首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Production crystallization and preliminary X-ray analysis of CTP:inositol-1-phosphate cytidylyltransferase from Archaeoglobus fulgidus
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Production crystallization and preliminary X-ray analysis of CTP:inositol-1-phosphate cytidylyltransferase from Archaeoglobus fulgidus

机译:细足古细菌CTP:肌醇-1-磷酸胞苷转移酶的生产结晶和初步X射线分析

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摘要

Archaeoglobus fulgidus, a hyperthermophilic archaeon, accumulates di-myo-inositol phosphate (DIP) in response to heat stress. Recently, the pathway for biosynthesis of DIP has been elucidated in this organism and involves a bifunctional enzyme that contains two domains: CTP:inositol-1-phosphate cytidylyltransferase (IPCT) as a soluble domain and di-myo-inositol-1,3′-phosphate-1-phosphate synthase (DIPPS) as a membrane domain. Here, the expression, purification, crystallization and preliminary X-ray diffraction analysis of the IPCT domain from A. fulgidus in the apo form are reported. The crystals diffracted to 2.4 Å resolution using a synchrotron source and belonged to the orthorhombic space group P21212, with unit-cell parameters a = 154.7, b = 83.9, c = 127.7 Å.
机译:嗜热古细菌古生菌(Archeeoglobus fulgidus)在热应激下会积累磷酸二肌醇磷酸酯(DIP)。最近,在这种生物体中已经阐明了DIP的生物合成途径,并且涉及一种双功能酶,该酶包含两个域:CTP:肌醇-1-磷酸胞嘧啶转移酶(IPCT)作为可溶性域和di-myo-inositol-1,3' -磷酸-1-磷酸合酶(DIPPS)作为膜结构域。在此,报道了来自Apo fulgidus的Apo形式的IPCT结构域的表达,纯化,结晶和初步X射线衍射分析。晶体使用同步加速器源衍射至2.4Å分辨率,并属于正交晶体空间群P21212,其晶胞参数a = 154.7,b = 83.9,c = 127.7Å。

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