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Crystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus.
|Title||Crystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus.|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Authors||Li X, Feng Y, Liu X|
|Journal||Acta crystallographica. Section F, Structural biology and crystallization communications|
|Date Published||2013 Jul|
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.
|Alternate Journal||Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.|