The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis.
The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis.
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DOI:
10.1107/s090744499701069x
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发表时间:
1998
期刊:
影响因子:
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通讯作者:
A. Gruez;M. Zeghouf;J. Bertrand;M. Eschenbrenner;J. Covès;M. Fontecave;D. Pignol;J. Fontecilla-Camps
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文献类型:
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作者:
A. Gruez;M. Zeghouf;J. Bertrand;M. Eschenbrenner;J. Covès;M. Fontecave;D. Pignol;J. Fontecilla-Camps
The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein subunit was crystallized using the hanging-drop technique, with PEG 4000 as precipitant. The crystals belong to space group P3112 or enantiomorph, with unit-cell parameters a = b = 171.0, c = 152.1 A. A solvent content of 75% was determined by a calibrated tetrachloromethane/toluene gradient which corresponds to three monomers per asymmetric unit. A 3 A resolution native data set was collected at beamline W32 of LURE, Orsay, France.