Crystallisation of the Glycyl-tRNA synthetase from thermus thermophilus and initial crystallographic data
(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
- Logan, Derek T. LU ; Cura, Vincent ; Touzel, Jean-Pierre ; Kern, Daniel and Moras, Dino
- publishing date
- 1994
- 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}}, }