Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(f)(Met) formyltransferase complexed with formyl-methionyl-tRNA(f)(Met)
E. Schmitt et al., Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(f)(Met) formyltransferase complexed with formyl-methionyl-tRNA(f)(Met), ACT CRYST D, 55, 1999, pp. 332-334
The structure of methionyl-tRNA(f)(Met) formyltransferase from E. coli, a m
onomeric protein of 34 kDa, has previously been determined at 2.0 Angstrom
resolution. In the present work, this enzyme was crystallized as a complex
with its macromolecular product, the initiator formyl-methionyl-tRNA(f)(Met
) (25 kDa). Polyethylene glycol 5000 monomethyl-ether was used as a precipi
tating agent. The crystals are orthorhombic and have unit-cell parameters a
= 201.7, b = 68.1, c = 86.4 Angstrom. They belong to space group P2(1)2(1)
2 and diffract to 2.8 Angstrom resolution. The structure is being solved wi
th the help of a mercury derivative.