ABSTRACT Methionyl-tRNA(fMet) formyltransferase from Escherichia coli, a monomer of 34kDa, was ov... more ABSTRACT Methionyl-tRNA(fMet) 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 A, c = 81.8 A. They belong to space group P3(2)21 and diffract to 2.0 A resolution. The structure is being solved by multiple isomorphous replacement.
ABSTRACT The structure of methionyl-tRNAfMet(f) formyltransferase from E. coli, a monomeric prote... more ABSTRACT The structure of methionyl-tRNAfMet(f) formyltransferase from E. coli, a monomeric protein of 34 kDa, has previously been determined at 2.0 A resolution. In the present work, this enzyme was crystallized as a complex with its macromolecular product, the initiator formyl-methionyl-tRNAfMet(f) (25 kDa). Polyethylene glycol 5000 monomethylether was used as a precipitating agent. The crystals are orthorhombic and have unit-cell parameters a = 201.7, b = 68.1, c = 86.4 A. They belong to space group P21212 and diffract to 2.8 A resolution. The structure is being solved with the help of a mercury derivative.
ABSTRACT Methionyl-tRNA(fMet) formyltransferase from Escherichia coli, a monomer of 34kDa, was ov... more ABSTRACT Methionyl-tRNA(fMet) 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 A, c = 81.8 A. They belong to space group P3(2)21 and diffract to 2.0 A resolution. The structure is being solved by multiple isomorphous replacement.
ABSTRACT The structure of methionyl-tRNAfMet(f) formyltransferase from E. coli, a monomeric prote... more ABSTRACT The structure of methionyl-tRNAfMet(f) formyltransferase from E. coli, a monomeric protein of 34 kDa, has previously been determined at 2.0 A resolution. In the present work, this enzyme was crystallized as a complex with its macromolecular product, the initiator formyl-methionyl-tRNAfMet(f) (25 kDa). Polyethylene glycol 5000 monomethylether was used as a precipitating agent. The crystals are orthorhombic and have unit-cell parameters a = 201.7, b = 68.1, c = 86.4 A. They belong to space group P21212 and diffract to 2.8 A resolution. The structure is being solved with the help of a mercury derivative.
Uploads
Papers by Yves Mechulam