The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis

Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):135-6. doi: 10.1107/s090744499701069x.

Abstract

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.

Publication types

  • Comparative Study

MeSH terms

  • Bacterial Proteins / chemistry*
  • Catalytic Domain
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins*
  • Flavoproteins / chemistry*
  • Iron-Sulfur Proteins / chemistry*
  • Oxidoreductases Acting on Sulfur Group Donors / chemistry*
  • Sulfite Reductase (NADPH)

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • FNR protein, E coli
  • Flavoproteins
  • Iron-Sulfur Proteins
  • Oxidoreductases Acting on Sulfur Group Donors
  • Sulfite Reductase (NADPH)
  • sulfite reductase (NADPH), E coli