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4 followed by a 50-minute soaking in the final solution The sequence of the plasmid carrying the gene coding for the repressor used in these studies was verified to be that reported by Betz (75). By all extensive biochemical critena, the protein in these studies behaves exactly like that described (3) In addition, mass spectroscopy indicated that the purified protein was full length
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MMG or methylmercury(II)-β-D-1-thiogalactoside was synthesized by reacting the sodium salt of β-D-1-thiogalactoside (Sigma Chemical Company) with methylmercury(II) chloride in methanol The product was purified by preparative silica thin-layer chromatography. A mimic of o-nitrophenyl-β-D-fucoside (ONPF), methylmercury(II)-β-D-1-thiofucoside, was synthesized in a slightly longer procedure starting with (+) D-fucose (Janseen Chimica) MMG-lac represser crystals were obtained as described for the protein alone. The initial protein solution contained a mixture (1.8 molar ratio) of lac represser and MMG.
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38
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4243184714
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note
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2-terminal and COOH-terminal subdomains were allowed to move independently, but were constrained by the noncrystallographic symmetry as was the intact tetramer. A subset of rotational and all of translational space were explored with a continuous transform to interpolate the rotational component of the molecular scattering, and a genetic algonthm to optimize the correlation of the structure amplitudes. The orientation and position of the model pieces were further refined with a modified version of GA_RB that maximized the peak height in the difference Founers at the heavy atom sites.
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42
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4243177954
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note
-
-4 M DNA) and placement over a reservoir solution containing 29 to 31 percent PEG 3K in 0.05 M potassium phosphate (pH 8.5) and 0.075 M sodium potassium tartrate yielded larger crystals (1 0 mm by 0.5 mm by O 5 mm) suitable for data collection.
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note
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We thank S. L Ginell, L J. Keefe, C. E. Schutt, R. Shigeta Jr., and A. Luptak for technical assistance and D. C Rees and M. J Bennett for discussions, and the Argonne National Laboratory Structural Biology Center and CHESS and MacCHESS for access to synchrotron x-ray facilities. Supported by National Institutes of Health (NIH) grant GM-44617 and an Army Research Office grant DAAL03-92-G-0713, NIH Cell and Molecular Biology training grants (N C H and M A.K ), and NIH Molecular Biophysics training grant 2-T32-GM082745 (G.C). The Argonne National Laboratory Structural Biology Center beamline, X-8-C of the National Synchrotron Light Source, is supported by the Department of Energy, Office of Health and Environmental Research, and by the NIH-NCRR grant P41-RR06017. The Cornell High Energy Synchrotron Source is supported by the National Science Foundation (DMR-9311772). Mac-CHESS is supported by a NIH grant RR-016416. Atomic coordinates have been deposited in the Protein Data Bank with accession numbers 1LBG (lac DNA), 1LBH (lac IPTG), and 1LBI (lac Apo).
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