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Crystallization and preliminary X-ray analysis of Escherichia coli methionyl–tRNA formyltransferase
Authors:Emmanuelle Schmitt  Yves Mechulam  Marc Ruff  Andre Mitschler  Dino Moras  Sylvain Blanquet
Abstract:Methionyl–tRNAurn:x-wiley:08873585:media:PROT14:tex2gif-stack-3 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 = 151.0Å, c = 81.8Å. They belong to space group P3221 and diffract to 2.0Å resolution. The structure is being solved by multiple isomorphous replacement. © 1996 Wiley-Liss, Inc.
Keywords:crystallization  X-ray structure  methionyl-tRNA  formyltransferase
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