Crystallization and preliminary crystallographic studies of human coactosin-like protein (CLP).

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.