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pubmed-article:12832801pubmed:abstractTextThermococcus litoralis uses a modified Embden-Meyerhof pathway. Its phosphofructokinase (TLPFK) catalyses the phosphorylation of fructose-6-phosphate by ADP, but not by ATP, in the presence of Mg(2+), yielding fructose-1,6-bisphosphate. The gene encoding TLPFK was cloned and overexpressed in Escherichia coli. Recombinant TLPFK consists of a dimer with a 52 kDa subunit. The native crystals belong to space group P4(1)2(1)2, with unit-cell parameters a = b = 85.41, c = 163.93 A, and diffract to beyond 2.6 A resolution. The TLPFK structure was preliminarily analyzed by means of multiple isomorphous replacement with four heavy-atom derivatives.lld:pubmed
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pubmed-article:12832801pubmed:authorpubmed-author:ShounHirofumi...lld:pubmed
pubmed-article:12832801pubmed:authorpubmed-author:WakagiTakayos...lld:pubmed
pubmed-article:12832801pubmed:authorpubmed-author:FushinobuShin...lld:pubmed
pubmed-article:12832801pubmed:authorpubmed-author:JeongJong-Jin...lld:pubmed
pubmed-article:12832801pubmed:authorpubmed-author:ItoSoheiSlld:pubmed
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pubmed-article:12832801pubmed:volume59lld:pubmed
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pubmed-article:12832801pubmed:pagination1327-9lld:pubmed
pubmed-article:12832801pubmed:dateRevised2007-7-24lld:pubmed
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pubmed-article:12832801pubmed:year2003lld:pubmed
pubmed-article:12832801pubmed:articleTitleArchaeal ADP-dependent phosphofructokinase: expression, purification, crystallization and preliminary crystallographic analysis.lld:pubmed
pubmed-article:12832801pubmed:affiliationDepartment of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.lld:pubmed
pubmed-article:12832801pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12832801pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed