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Crystallization and preliminary X‐ray analysis of Escherichia coli methionyl–tRNA f Met formyltransferase
Author(s) -
Schmitt Emmanuelle,
Mechulam Yves,
Ruff Marc,
Mitschler Andre,
Moras Dino,
Blanquet Sylvain
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199605)25:1<139::aid-prot14>3.0.co;2-l
Subject(s) - escherichia coli , transfer rna , crystallization , resolution (logic) , monomer , microbiology and biotechnology , biology , chemistry , gene , crystallography , stereochemistry , biochemistry , rna , organic chemistry , artificial intelligence , computer science , polymer
Methionyl–tRNA f Metformyltransferase 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 P3 2 21 and diffract to 2.0Å resolution. The structure is being solved by multiple isomorphous replacement. © 1996 Wiley‐Liss, Inc.