Literature DB >> 7932734

Crystallization and preliminary diffraction studies of Escherichia coli lysyl-tRNA synthetase (LysU).

S Onesti1, M E Theoclitou, E Pernilla, L Wittung, A D Miller, P Plateau, S Blanquet, P Brick.   

Abstract

Crystals of Escherichia coli lysyl-tRNA synthetase (lysU gene product) have been obtained by vapour diffusion techniques. Three different crystal forms could be grown under similar conditions. The crystals that have been chosen for the structure determination belong to space group C222(1) with cell dimensions a = 144.3 A, b = 257.8 A, c = 182.1 A and contain three monomers in the asymmetric unit. They diffract to at least 2.1 A resolution, but are very sensitive to radiation damage.

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Year:  1994        PMID: 7932734     DOI: 10.1006/jmbi.1994.1635

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


  2 in total

1.  Structure-specific tRNA-binding protein from the extreme thermophile Aquifex aeolicus.

Authors:  A J Morales; M A Swairjo; P Schimmel
Journal:  EMBO J       Date:  1999-06-15       Impact factor: 11.598

2.  Functional asymmetry in the lysyl-tRNA synthetase explored by molecular dynamics, free energy calculations and experiment.

Authors:  Samantha J Hughes; Julian A Tanner; Alison D Hindley; Andrew D Miller; Ian R Gould
Journal:  BMC Struct Biol       Date:  2003-06-04
  2 in total

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