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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Konstantin M BoykoV O Popov

Abstract

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 data set was obtained to 1.5 A resolution. The structure was solved by the SAD technique using the data collected at the Fe absorption peak wavelength.

References

May 20, 1999·Nature Structural Biology·A PerrakisV S Lamzin
May 29, 1999·Current Opinion in Chemical Biology·D J Richardson, N J Watmough
Aug 10, 1999·Nature·O EinsleP M Kroneck
Aug 8, 2002·FEMS Microbiology Reviews·Jörg Simon
Sep 28, 2002·Acta Crystallographica. Section D, Biological Crystallography·Thomas R Schneider, George M Sheldrick
Dec 6, 2003·International Journal of Systematic and Evolutionary Microbiology·Dimitry Yu SorokinJ Gijs Kuenen

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Citations

Apr 6, 2013·Biochimica Et Biophysica Acta·Kathryn D BewleySean J Elliott
Jan 28, 2012·Acta Crystallographica. Section D, Biological Crystallography·Anton A TrofimovVladimir O Popov
Dec 21, 2012·Journal of Synchrotron Radiation·Ricardo Miguel Ferraz LealAlexander N Popov

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