Preliminary crystallographic analysis of the oxidized form of a two mono-nuclear iron centres protein from Desulfovibrio desulfuricans ATCC 27774

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Abstract

Crystals of the fully oxidized form of desulfoferrodoxin were obtained by vapor diffusion from a solution containing 20% PEG 4000, 0.1 M HEPES buffer, pH 7.5, and 0.2 M CaCl2. Trigonal and/or rectangular prisms could be obtained, depending on the temperature used for the crystal growth. Trigonal prisms belong to the rhombohedral space group R32, with a = 112.5 Å and c = 63.2 Å; rectangular prisms belong to the monoclinic space group C2, with a = 77.7 Å, b = 80.9 Å, c = 53.9 Å, and β =98.1°. The crystallographic asymmetric unit of the rhombohedral crystal form contains one molecule. There are two molecules in the asymmetric unit of the monoclinic form, in agreement with the self-rotation function.

Original languageEnglish
Pages (from-to)1189-1191
Number of pages3
JournalProtein Science
Volume5
Issue number6
Publication statusPublished - 1 Jun 1996

Keywords

  • Crystallization
  • Desulfoferrodoxin
  • Non-heme iron proteins
  • Sulfate reducing bacteria
  • X-ray diffraction

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