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Crystallization and preliminary crystallographic analysis of Thermus thermophilus leucyl-tRNA synthetase and its complexes with leucine and a non-hydrolysable leucyl-adenylate analogue.
Acta Crystallogr D Biol Crystallogr. 2000 May; 56(Pt 5):667-9.AC

Abstract

Leucyl-tRNA synthetase from Thermus thermophilus (LeuRSTT) is the first LeuRS to be crystallized. Two crystal forms of the native enzyme have been obtained using the hanging-drop vapour-diffusion method with ammonium sulfate as a precipitant. Crystals of the first form belong to space group I422 and have unit-cell parameters a = b = 312.4, c = 100.4 A. They diffract anisotropically to 3.5 A resolution in the c-axis direction and to only 6 A resolution in the perpendicular direction. Crystals of the second form, which can be obtained native or with leucine or a leucyl-adenylate analogue bound, belong to space group C222(1) and have unit-cell parameters a = 102. 4, b = 154.1, c = 174.3 A. They diffract to 1.9 A resolution and contain one monomer in the asymmetric unit. Selenomethionated LeuRSTT has been produced and crystals of the second form suitable for MAD analysis have been grown.

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Authors+Show Affiliations

Yaremchuk A
EMBL, Grenoble Outstation, c/o ILL, 6 Rue Jules Horowitz, F-38042 Grenoble CEDEX 9, France.
Cusack S
No affiliation info available
Gudzera O
No affiliation info available
Grøtli M
No affiliation info available
Tukalo M
No affiliation info available

MeSH

CrystallizationCrystallography, X-RayLeucineLeucine-tRNA LigaseSelenomethionineThermus thermophilus

Pub Type(s)

Journal Article

Language

eng

PubMed ID

10771445

Citation

Yaremchuk, A, et al. "Crystallization and Preliminary Crystallographic Analysis of Thermus Thermophilus leucyl-tRNA Synthetase and Its Complexes With Leucine and a Non-hydrolysable Leucyl-adenylate Analogue." Acta Crystallographica. Section D, Biological Crystallography, vol. 56, no. Pt 5, 2000, pp. 667-9.
Yaremchuk A, Cusack S, Gudzera O, et al. Crystallization and preliminary crystallographic analysis of Thermus thermophilus leucyl-tRNA synthetase and its complexes with leucine and a non-hydrolysable leucyl-adenylate analogue. Acta Crystallogr D Biol Crystallogr. 2000;56(Pt 5):667-9.
Yaremchuk, A., Cusack, S., Gudzera, O., Grøtli, M., & Tukalo, M. (2000). Crystallization and preliminary crystallographic analysis of Thermus thermophilus leucyl-tRNA synthetase and its complexes with leucine and a non-hydrolysable leucyl-adenylate analogue. Acta Crystallographica. Section D, Biological Crystallography, 56(Pt 5), 667-9.
Yaremchuk A, et al. Crystallization and Preliminary Crystallographic Analysis of Thermus Thermophilus leucyl-tRNA Synthetase and Its Complexes With Leucine and a Non-hydrolysable Leucyl-adenylate Analogue. Acta Crystallogr D Biol Crystallogr. 2000;56(Pt 5):667-9. PubMed PMID: 10771445.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary crystallographic analysis of Thermus thermophilus leucyl-tRNA synthetase and its complexes with leucine and a non-hydrolysable leucyl-adenylate analogue. AU - Yaremchuk,A, AU - Cusack,S, AU - Gudzera,O, AU - Grøtli,M, AU - Tukalo,M, PY - 2000/4/20/pubmed PY - 2000/9/2/medline PY - 2000/4/20/entrez SP - 667 EP - 9 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 56 IS - Pt 5 N2 - Leucyl-tRNA synthetase from Thermus thermophilus (LeuRSTT) is the first LeuRS to be crystallized. Two crystal forms of the native enzyme have been obtained using the hanging-drop vapour-diffusion method with ammonium sulfate as a precipitant. Crystals of the first form belong to space group I422 and have unit-cell parameters a = b = 312.4, c = 100.4 A. They diffract anisotropically to 3.5 A resolution in the c-axis direction and to only 6 A resolution in the perpendicular direction. Crystals of the second form, which can be obtained native or with leucine or a leucyl-adenylate analogue bound, belong to space group C222(1) and have unit-cell parameters a = 102. 4, b = 154.1, c = 174.3 A. They diffract to 1.9 A resolution and contain one monomer in the asymmetric unit. Selenomethionated LeuRSTT has been produced and crystals of the second form suitable for MAD analysis have been grown. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/10771445/Crystallization_and_preliminary_crystallographic_analysis_of_Thermus_thermophilus_leucyl_tRNA_synthetase_and_its_complexes_with_leucine_and_a_non_hydrolysable_leucyl_adenylate_analogue_ L2 - http://scripts.iucr.org/cgi-bin/paper?LI0348 DB - PRIME DP - Unbound Medicine ER -