Crystallization and preliminary X-ray analysis of cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens.

@article{Boyko2006CrystallizationAP,
  title={Crystallization and preliminary X-ray analysis of cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens.},
  author={Konstantin M. Boyko and Konstantin M Polyakov and Tamara V Tikhonova and Alvira Slutsky and Alexey N. Antipov and R. A. Zvyagilskaya and Gleb P. Bourenkov and Alexandre N Popov and Victor S. Lamzin and Vladimir O. Popov},
  journal={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2006},
  volume={62 Pt 3},
  pages={215-7}
}
A novel cytochrome c nitrite reductase (TvNiR) was isolated from the haloalkalophilic bacterium Thioalkalivibrio nitratireducens. The enzyme catalyses nitrite and hydroxylamine reduction, with ammonia as the only product of both reactions. It consists of 525 amino-acid residues and contains eight haems c. TvNiR crystals were grown by the hanging-drop vapour-diffusion technique. The crystals display cubic symmetry and belong to space group P2(1)3, with unit-cell parameter a = 194 A. A native… CONTINUE READING

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