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Crystallization and preliminary X-ray crystallographic study of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii.
Acta Crystallogr D Biol Crystallogr. 2004 Oct; 60(Pt 10):1916-8.AC

Abstract

The leucyl-tRNA synthetase (LeuRS) from the archaeon Pyrococcus horikoshii was overexpressed in a C-terminally truncated form in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belong to the rhombohedral space group R3, with unit-cell parameters a = b = 186.20, c = 91.43 A, alpha = beta = 90, gamma = 120 degrees. The asymmetric unit contains one molecule of LeuRS, with a corresponding crystal volume per protein weight of 3.2 A3 Da(-1) and a solvent content of 60.7%. A data set diffracting to 2.2 A resolution was collected from a single crystal at 100 K. Selenomethionine-substituted protein crystals were prepared in order to solve the structure by the SAD phasing method.

Authors+Show Affiliations

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

MeSH

Crystallography, X-RayEscherichia coliLeucine-tRNA LigasePyrococcus horikoshiiSelenomethionineTemperature

Pub Type(s)

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

Language

eng

PubMed ID

15388951

Citation

Fukunaga, Ryuya, and Shigeyuki Yokoyama. "Crystallization and Preliminary X-ray Crystallographic Study of leucyl-tRNA Synthetase From the Archaeon Pyrococcus Horikoshii." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 10, 2004, pp. 1916-8.
Fukunaga R, Yokoyama S. Crystallization and preliminary X-ray crystallographic study of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 10):1916-8.
Fukunaga, R., & Yokoyama, S. (2004). Crystallization and preliminary X-ray crystallographic study of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 10), 1916-8.
Fukunaga R, Yokoyama S. Crystallization and Preliminary X-ray Crystallographic Study of leucyl-tRNA Synthetase From the Archaeon Pyrococcus Horikoshii. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 10):1916-8. PubMed PMID: 15388951.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic study of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii. AU - Fukunaga,Ryuya, AU - Yokoyama,Shigeyuki, Y1 - 2004/09/23/ PY - 2004/07/12/received PY - 2004/08/20/accepted PY - 2004/9/25/pubmed PY - 2005/3/30/medline PY - 2004/9/25/entrez SP - 1916 EP - 8 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 10 N2 - The leucyl-tRNA synthetase (LeuRS) from the archaeon Pyrococcus horikoshii was overexpressed in a C-terminally truncated form in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belong to the rhombohedral space group R3, with unit-cell parameters a = b = 186.20, c = 91.43 A, alpha = beta = 90, gamma = 120 degrees. The asymmetric unit contains one molecule of LeuRS, with a corresponding crystal volume per protein weight of 3.2 A3 Da(-1) and a solvent content of 60.7%. A data set diffracting to 2.2 A resolution was collected from a single crystal at 100 K. Selenomethionine-substituted protein crystals were prepared in order to solve the structure by the SAD phasing method. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15388951/Crystallization_and_preliminary_X_ray_crystallographic_study_of_leucyl_tRNA_synthetase_from_the_archaeon_Pyrococcus_horikoshii_ DB - PRIME DP - Unbound Medicine ER -