Crystallization and preliminary X-ray analysis of cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens
Crystallization and preliminary X-ray analysis of cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens
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DOI：
10.1107/s174430910600296x
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发表时间：
2006-03-01
影响因子：
0.9
通讯作者：
Popov, VO
中科院分区：
文献类型：
--
作者：
Boyko, KM;Polyakov, KM;Popov, VO
从嗜盐碱细菌硝基还原硫碱弧菌中分离出一种新型细胞色素 C 亚硝酸还原酶 (TvNiR)。该酶催化亚硝酸盐和羟胺还原，氨是这两个反应的唯一产物。它由 525 个氨基酸残基组成，含有 8 个血红素 c． TvNiR 晶体是通过悬滴蒸气扩散技术生长的。该晶体具有立方对称性，属于P2(1)3空间群，晶胞参数a=194埃。获得了分辨率为 1.5 埃的原始数据集。使用在 Fe 吸收峰值波长处收集的数据，通过 SAD 技术解析该结构。
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 unitcell parameter a = 194 angstrom. A native data set was obtained to 1.5 angstrom resolution. The structure was solved by the SAD technique using the data collected at the Fe absorption peak wavelength.