PMID:10089442

Citation	Schmitt, E, Blanquet, S and Mechulam, Y (1999) Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAMet(f) formyltransferase complexed with formyl-methionyl-tRNAMet(f). Acta Crystallogr. D Biol. Crystallogr. 55:332-4
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.
Links	PubMed Online version:10.1107/S0907444998011780
Keywords	Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Hydroxymethyl and Formyl Transferases/chemistry; Hydroxymethyl and Formyl Transferases/isolation & purification; Macromolecular Substances; RNA, Transfer, Met/chemistry; RNA, Transfer, Met/isolation & purification
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