Literature DB >> 8071996

Crystallisation of the glycyl-tRNA synthetase from Thermus thermophilus and initial crystallographic data.

D T Logan1, V Cura, J P Touzel, D Kern, D Moras.   

Abstract

The glycyl-tRNA synthetase from Thermus thermophilus is a dimer of molecular mass 115 kDa, which has been crystallised using the vapour diffusion method from 5 to 7% polyethylene glycol 6000, 0.8 to 1.4 M NaCl at protein concentrations of 2 to 8 mg/ml. Nucleation is carried out at 4 degrees C and crystals are subsequently transferred to 15 degrees C to maximise growth. Crystals are truncated rhombohedra measuring on average 0.4 mm x 0.4 mm x 0.2 mm, which appear within a few days and reach full size in one to two months. GlyRS crystallises in two closely related space groups, P2(1)2(1)2(1) and C2,2,2(1), both with the same cell a = 125 A, b = 254 A, c = 104 A. Crystal packing in P2(1)2(1)2(1) is strongly C-centred. The crystals have VM = 3.6 A3/Da and a solvent content of 61%, with one dimer in the asymmetric unit in C2,2,2(1) and two dimers in P2(1)2(1)2(1). The best native data extend to 2.9 A in C2,2,2(1) and are 90.6% complete with an R-factor between symmetry-related reflections of 10.0%. The structure has been solved by multiple isomorphous replacement and model building is in progress.

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Year:  1994        PMID: 8071996     DOI: 10.1006/jmbi.1994.1547

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


  3 in total

1.  Reconstitution of translation from Thermus thermophilus reveals a minimal set of components sufficient for protein synthesis at high temperatures and functional conservation of modern and ancient translation components.

Authors:  Ying Zhou; Haruichi Asahara; Eric A Gaucher; Shaorong Chong
Journal:  Nucleic Acids Res       Date:  2012-06-20       Impact factor: 16.971

2.  Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus.

Authors:  D T Logan; M H Mazauric; D Kern; D Moras
Journal:  EMBO J       Date:  1995-09-01       Impact factor: 11.598

3.  The structure of Rpf2-Rrs1 explains its role in ribosome biogenesis.

Authors:  Satyavati Kharde; Fabiola R Calviño; Andrea Gumiero; Klemens Wild; Irmgard Sinning
Journal:  Nucleic Acids Res       Date:  2015-06-27       Impact factor: 16.971

  3 in total

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