Article

Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase from Nitrosomonas europaea.

University of Minnesota, Minneapolis, USA.
Acta Crystallographica Section F Structural Biology and Crystallization Communications (impact factor: 0.51). 12/2009; 65(Pt 12):1296-8. DOI:10.1107/S1744309109046119
Source: PubMed

ABSTRACT Hydroxylamine oxidoreductase (HAO) from Nitrosomonas europaea is a homotrimeric protein that catalyzes the oxidation of hydroxylamine to nitrite. Each monomer, with a molecular weight of 67.1 kDa, contains seven c-type hemes and one heme P460, the porphyrin ring of which is covalently linked to a tyrosine residue from an adjacent subunit. HAO was first crystallized and structurally characterized at a resolution of 2.8 A in 1997. The structure was solved in space group P6(3) and suffered from merohedral twinning. Here, a crystallization procedure is presented that yielded untwinned crystals belonging to space group P2(1)2(1)2, which diffracted to 2.25 A resolution and contained one trimer in the asymmetric unit. The unit-cell parameters were a = 140.7, b = 142.6, c = 107.4 A.

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Keywords

adjacent subunit
 
asymmetric unit
 
c-type hemes
 
homotrimeric protein
 
Hydroxylamine oxidoreductase
 
merohedral twinning
 
nitrite
 
Nitrosomonas europaea
 
tyrosine residue
 
unit-cell parameters
 
yielded untwinned crystals
 

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