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

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

Access to Document

10.1107/S1744309106036700

Cite this

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; Fukunaga, Ryuya; Yokoyama, Shigeyuki.

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. https://doi.org/10.1107/S1744309106036700

Ishii, Ryohei ; Nureki, Osamu ; Yanagisawa, Tatsuo ; Fukunaga, Ryuya ; Yokoyama, Shigeyuki. / Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2006 ; Vol. 62, No. 10. pp. 1031-1033.

@article{60a09e573e444c44bf9853f646a3ad5f,

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

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",

author = "Ryohei Ishii and Osamu Nureki and Tatsuo Yanagisawa and Ryuya Fukunaga and Shigeyuki Yokoyama",

year = "2006",

month = oct,

doi = "10.1107/S1744309106036700",

language = "English (US)",

volume = "62",

pages = "1031--1033",

journal = "Acta Crystallographica Section F:Structural Biology Communications",

issn = "1744-3091",

publisher = "John Wiley and Sons Ltd",

number = "10",

}

TY - JOUR

T1 - Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei

AU - Ishii, Ryohei

AU - Nureki, Osamu

AU - Yanagisawa, Tatsuo

AU - Fukunaga, Ryuya

AU - Yokoyama, Shigeyuki

PY - 2006/10

Y1 - 2006/10

N2 - 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.

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.

KW - Methanosarcina mazei

KW - Pyrrolysyl-tRNA synthetase

UR - http://www.scopus.com/inward/record.url?scp=33749524376&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33749524376&partnerID=8YFLogxK

U2 - 10.1107/S1744309106036700

DO - 10.1107/S1744309106036700

M3 - Article

C2 - 17012805

AN - SCOPUS:33749524376

VL - 62

SP - 1031

EP - 1033

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 10

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this