| Literature DB >> 16511304 |
K M Boyko1, K M Polyakov, T V Tikhonova, A Slutsky, A N Antipov, R A Zvyagilskaya, G P Bourenkov, A N Popov, V S Lamzin, V 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.Entities:
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Year: 2006 PMID： 16511304 PMCID： PMC2197178 DOI： 10.1107/S174430910600296X
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091