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pubmed-article:2668541pubmed:abstractTextHistidine-binding protein, purified from periplasmic space of Escherichia coli K12, has been crystallized in a form suitable for X-ray analysis. Crystals of average size 0.3 mm x 0.15 mm x 0.15 mm have been grown by the hanging-drop method, with ammonium sulfate as precipitant. The space group if I4(1)22, with the unit cell dimensions a = b = 119.1 A; c = 151.8 A; Vm = 2.7 A3/dalton. There appear to be two protein subunits of molecular weight 25,000 each in the asymmetric unit.lld:pubmed
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pubmed-article:2668541pubmed:authorpubmed-author:Chirgadze NYulld:pubmed
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pubmed-article:2668541pubmed:dateRevised2003-11-14lld:pubmed
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pubmed-article:2668541pubmed:articleTitleCrystallization and preliminary X-ray crystallographic data of a histidine-binding protein from Escherichia coli.lld:pubmed
pubmed-article:2668541pubmed:affiliationInstitute of Crystallography, Academy of Sciences of the USSR, Moscow.lld:pubmed
pubmed-article:2668541pubmed:publicationTypeJournal Articlelld:pubmed
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