Cloning, purification, crystallization and preliminary X-ray diffraction analysis of mouse PACSIN 3 protein

被引:1
作者
Bai, Xiaoyun [1 ,2 ]
Meng, Geng [1 ,2 ]
Zheng, Xiaofeng [1 ,2 ]
机构
[1] Peking Univ, Sch Life Sci, State Key Lab Prot & Plant Gene Res, Beijing 100871, Peoples R China
[2] Peking Univ, Sch Life Sci, Dept Biochem & Mol Biol, Beijing 100871, Peoples R China
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2012年 / 68卷
关键词
PACSIN; 3; BAR-domain proteins; F-BAR domain; F-BAR DOMAINS; MEMBRANE CURVATURE; MEDIATED ENDOCYTOSIS; VESICLE FORMATION; SYNDAPIN-II; DYNAMIN; MECHANISM; BIND; PACSIN/SYNDAPIN; INVAGINATION;
D O I
10.1107/S1744309111049116
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 (1341) diffracted to 2.6 angstrom resolution and belonged to space group P21, with unit-cell parameters a = 46.9, b = 54.7, c = 193.7 angstrom, a = 90, beta = 96.9, = 90 degrees. These data should provide further information on PACSIN-family protein structures.
引用
收藏
页码:159 / 162
页数:4
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