Crystallization and preliminary X-ray crystallographic analysis of human PACSIN 1 protein.
PACSIN 1, which is mainly detected in brain tissue, is one of the PACSIN-family proteins involved in endocytosis and recruitment of synaptic vesicles. It binds to dynamin, synaptojanin 1 and N-WASP, and functions in vesicle formation and transport. However, the mechanisms of action of PACSIN 1 in these processes are largely unknown. Here, full-length and five C-terminal truncation constructs of human PACSIN 1 have been successfully expressed and purified in Escherichia coli. PACSIN 1 (1-344) was crystallized and diffracted to a resolution of 3.0 A. The crystal belonged to space group C2, with unit-cell parameters a = 158.65, b = 87.38, c = 91.76 A, alpha = 90.00, beta = 113.61, gamma = 90.00 degrees . There were two molecules in the asymmetric unit and the solvent content was estimated to be about 70.47%.
Bai
Xiaoyun
X
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
Meng
Geng
G
Li
Guoming
G
Luo
Ming
M
Zheng
Xiaofeng
X
D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans
D048868:Adaptor Proteins, Signal Transducing; C492182:PACSIN1 protein, human