Article Dans Une Revue Journal of Molecular Biology Année : 1991

Crystallization and crystal packing of Proteus mirabilis PR catalase.

Résumé

The tetrameric catalase from Proteus mirabilis PR (EC 1.11.1.6), known to bind NADPH, has been crystallized by the hanging-drop method in a form apparently depleted in dinucleotide. The crystals belong to the hexagonal space group P6(2)22 with a = b = 111.7 A, c = 248.8 A. There is one subunit in the asymmetric unit. Data were collected to 2.9 A at the L.U.R.E. (Orsay) synchrotron radiation facility. The tetramers have been located in the crystal, centered on the site (1/2, 0, 0) with 222 symmetry.The tetrameric catalase from Proteus mirabilis PR (EC 1.11.1.6), known to bind NADPH, has been crystallized by the hanging-drop method in a form apparently depleted in dinucleotide. The crystals belong to the hexagonal space group P6(2)22 with a = b = 111.7 A, c = 248.8 A. There is one subunit in the asymmetric unit. Data were collected to 2.9 A at the L.U.R.E. (Orsay) synchrotron radiation facility. The tetramers have been located in the crystal, centered on the site (1/2, 0, 0) with 222 symmetry.

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Dates et versions

hal-00314301 , version 1 (27-08-2008)

Identifiants

  • HAL Id : hal-00314301 , version 1
  • PUBMED : 1942042

Citer

Hm Jouve, P. Gouet, N. Boudjada, G. Buisson, R. Kahn, et al.. Crystallization and crystal packing of Proteus mirabilis PR catalase.. Journal of Molecular Biology, 1991, 221, pp.1075-1077. ⟨hal-00314301⟩
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