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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-8-24
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pubmed:abstractText |
A 25 kDa C-terminal tryptic fragment of elongation factor Ts has been purified to homogeneity. Experimental evidence suggests that the 25 kDa C-terminal and the 5.3 kDa N-terminal fragments are structurally independent domains. The N-terminal fragment is shown to be essential for the nucleotide exchange activity. Crystals of the C-terminal fragment belong to space group P2 or P2(1). The diffraction pattern shows a pronounced pseudo-C2 symmetry at low resolution. This pseudo symmetry increases when the crystals are irradiated with X-rays for a few hours.
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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 |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
368
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
49-54
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7615087-Amino Acid Sequence,
pubmed-meshheading:7615087-Amino Acids,
pubmed-meshheading:7615087-Base Sequence,
pubmed-meshheading:7615087-Cloning, Molecular,
pubmed-meshheading:7615087-Crystallography, X-Ray,
pubmed-meshheading:7615087-DNA Primers,
pubmed-meshheading:7615087-Escherichia coli,
pubmed-meshheading:7615087-Mass Spectrometry,
pubmed-meshheading:7615087-Molecular Sequence Data,
pubmed-meshheading:7615087-Peptide Elongation Factors,
pubmed-meshheading:7615087-Protein Conformation,
pubmed-meshheading:7615087-Recombinant Proteins,
pubmed-meshheading:7615087-Trypsin
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pubmed:year |
1995
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pubmed:articleTitle |
Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli.
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pubmed:affiliation |
Department of Chemistry, Aarhus University, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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