Literature DB >> 1569573

Crystallization of aspartyl-tRNA synthetase-tRNA(Asp) complex from Escherichia coli and first crystallographic results.

S Eiler1, M Boeglin, F Martin, G Eriani, J Gangloff, J C Thierry, D Moras.   

Abstract

Crystals of the dimeric aspartyl-tRNA synthetase from Escherichia coli (molecular mass 132,000 Da) complexed with its cognate tRNA (molecular mass 25,000 Da) have been grown using ammonium sulfate as precipitant. The crystals belong to the orthorhombic space group C222(1) with unit cell parameters a = 102.75 A, b = 128.11 A, c = 231.70 A and diffract to 3 A. The asymmetric unit contains one monomer of the aspartyl-tRNA synthetase and one tRNA molecule.

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Year:  1992        PMID: 1569573     DOI: 10.1016/0022-2836(92)90478-3

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  3 in total

1.  Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases.

Authors:  Christopher S Francklyn; Eric A First; John J Perona; Ya-Ming Hou
Journal:  Methods       Date:  2008-02       Impact factor: 3.608

2.  Properties of the lysyl-tRNA synthetase gene and product from the extreme thermophile Thermus thermophilus.

Authors:  J Chen; A Brevet; M Lapadat-Tapolsky; S Blanquet; P Plateau
Journal:  J Bacteriol       Date:  1994-05       Impact factor: 3.490

3.  Determination of 2'-hydroxyl and phosphate groups important for aminoacylation of Escherichia coli tRNAAsp: a nucleotide analogue interference study.

Authors:  C S Vörtler; O Fedorova; T Persson; U Kutzke; F Eckstein
Journal:  RNA       Date:  1998-11       Impact factor: 4.942

  3 in total

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