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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1997-8-18
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pubmed:abstractText |
Peptidyl-tRNA hydrolase from Escherichia coli, a monomer of 21 kDa, was overexpressed from its cloned gene pth and crystallized by using polyethylene glycol as precipitant. The crystals are orthorhombic and have unit cell parameters a = 47.24 A, b = 63.59 A, and c = 62.57 A. They belong to space group P2(1)2(1)2(1) and diffract to better than 1.2 A resolution. The structure is being solved by multiple isomorphous replacement.
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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 |
May
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pubmed:issn |
0887-3585
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
135-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9144799-1-Propanol,
pubmed-meshheading:9144799-Carboxylic Ester Hydrolases,
pubmed-meshheading:9144799-Cell Line,
pubmed-meshheading:9144799-Crystallization,
pubmed-meshheading:9144799-Crystallography, X-Ray,
pubmed-meshheading:9144799-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9144799-Escherichia coli,
pubmed-meshheading:9144799-Polyethylene Glycols
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pubmed:year |
1997
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pubmed:articleTitle |
Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase.
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pubmed:affiliation |
Laboratoire de Biochimie, Unité de Recherche Associée 1970 du Centre National de la Recherche Scientifique, Palaiseau, France.
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pubmed:publicationType |
Journal Article
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