Open AccessCrystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus
Author(s) -
Li Xinxin,
Feng Yanbin,
Liu Xinqi
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113015583
Subject(s) - golgi apparatus , crystallization , crystallography , domain (mathematical analysis) , biology , mitosis , stacking , microbiology and biotechnology , chemistry , mathematical analysis , mathematics , organic chemistry , endoplasmic reticulum
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 P 2 1 2 1 2, 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 .