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 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.
Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale J. P. Ebel, CEA-CNRS, 41 avenue de Martyrs, 38027 Grenoble CEDEX 1, France.
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Gruez
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Zeghouf
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Bertrand
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Eschenbrenner
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Covès
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Fontecave
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Pignol
J C
JC
Fontecilla-Camps
D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D005420:Flavoproteins / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000737:chemistry*; D050864:Sulfite Reductase (NADPH)
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C060704:FNR protein, E coli; D005420:Flavoproteins; D007506:Iron-Sulfur Proteins; D050862:Oxidoreductases Acting on Sulfur Group Donors; D050864:Sulfite Reductase (NADPH); C494314:sulfite reductase (NADPH), E coli