Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(fMet) formyltransferase.
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.
Schmitt
E
E
Laboratorie de Biochimie, Unité de Recherche Associée no. 1970 du Centre National de la Recherche Scientifique, Ecole Polytechnique, Palaiseau, France.
Mechulam
Y
Y
Ruff
M
M
Mitschler
A
A
Moras
D
D
Blanquet
S
S
D000217:Acyltransferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D000645:Ammonium Sulfate; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D019877:Hydroxymethyl and Formyl Transferases
D019877:Hydroxymethyl and Formyl Transferases; C021561:methionyl-tRNA formyltransferase; D000217:Acyltransferases; D000645:Ammonium Sulfate