Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAMet(f) formyltransferase complexed with formyl-methionyl-tRNAMet(f).

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.