Crystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus.

TitleCrystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus.
Publication TypeJournal Article
Year of Publication2013
AuthorsLi X, Feng Y, Liu X
JournalActa crystallographica. Section F, Structural biology and crystallization communications
Volume69
IssuePt 7
Pagination792-5
Date Published2013 Jul
Abstract

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.

DOI10.1007/s00586-013-2886-2
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.