Cloning, purification, crystallization and preliminary X-ray diffraction analysis of mouse PACSIN 3 protein.
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 P2(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.
State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, People's Republic of China.
Xiaoyun
X
Bai
Geng
G
Meng
Xiaofeng
X
Zheng
D048868:Adaptor Proteins, Signal Transducing; D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D003598:Cytoskeletal Proteins; D051379:Mice; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000737:chemistry* / Q000302:isolation & purification; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D048868:Adaptor Proteins, Signal Transducing; D003598:Cytoskeletal Proteins; C486019:Pacsin3 protein, mouse; D010750:Phosphoproteins