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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus
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Crystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus

机译：褐家鼠GRASP65 GRASP结构域的结晶和初步晶体学研究

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摘要

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 angstrom resolution and belonged to space group P2(1)2(1)2, with unit-cell parameters a = 44.99, b = 104.29, c = 37.93 angstrom, alpha = beta = gamma = 90 degrees. Furthermore, molecular replacement was employed to determine the structure of the GRASP65 GRASP domain from R. norvegicus.
机译：GRASP65和GRASP55被归类为高尔基体重组堆叠蛋白，它们在高尔基蓄水池的堆叠中起关键和互补的作用。它们还参与有丝分裂中的囊泡束缚，有丝分裂进程，高尔基体的拆卸和重新组装以及非常规的分泌途径调节。在这项研究中，提出了褐家鼠的GRASP65 GRASP结构域的表达，结晶和初步晶体学分析。晶体衍射到2.0埃分辨率，并属于空间群P2（1）2（1）2，其晶胞参数a = 44.99，b = 104.29，c = 37.93埃，α=β=伽马= 90度。此外，采用分子置换来确定来自R. norvegicus的GRASP65 GRASP结构域的结构。

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