Crystallization and crystal packing of Proteus mirabilis PR catalase.
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.
Laboratoire de Biologie Structurale, CEA et URA 1333 CNRS, Grenoble, France.
H M
HM
Jouve
P
P
Gouet
N
N
Boudjada
G
G
Buisson
R
R
Kahn
E
E
Duee
D002374:Catalase / Q000737:chemistry*; D003460:Crystallization; D046911:Macromolecular Substances; D009249:NADP / Q000737:chemistry; D011513:Proteus mirabilis / Q000737:chemistry / Q000201:enzymology*; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D009249:NADP; D002374:Catalase