Literature DB >> 15299749

Crystallization of Escherichia coli aspartyl-tRNA synthetase in its free state and in a complex with yeast tRNA(Asp).

M Boeglin1, A C Dock-Brégeon, G Eriani, J Gangloff, M Ruff, A Poterszman, J C Thierry, D Moras.   

Abstract

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.

Entities:  

Year:  1996        PMID: 15299749     DOI: 10.1107/S090744499500727X

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.

Authors:  L Moulinier; S Eiler; G Eriani; J Gangloff; J C Thierry; K Gabriel; W H McClain; D Moras
Journal:  EMBO J       Date:  2001-09-17       Impact factor: 11.598

2.  Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant.

Authors:  F Martin; G J Sharples; R G Lloyd; S Eiler; D Moras; J Gangloff; G Eriani
Journal:  J Bacteriol       Date:  1997-06       Impact factor: 3.490

  2 in total

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