Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(f)(Met) formyltransferase complexed with formyl-methionyl-tRNA(f)(Met)

Citation
E. Schmitt et al., Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(f)(Met) formyltransferase complexed with formyl-methionyl-tRNA(f)(Met), ACT CRYST D, 55, 1999, pp. 332-334
Citations number
21
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
55
Year of publication
1999
Part
1
Pages
332 - 334
Database
ISI
SICI code
0907-4449(199901)55:<332:CAPXAO>2.0.ZU;2-4
Abstract
The structure of methionyl-tRNA(f)(Met) formyltransferase from E. coli, a m onomeric protein of 34 kDa, has previously been determined at 2.0 Angstrom resolution. In the present work, this enzyme was crystallized as a complex with its macromolecular product, the initiator formyl-methionyl-tRNA(f)(Met ) (25 kDa). Polyethylene glycol 5000 monomethyl-ether was used as a precipi tating agent. The crystals are orthorhombic and have unit-cell parameters a = 201.7, b = 68.1, c = 86.4 Angstrom. They belong to space group P2(1)2(1) 2 and diffract to 2.8 Angstrom resolution. The structure is being solved wi th the help of a mercury derivative.