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

Résultats de recherche: Contribution à un journal › Article › Revue par des pairs

10 Citations (Scopus)

Résumé

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.

langue originale	Anglais
Pages (de - à)	139-141
Nombre de pages	3
journal	Proteins: Structure, Function and Genetics
Volume	25
Numéro de publication	1
Les DOIs	https://doi.org/10.1002/prot.14
état	Publié - 1 janv. 1996

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10.1002/prot.14

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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",

month = jan,

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TY - JOUR

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

C2 - 8727328

AN - SCOPUS:0029970052

SN - 0887-3585

VL - 25

SP - 139

EP - 141

JO - Proteins: Structure, Function and Genetics

JF - Proteins: Structure, Function and Genetics

IS - 1

ER -

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

Résumé

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