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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1997-1-14
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pubmed:abstractText |
The 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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
120
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
26-8
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading | |
pubmed:year |
1996
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pubmed:articleTitle |
A preliminary description of the crystal structure of gamma-glutamyltranspeptidase from E. coli K-12.
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pubmed:affiliation |
Department of Synchrotron Radiation Science, Graduate University for Advanced Studies and Photon Factory, National Laboratory for High Energy Physics, Ibaraki.
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pubmed:publicationType |
Journal Article
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