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
PY - 2004/10
Y1 - 2004/10
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 Å, α = β = 90, γ = 120°. The asymmetric unit contains one molecule of LeuRS, with a corresponding crystal volume per protein weight of 3.2 Å3 Da-1 and a solvent content of 60.7%. A data set diffracting to 2.2 Å 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.
AB - 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 Å, α = β = 90, γ = 120°. The asymmetric unit contains one molecule of LeuRS, with a corresponding crystal volume per protein weight of 3.2 Å3 Da-1 and a solvent content of 60.7%. A data set diffracting to 2.2 Å 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.
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U2 - 10.1107/S0907444904020700
DO - 10.1107/S0907444904020700
M3 - Article
C2 - 15388951
AN - SCOPUS:12344299423
SN - 0907-4449
VL - 60
SP - 1916
EP - 1918
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 10
ER -