Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAfMet formyltransferase

Emmanuelle Schmitt; Yves Mechulam; Marc Ruff; Andre Mitschler; Dino Moras; Sylvain Blanquet

doi:10.1002/prot.14

Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA_f^Met formyltransferase

Emmanuelle Schmitt
, Yves Mechulam
, Marc Ruff
, Andre Mitschler
, Dino Moras
, Sylvain Blanquet

U. Propre Rech. Biol. Struct. N.
Institut de Génétique et de Biologie Moléculaire et Cellulaire
Institut Polytechnique de Paris

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

10 Citations (Scopus)

Abstract

Methionyl-tRNA_f^Met formyltransferase from Escherichia coli, a monomer of 34kDa, was overexpressed from its cloned gene fmt (Guillon, J.M., Mechulam, Y., Schmitter, J.M., Blanquet, S., and Fayat, G., J. Bacteriol. 174:4294-4301, 1992) and crystallized using ammonium sulphate as precipitant. The crystals are trigonal and have unit cell parameters a=b=151.0Å, c=81.8Å. They belong to space group P3₂21 and diffract to 2.0Å resolution. The structure is being solved by multiple isomorphous replacement.

Original language	English
Pages (from-to)	139-141
Number of pages	3
Journal	Proteins: Structure, Function and Genetics
Volume	25
Issue number	1
DOIs	https://doi.org/10.1002/prot.14
Publication status	Published - 1 Jan 1996

Keywords

Crystallization
Methionyl-tRNA formyltransferase
X-ray structure

Access to Document

10.1002/prot.14

Cite this

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title = "Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAfMet formyltransferase",

abstract = "Methionyl-tRNAfMet formyltransferase from Escherichia coli, a monomer of 34kDa, was overexpressed from its cloned gene fmt (Guillon, J.M., Mechulam, Y., Schmitter, J.M., Blanquet, S., and Fayat, G., J. Bacteriol. 174:4294-4301, 1992) and crystallized using ammonium sulphate as precipitant. The crystals are trigonal and have unit cell parameters a=b=151.0{\AA}, c=81.8{\AA}. They belong to space group P3221 and diffract to 2.0{\AA} resolution. The structure is being solved by multiple isomorphous replacement.",

keywords = "Crystallization, Methionyl-tRNA formyltransferase, X-ray structure",

author = "Emmanuelle Schmitt and Yves Mechulam and Marc Ruff and Andre Mitschler and Dino Moras and Sylvain Blanquet",

year = "1996",

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T1 - Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAfMet formyltransferase

AU - Schmitt, Emmanuelle

AU - Mechulam, Yves

AU - Ruff, Marc

AU - Mitschler, Andre

AU - Moras, Dino

AU - Blanquet, Sylvain

PY - 1996/1/1

Y1 - 1996/1/1

N2 - Methionyl-tRNAfMet formyltransferase from Escherichia coli, a monomer of 34kDa, was overexpressed from its cloned gene fmt (Guillon, J.M., Mechulam, Y., Schmitter, J.M., Blanquet, S., and Fayat, G., J. Bacteriol. 174:4294-4301, 1992) and crystallized using ammonium sulphate as precipitant. The crystals are trigonal and have unit cell parameters a=b=151.0Å, c=81.8Å. They belong to space group P3221 and diffract to 2.0Å resolution. The structure is being solved by multiple isomorphous replacement.

AB - Methionyl-tRNAfMet formyltransferase from Escherichia coli, a monomer of 34kDa, was overexpressed from its cloned gene fmt (Guillon, J.M., Mechulam, Y., Schmitter, J.M., Blanquet, S., and Fayat, G., J. Bacteriol. 174:4294-4301, 1992) and crystallized using ammonium sulphate as precipitant. The crystals are trigonal and have unit cell parameters a=b=151.0Å, c=81.8Å. They belong to space group P3221 and diffract to 2.0Å resolution. The structure is being solved by multiple isomorphous replacement.

KW - Crystallization

KW - Methionyl-tRNA formyltransferase

KW - X-ray structure

U2 - 10.1002/prot.14

DO - 10.1002/prot.14

M3 - Article

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SN - 0887-3585

VL - 25

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JO - Proteins: Structure, Function and Genetics

JF - Proteins: Structure, Function and Genetics

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