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Crystallization and crystal packing of Proteus mirabilis PR catalase
H M Jouve1, P Gouet, N Boudjada
1Laboratoire de Biologie Structurale, CEA et URA 1333 CNRS, Grenoble, France.
Journal of Molecular Biology
|October 20, 1991
Abstract:
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.