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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 7
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pubmed:dateCreated |
2000-10-13
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pubmed:abstractText |
The vacuolar aspartic proteinase from baker's yeast, saccharopepsin, has been co-crystallized with its natural inhibitor I(A)3, found in the cytosol. The I(A)3-saccharopepsin complex crystals belong to the space group P6(2)22, with unit-cell parameters a = b = 192.1, c = 59. 80 A and one molecule per asymmetric unit. The initial X-ray analysis of the complex indicates that the crystals diffract to 5.0 A, similar to native saccharopepsin crystals. This is probably a consequence in part of glycosylation of the native saccharopepsin. Full structural analysis of the complex crystal is in progress.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0907-4449
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
915-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
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pubmed:year |
2000
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pubmed:articleTitle |
Purification, co-crystallization and preliminary X--ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae.
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pubmed:affiliation |
Departments of Microbiology and Oral Science, University of Minnesota, 18-246 Moos Tower, 515 Delaware Street SE, Minneapolis, MN 55455, USA. mohammed@dcmir.med.umn.edu.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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