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rdf:type
lifeskim:mentions
pubmed:issue
Pt 1
pubmed:dateCreated
2004-8-9
pubmed:abstractText
Overexpressed dimeric E. coli aspartyl-tRNA synthetase (AspRS) has been crystallized in its free state and complexed with yeast tRNA(Asp). Triclinic crystals of the enzyme alone (a = 104.4, b = 107.4, c = 135.0 A, alpha = 102.9, beta = 101.0, gamma = 106.3 degrees ), have been grown using ammonium sulfate as the precipitant and monoclinic crystals (a = 127.1, b = 163.6, c = 140.1 A, beta = 111.7 degrees ), space group C2, have been grown using polyethylene glycol 6000. They diffract to 2.8 and 3.0 A, respectively. Crystals of the heterologous complex between E. coli AspRS and yeast tRNA have been obtained using ammonium sulfate as the precipitant and 2-propanol as the nucleation agent. They belong to the monoclinic space group P2(1) (a = 76.2, b = 227.3, c = 82.3 A, beta = 111.7 degrees ) and diffract to 2.7 A.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Jan
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
52
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
211-4
pubmed:dateRevised
2007-7-24
pubmed:year
1996
pubmed:articleTitle
Crystallization of Escherichia coli aspartyl-tRNA synthetase in its free state and in a complex with yeast tRNA(Asp).
pubmed:affiliation
UPR 9004 de Biologie Structurale, IGBMC, CNRS/INSERM/ULP, Illkirch, France.
pubmed:publicationType
Journal Article