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Updated: May 25, 2026

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
Published on: March 19, 2014
Cloning, purification, crystallization and preliminary X-ray diffraction analysis of mouse PACSIN 3 protein
Xiaoyun Bai1, Geng Meng, Xiaofeng Zheng
1State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing, People's Republic of China.
Abstract:
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.
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