Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei

Ryohei Ishii; Osamu Nureki; Tatsuo Yanagisawa; Ryuya Fukunaga; Shigeyuki Yokoyama

doi:10.1107/S1744309106036700

Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei

Ryohei Ishii, Osamu Nureki, Tatsuo Yanagisawa, Ryuya Fukunaga, Shigeyuki Yokoyama

Research output: Contribution to journal › Article › peer-review

30 Scopus citations

Abstract

Pyrrolysyl-tRNA synthetase (PylRS) from Methanosarcina mazei was overexpressed in an N-terminally truncated form PylRS(c270) in Escherichia coli, purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. The native PylRS(c270) crystals in complex with an ATP analogue belonged to space group P6₄, with unit-cell parameters a = b = 104.88, c = 70.43 Å, α = β = 90, γ = 120°, and diffracted to 1.9 Å resolution. The asymmetric unit contains one molecule of PylRS(c270). Selenomethionine- substituted protein crystals were prepared in order to solve the structure by the MAD phasing method.

Original language	English (US)
Pages (from-to)	1031-1033
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	62
Issue number	10
DOIs	https://doi.org/10.1107/S1744309106036700
State	Published - Oct 2006
Externally published	Yes

Keywords

Methanosarcina mazei
Pyrrolysyl-tRNA synthetase

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309106036700

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Ishii, R., Nureki, O., Yanagisawa, T., Fukunaga, R., & Yokoyama, S. (2006). Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(10), 1031-1033. https://doi.org/10.1107/S1744309106036700

Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei. / Ishii, Ryohei; Nureki, Osamu; Yanagisawa, Tatsuo et al.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 62, No. 10, 10.2006, p. 1031-1033.

Research output: Contribution to journal › Article › peer-review

Ishii, R, Nureki, O, Yanagisawa, T, Fukunaga, R & Yokoyama, S 2006, 'Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 62, no. 10, pp. 1031-1033. https://doi.org/10.1107/S1744309106036700

Ishii R, Nureki O, Yanagisawa T, Fukunaga R, Yokoyama S. Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2006 Oct;62(10):1031-1033. doi: 10.1107/S1744309106036700

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abstract = "Pyrrolysyl-tRNA synthetase (PylRS) from Methanosarcina mazei was overexpressed in an N-terminally truncated form PylRS(c270) in Escherichia coli, purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. The native PylRS(c270) crystals in complex with an ATP analogue belonged to space group P64, with unit-cell parameters a = b = 104.88, c = 70.43 {\AA}, α = β = 90, γ = 120°, and diffracted to 1.9 {\AA} resolution. The asymmetric unit contains one molecule of PylRS(c270). Selenomethionine- substituted protein crystals were prepared in order to solve the structure by the MAD phasing method.",

keywords = "Methanosarcina mazei, Pyrrolysyl-tRNA synthetase",

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AU - Fukunaga, Ryuya

AU - Yokoyama, Shigeyuki

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AB - Pyrrolysyl-tRNA synthetase (PylRS) from Methanosarcina mazei was overexpressed in an N-terminally truncated form PylRS(c270) in Escherichia coli, purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. The native PylRS(c270) crystals in complex with an ATP analogue belonged to space group P64, with unit-cell parameters a = b = 104.88, c = 70.43 Å, α = β = 90, γ = 120°, and diffracted to 1.9 Å resolution. The asymmetric unit contains one molecule of PylRS(c270). Selenomethionine- substituted protein crystals were prepared in order to solve the structure by the MAD phasing method.

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Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei

Abstract

Keywords

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