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.

[1]  J. Covès,et al.  NADPH‐sulfite reductase flavoprotein from Escherichia coli: Contribution to the flavin content and subunit interaction , 1995, FEBS letters.

[2]  E. Getzoff,et al.  Sulfite Reductase Structure at 1.6 Å: Evolution and Catalysis for Reduction of Inorganic Anions , 1995, Science.

[3]  Marc Fontecave,et al.  The Flavin Reductase Activity of the Flavoprotein Component of Sulfite Reductase from Escherichia coli , 1995, The Journal of Biological Chemistry.

[4]  J. Navaza,et al.  AMoRe: an automated package for molecular replacement , 1994 .

[5]  C. C. Correll,et al.  Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. , 1992, Science.

[6]  Sung-Hou Kim,et al.  Sparse matrix sampling: a screening method for crystallization of proteins , 1991 .

[7]  P. Karplus,et al.  Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family. , 1991, Science.

[8]  D. Rueger,et al.  Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase. , 1989, The Journal of biological chemistry.

[9]  C. Carter.  Protein crystallization using incomplete factorial experiments. , 1979, The Journal of biological chemistry.

[10]  H. Kamin,et al.  Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow. , 1974, The Journal of biological chemistry.

[11]  N. M. Kredich.  Regulation of L-cysteine biosynthesis in Salmonella typhimurium. I. Effects of growth of varying sulfur sources and O-acetyl-L-serine on gene expression. , 1971, The Journal of biological chemistry.

[12]  B. Matthews.  Solvent content of protein crystals. , 1968, Journal of molecular biology.