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Updated: Aug 22, 2026

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
Published on: January 6, 2017
Expression, purification and preliminary crystallographic studies of human coactosin-like protein
Lin Liu1, Yanli Wang, Ping Zhang
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Abstract:
Coactosin-like protein (CLP) is an actin-binding protein as well as a 5-lipoxygenase binding partner. Human coactosin-like protein has been expressed in high yield and the His-tagged protein was purified by affinity chromatography. Several different crystal forms were obtained by the hanging-drop vapour-diffusion method. X-ray diffraction data to 2.0 A resolution were collected from the best crystal. The space group was determined to be P2(1)2(1)2(1), with unit-cell parameters a = 38.4, b = 48.7, c = 72.6 A.
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