PMID:8727328
| Citation |
Schmitt, E, Mechulam, Y, Ruff, M, Mitschler, A, Moras, D and Blanquet, S (1996) Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(fMet) formyltransferase. Proteins 25:139-41 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1002/prot.14 |
| Keywords |
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 |
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