Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(fMet) formyltransferase

Proteins. 1996 May;25(1):139-41. doi: 10.1002/prot.14.

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.

MeSH terms

  • Acyltransferases / chemistry*
  • Acyltransferases / genetics
  • Acyltransferases / isolation & purification
  • Ammonium Sulfate
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Hydroxymethyl and Formyl Transferases*

Substances

  • Hydroxymethyl and Formyl Transferases
  • methionyl-tRNA formyltransferase
  • Acyltransferases
  • Ammonium Sulfate