博文
大肠杆菌中半胱氨酸合成过程中的一个酶的纯化，过表达
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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 (Vm = 2.55 Å3/Da).
fulltext: The serine acetyltransferase from E. coli
另一篇：大肠杆菌和沙门氏菌中酶促合成的半胱氨酸的过程：
The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimuriumhttps://blog.sciencenet.cn/blog-3533-11616.html
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