枯草芽孢杆菌肌醇脱氢酶（IDH）的纯化、结晶及初步X射线分析
Purification, crystallization and preliminary X-ray analysis of inositol dehydrogenase (IDH) from Bacillus subtilis.
作者信息
Van Straaten K E, Hoffort A, Palmer D R J, Sanders D A R
机构信息
Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, Saskatchewan S7N 5C9, Canada.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Feb 1;64(Pt 2):98-101. doi: 10.1107/S1744309108000328. Epub 2008 Jan 31.
Abstract
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 Ni(2+)-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 A resolution from a SeMet-labelled crystal at the Advanced Photon Source (APS) and a MAD data set was collected to 1.75 A 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.
摘要
肌醇脱氢酶（IDH）是一种催化NAD（+）依赖性将肌醇氧化为 scyllo-肌醇酮的酶。该酶已通过Ni（2+）亲和色谱法纯化至同质，并使用微量分批法以天然和硒代甲硫氨酸（SeMet）标记形式结晶。在高级光子源（APS）从SeMet标记的晶体收集了分辨率为2.0 Å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 Å的MAD数据集；这是首次报道来自CLS的异常衍射实验。晶体属于空间群I222，每个不对称单元包含一个分子。
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