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2-terminus [GrpE(34-197)], was as active as full-length GrpE.
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Purified ATPase domain of DnaK and truncated GrpE were mixed such that there was a twofold excess of DnaK relative to the GrpE dimer. About 40 mg of complex was purified away from the excess DnaK on a Sephacryl S-100 column (2.5 cm by 63 cm) in 25 mM Mopso (pH 6.8), 25 mM NaCl, 5 mM dithiothreitol, and 10 mM (D,L)-methionine. The complex was concentrated to 200 mg/ml. Seleno-methionine-substituted DnaK and GrpE complexes, as well as complexes made with the DnaK cysteine mutants R235C and D289C (R, Arg; C, Cys; D, Asp), were prepared in the same way.
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1842361222
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note
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We thank A. Szabo for the initial clone of the ATPase domain of DnaK, S. Jacques for technical assistance, F. Sicheri and D. Jeruzalmi for help with data collection, A. Bohm for critically reading the manuscript, and H. Nelson, T. Alber, and his group for helpful discussions. The 2.8 Å data set was measured at the Cornell High Energy Synchrotron Source. The coordinates have been deposited in the Brookhaven Protein Data Bank with the accession code 1DKG.
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