TY - JOUR
T1 - Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAfMet formyltransferase
AU - Schmitt, Emmanuelle
AU - Mechulam, Yves
AU - Ruff, Marc
AU - Mitschler, Andre
AU - Moras, Dino
AU - Blanquet, Sylvain
PY - 1996/1/1
Y1 - 1996/1/1
N2 - Methionyl-tRNAfMet 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.
AB - Methionyl-tRNAfMet 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.
KW - Crystallization
KW - Methionyl-tRNA formyltransferase
KW - X-ray structure
U2 - 10.1002/prot.14
DO - 10.1002/prot.14
M3 - Article
C2 - 8727328
AN - SCOPUS:0029970052
SN - 0887-3585
VL - 25
SP - 139
EP - 141
JO - Proteins: Structure, Function and Genetics
JF - Proteins: Structure, Function and Genetics
IS - 1
ER -