title: Crystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus.
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.
authors.affiliation: State Key Laboratory of Medicinal Chemical Biology and College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, People's Republic of China.
authors.forename: Xinxin
authors.initials: X
authors.lastname: Li
authors.forename: Yanbin
authors.initials: Y
authors.lastname: Feng
authors.forename: Xinqi
authors.initials: X
authors.lastname: Liu
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D006056:Golgi Apparatus / Q000378:metabolism; D000077614:Golgi Matrix Proteins; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D017434:Protein Structure, Tertiary; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D000077614:Golgi Matrix Proteins; C491577:Gorasp1 protein, rat; D008565:Membrane Proteins; D011994:Recombinant Proteins
keywords: GRASP domain; GRASP65; Golgi; Rattus norvegicus; membrane stacking