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Crystallization of leucyl-tRNA synthetase complexed with tRNALeu from the archaeon Pyrococcus horikoshii.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 01; 61(Pt 1):30-2.AC

Abstract

All five tRNALeu isoacceptors from the archaeon Pyrococcus horikoshii have been transcribed in vitro and purified. The leucyl-tRNA synthetase (LeuRS) from P. horikoshii was overexpressed in Escherichia coli and purified, and cocrystallizations with each of the tRNALeu isoacceptors were attempted. Cocrystals were obtained by the hanging-drop vapour-diffusion method, but only when the tRNALeu isoacceptor with the anticodon CAA was used. Electrophoretic analyses revealed that the crystals contain both LeuRS and tRNALeu, suggesting that they are LeuRS-tRNALeu complex crystals. A data set diffracting to 3.3 A resolution was collected from a single crystal at 100 K. The crystal belongs to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 118.18, b = 120.55, c = 231.13 A. The asymmetric unit is expected to contain two complexes of LeuRS-tRNALeu, with a corresponding crystal volume per protein weight of 2.9 A3 Da(-1) and a solvent content of 57.3%.

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Authors+Show Affiliations

Fukunaga R
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
Ishitani R
No affiliation info available
Nureki O
No affiliation info available
Yokoyama S
No affiliation info available

MeSH

Archaeal ProteinsCrystallography, X-RayLeucine-tRNA LigaseMolecular WeightProtein BindingPyrococcus horikoshiiRNA, ArchaealRNA, Transfer, LeuX-Ray Diffraction

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16508082

Citation

Fukunaga, Ryuya, et al. "Crystallization of leucyl-tRNA Synthetase Complexed With tRNALeu From the Archaeon Pyrococcus Horikoshii." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 61, no. Pt 1, 2005, pp. 30-2.
Fukunaga R, Ishitani R, Nureki O, et al. Crystallization of leucyl-tRNA synthetase complexed with tRNALeu from the archaeon Pyrococcus horikoshii. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005;61(Pt 1):30-2.
Fukunaga, R., Ishitani, R., Nureki, O., & Yokoyama, S. (2005). Crystallization of leucyl-tRNA synthetase complexed with tRNALeu from the archaeon Pyrococcus horikoshii. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 61(Pt 1), 30-2.
Fukunaga R, et al. Crystallization of leucyl-tRNA Synthetase Complexed With tRNALeu From the Archaeon Pyrococcus Horikoshii. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt 1):30-2. PubMed PMID: 16508082.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization of leucyl-tRNA synthetase complexed with tRNALeu from the archaeon Pyrococcus horikoshii. AU - Fukunaga,Ryuya, AU - Ishitani,Ryuichiro, AU - Nureki,Osamu, AU - Yokoyama,Shigeyuki, Y1 - 2004/09/25/ PY - 2004/08/26/received PY - 2004/09/06/accepted PY - 2006/3/2/pubmed PY - 2006/5/16/medline PY - 2006/3/2/entrez SP - 30 EP - 2 JF - Acta crystallographica. Section F, Structural biology and crystallization communications JO - Acta Crystallogr Sect F Struct Biol Cryst Commun VL - 61 IS - Pt 1 N2 - All five tRNALeu isoacceptors from the archaeon Pyrococcus horikoshii have been transcribed in vitro and purified. The leucyl-tRNA synthetase (LeuRS) from P. horikoshii was overexpressed in Escherichia coli and purified, and cocrystallizations with each of the tRNALeu isoacceptors were attempted. Cocrystals were obtained by the hanging-drop vapour-diffusion method, but only when the tRNALeu isoacceptor with the anticodon CAA was used. Electrophoretic analyses revealed that the crystals contain both LeuRS and tRNALeu, suggesting that they are LeuRS-tRNALeu complex crystals. A data set diffracting to 3.3 A resolution was collected from a single crystal at 100 K. The crystal belongs to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 118.18, b = 120.55, c = 231.13 A. The asymmetric unit is expected to contain two complexes of LeuRS-tRNALeu, with a corresponding crystal volume per protein weight of 2.9 A3 Da(-1) and a solvent content of 57.3%. SN - 1744-3091 UR - https://www.unboundmedicine.com/medline/citation/16508082/Crystallization_of_leucyl_tRNA_synthetase_complexed_with_tRNALeu_from_the_archaeon_Pyrococcus_horikoshii_ DB - PRIME DP - Unbound Medicine ER -