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Crystallisation of the Glycyl-tRNA synthetase from thermus thermophilus and initial crystallographic data

Logan, Derek T. LU orcid ; Cura, Vincent ; Touzel, Jean-Pierre ; Kern, Daniel and Moras, Dino (1994) In Journal of Molecular Biology 241(5). p.732-735
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°C and crystals are subsequently transferred to 15°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, P212121 and C2,2,21, both with the same cell a = 125 AÅ, b = 254 AÅ, c = 104 AÅ. Crystal packing in... (More)

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°C and crystals are subsequently transferred to 15°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, P212121 and C2,2,21, both with the same cell a = 125 AÅ, b = 254 AÅ, c = 104 AÅ. Crystal packing in P212121 is strongly C-centred. The crystals have V(M) = 3.6 AÅ3/Da and a solvent content of 61%, with one dimer in the asymmetric unit in C2,2,21 and two dimers in P212121. The best native data extend to 2.9 AÅ in C2,2,21 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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author
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publishing date
type
Contribution to journal
publication status
published
subject
keywords
Glycyl-tRNA synthetase, Protein crystallisation, Pseudo-symmetry, Three-dimensional structure
in
Journal of Molecular Biology
volume
241
issue
5
pages
4 pages
publisher
Elsevier
external identifiers
  • scopus:0028169619
ISSN
0022-2836
DOI
10.1006/jmbi.1994.1547
language
English
LU publication?
no
id
7e141e98-048a-406f-806b-5f2711bf55ae
date added to LUP
2022-04-25 11:33:18
date last changed
2022-04-27 10:46:20
@article{7e141e98-048a-406f-806b-5f2711bf55ae,
  abstract     = {{<p>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°C and crystals are subsequently transferred to 15°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<sub>1</sub>2<sub>1</sub>2<sub>1</sub> and C2,2,2<sub>1</sub>, both with the same cell a = 125 AÅ, b = 254 AÅ, c = 104 AÅ. Crystal packing in P2<sub>1</sub>2<sub>1</sub>2<sub>1</sub> is strongly C-centred. The crystals have V(M) = 3.6 AÅ<sup>3</sup>/Da and a solvent content of 61%, with one dimer in the asymmetric unit in C2,2,2<sub>1</sub> and two dimers in P2<sub>1</sub>2<sub>1</sub>2<sub>1</sub>. The best native data extend to 2.9 AÅ in C2,2,2<sub>1</sub> 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.</p>}},
  author       = {{Logan, Derek T. and Cura, Vincent and Touzel, Jean-Pierre and Kern, Daniel and Moras, Dino}},
  issn         = {{0022-2836}},
  keywords     = {{Glycyl-tRNA synthetase; Protein crystallisation; Pseudo-symmetry; Three-dimensional structure}},
  language     = {{eng}},
  number       = {{5}},
  pages        = {{732--735}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Molecular Biology}},
  title        = {{Crystallisation of the Glycyl-tRNA synthetase from <i>thermus thermophilus</i> and initial crystallographic data}},
  url          = {{http://dx.doi.org/10.1006/jmbi.1994.1547}},
  doi          = {{10.1006/jmbi.1994.1547}},
  volume       = {{241}},
  year         = {{1994}},
}