来自褐家鼠的GRASP65 GRASP结构域的结晶及初步晶体学研究。
Crystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus.
作者信息
Li Xinxin, Feng Yanbin, Liu Xinqi
机构信息
State Key Laboratory of Medicinal Chemical Biology and College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, People's Republic of China.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul;69(Pt 7):792-5. doi: 10.1107/S1744309113015583. Epub 2013 Jun 28.
GRASP65 and GRASP55 were classified as Golgi reassembly stacking proteins which play crucial and complementary roles in the stacking of Golgi cisternae. They also participate in vesicle tethering, mitotic progression, the disassembly and reassembly of the Golgi apparatus during mitosis and unconventional secretory pathway regulation. In this study, the expression, crystallization and preliminary crystallographic analysis of the GRASP65 GRASP domain from Rattus norvegicus are presented. The crystals diffracted to 2.0 Å resolution and belonged to space group P21212, with unit-cell parameters a = 44.99, b = 104.29, c = 37.93 Å, α = β = γ = 90°. Furthermore, molecular replacement was employed to determine the structure of the GRASP65 GRASP domain from R. norvegicus.
GRASP65和GRASP55被归类为高尔基体重新组装堆叠蛋白，它们在高尔基体潴泡的堆叠中发挥着关键且互补的作用。它们还参与囊泡拴系、有丝分裂进程、有丝分裂期间高尔基体的解体和重新组装以及非常规分泌途径的调节。在本研究中，展示了来自褐家鼠的GRASP65 GRASP结构域的表达、结晶及初步晶体学分析。这些晶体的衍射分辨率为2.0 Å，属于空间群P21212，晶胞参数为a = 44.99、b = 104.29、c = 37.93 Å，α = β = γ = 90°。此外，采用分子置换法确定了来自褐家鼠的GRASP65 GRASP结构域的结构。
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