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.
Li
Xuemei
X
National Laboratory of Biomacromolecules, Institute of Biophysics of Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Liu
Xueqi
X
Zhao
Qiang
Q
Liu
Yiwei
Y
Duan
Xin
X
Rao
Zihe
Z
D000199:Actins / Q000737:chemistry; D000645:Ammonium Sulfate / Q000494:pharmacology; D001094:Arachidonate 5-Lipoxygenase / Q000737:chemistry; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000378:metabolism; D008840:Microfilament Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
D000199:Actins; C118115:COTL1 protein, human; D008840:Microfilament Proteins; D001094:Arachidonate 5-Lipoxygenase; D000645:Ammonium Sulfate