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  • Title: Crystallization and preliminary crystallographic studies of human coactosin-like protein (CLP).
    Author: Li X, Liu X, Zhao Q, Liu Y, Duan X, Rao Z.
    Journal: Acta Crystallogr D Biol Crystallogr; 2004 Dec; 60(Pt 12 Pt 2):2387-8. PubMed ID: 15583396.
    Abstract:
    The human coactosin-like protein (CLP) belongs to the actin-depolymerizing factor (ADF) family of actin-binding proteins. CLP interacts with 5-lipoxygenase (5LO) and filamentous actin (F-actin) via different binding sites. The full-length CLP comprising of 142 amino acids has been overexpressed in Escherichia coli. Crystals of CLP were obtained using the hanging-drop vapour-diffusion technique with ammonium sulfate as precipitant at pH 8.5. Diffraction data to 1.9 A resolution were collected from a crystal belonging to space group P2(1), with unit-cell parameters a = 25.6, b = 55.2, c = 37.4 A, beta = 96.0 degrees. There is one molecule per asymmetric unit.
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