Crystallization and preliminary X-ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3
Crystallization and preliminary X-ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3
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DOI：
10.1107/s1744309105007815
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发表时间：
2005-04-01
影响因子：
0.9
通讯作者：
Fukui, K
中科院分区：
文献类型：
--
作者：
Lin, LY;Nakano, H;Fukui, K
植物和原核生物保守结构域(PPC)在AT-Hook基序核定位蛋白1(AHL1)中被发现，定位于拟南芥(AtAHL1)的核基质中。AtAHL1具有DNA结合功能。此前对AtAHL1的突变分析表明，PPC结构域的疏水区是其核定位所必需的。本研究采用悬滴气相扩散法对嗜热古细菌平谷热杆菌(PhPPC)的PPC进行了结晶。晶体属六方空间群P6(3)22，晶胞参数a=b=53.69，c=159.2埃。数据是在100K下获得的，观察到的衍射分辨率为1.7埃。还获得了SEMET取代蛋白晶体的完整数据集。
A plant- and prokaryote-conserved domain ( PPC) has previously been found in AT-hook motif nuclear localized protein 1 ( AHL1) localized in the nuclear matrix of Arabidopsis thaliana ( AtAHL1). AtAHL1 has a DNA-binding function. Mutation analyses of AtAHL1 has previously revealed that the hydrophobic region of the PPC domain is essential for its nuclear localization. In this study, the PPC of the hyperthermophilic archaebacterium Pyrococcus horikoshii ( PhPPC) was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to the hexagonal space group P6(3)22, with unitcell parameters a = b = 53.69, c = 159.2 angstrom. Data were obtained at 100 K, with diffraction being observed to a resolution of 1.7 angstrom. A complete data set from crystals of the SeMet-substituted protein was also obtained.