Purification, crystallization and preliminary X-ray analysis of inositol dehydrogenase (IDH) from Bacillus subtilis.
Purification, crystallization and preliminary X-ray analysis of inositol dehydrogenase (IDH) from Bacillus subtilis.
复制标题
枯草芽孢杆菌肌醇脱氢酶 (IDH) 的纯化、结晶和初步 X 射线分析。
DOI：
10.1107/s1744309108000328
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发表时间：
2008
期刊：
影响因子：
--
通讯作者：
Sanders,DAR
中科院分区：
文献类型：
--
作者：
VanStraaten,KE;Hoffort,A;Palmer,DRJ;Sanders,DAR
肌醇脱氢酶(IDH)是一种催化依赖NAD+的肌醇氧化生成肌糖的酶。用Ni2+亲和层析纯化了该酶，并用微批法将其结晶为天然形式和硒蛋氨酸(SeMet)标记形式。在高级光子源(APS)从标记有SMET的晶体上收集了分辨率为2.0 ？的SAD X射线衍射数据，并在加拿大光源(CLS)收集了分辨率为1.75 ？的MAD数据集；这是首次报道的来自CLS的异常衍射实验。晶体属于空间群I222，每个不对称单元含有一个分子。
Inositol dehydrogenase (IDH) is an enzyme that catalyses the NAD+-dependent oxidation of myo-inositol to scyllo-inosose. The enzyme has been purified to homogeneity by means of Ni2+-affinity chromatography and was crystallized in both native and selenomethionine (SeMet) labelled forms using the microbatch method. SAD X-ray diffraction data were collected to 2.0 Å resolution from a SeMet-labelled crystal at the Advanced Photon Source (APS) and a MAD data set was collected to 1.75 Å resolution at the Canadian Light Source (CLS); this is the first reported anomalous diffraction experiment from the CLS. The crystals belong to space group I222 and contain one molecule per asymmetric unit.