Crystallization and preliminary X-ray crystallographic study of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii

Ryuya Fukunaga, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

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 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.

Original languageEnglish (US)
Pages (from-to)1916-1918
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number10
DOIs
StatePublished - Oct 1 2004
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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