Open AccessCloning, purification, crystallization and preliminary X‐ray diffraction analysis of mouse PACSIN 3 protein
Author(s) -
Bai Xiaoyun,
Meng Geng,
Zheng Xiaofeng
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111049116
Subject(s) - cloning (programming) , resolution (logic) , crystallization , cytoplasm , crystallography , chemistry , actin , vesicle , diffraction , amino acid , microbiology and biotechnology , biology , membrane , biochemistry , physics , optics , organic chemistry , artificial intelligence , computer science , programming language
PACSIN‐family proteins are cytoplasmic proteins that have vesicle‐transport, membrane‐dynamics, actin‐reorganization and microtubule activities. Here, the N‐terminal F‐BAR domain of mouse PACSIN 3, which contains 341 amino acids, was successfully cloned, purified and crystallized. The crystal of PACSIN 3 (1–341) diffracted to 2.6 Å resolution and belonged to space group P 2 1 , with unit‐cell parameters a = 46.9, b = 54.7, c = 193.7 Å, α = 90, β = 96.9, γ = 90°. These data should provide further information on PACSIN‐family protein structures.