''':267-71</span>
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!align=left  |Citation
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'''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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!align=left  |Abstract
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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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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2125278 PubMed]


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|{{TableHeadingColor}} |'''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).
!align=left  |Keywords
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Acetyltransferases/genetics; Acetyltransferases/isolation & purification; Acetyltransferases/ultrastructure; Chromatography, Gel; Cloning, Molecular; Crystallography; Escherichia coli/enzymology; Gene Expression; Molecular Structure; Serine; Serine O-Acetyltransferase
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2125278 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}

Revision as of 19:11, 1 September 2013

Citation

No author listed (1990) The serine acetyltransferase from Escherichia coli. Over-expression, purification and preliminary crystallographic analysis. FEBS Lett. 277:267-71

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).

Links

PubMed

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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