Crystallization and preliminary crystallographic analysis of a calcineurin B-like protein 1 (CBL1) mutant from Ammopiptanthus mongolicus.
Calcineurin B-like protein 1 (CBL1) is a calcium sensor in plants. It transmits the calcium signal through the downstream protein CBL-interacting protein kinase (CIPK). CBL1 and CIPK play crucial roles in the response to environmental stresses such as low K+, osmotic shock, high salt, cold and drought. Recombinant CBL1 from Ammopiptanthus mongolicus (AmCBL1) was overexpressed, purified and crystallized. However, the crystal did not diffract well. A mutant prepared using the surface-entropy method and crystallized using the hanging-drop method at 298 K with PEG 2000 MME as a precipitant diffracted to 2.90 Å resolution. The crystal belonged to space group P2(1)2(1)2, with unit-cell parameters a=99.87, b=114.42, c=63.80 Å, α=β=γ=90.00° and three molecules per asymmetric unit.
College of Science, Beijing Forestry University, 35 Qinghuadong Road, Haidian District, Beijing 100083, People's Republic of China.
Guijun
G
Shang
Huaixing
H
Cang
Zhijie
Z
Liu
Wei
W
Gao
Ruchang
R
Bi
D002135:Calcium-Binding Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000737:chemistry*; D050505:Mutant Proteins / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*
D002135:Calcium-Binding Proteins; D050505:Mutant Proteins; D010940:Plant Proteins