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pubmed-article:8864839pubmed:abstractTextThe structure of GGT [EC 2.3.2.2] from E. coli K-12 was studied at 3 A resolution by X-ray crystallography. Initial protein phases were calculated using two kinds of Pb2+ derivatives. The phases were refined by non-crystallographic 2-fold symmetry electron density averaging combined with solvent flattening and histogram matching. The GGT molecule has overall dimensions of 60 x 50 x 40 A. There are two antiparallel beta-pleated sheets consisting of 6 and 7 beta-strands. The two beta-sheets form a wall-like structure. Twelve short alpha-helices were detected, of which the maximum length appears to be four helix turns.lld:pubmed
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pubmed-article:8864839pubmed:authorpubmed-author:SasakiKKlld:pubmed
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pubmed-article:8864839pubmed:volume120lld:pubmed
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pubmed-article:8864839pubmed:pagination26-8lld:pubmed
pubmed-article:8864839pubmed:dateRevised2007-12-19lld:pubmed
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pubmed-article:8864839pubmed:articleTitleA preliminary description of the crystal structure of gamma-glutamyltranspeptidase from E. coli K-12.lld:pubmed
pubmed-article:8864839pubmed:affiliationDepartment of Synchrotron Radiation Science, Graduate University for Advanced Studies and Photon Factory, National Laboratory for High Energy Physics, Ibaraki.lld:pubmed
pubmed-article:8864839pubmed:publicationTypeJournal Articlelld:pubmed
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