Open AccessCrystallization and preliminary crystallographic analysis of a calcineurin B‐like protein 1 (CBL1) mutant from Ammopiptanthus mongolicus
Author(s) -
Shang Guijun,
Cang Huaixing,
Liu Zhijie,
Gao Wei,
Bi Ruchang
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110039667
Subject(s) - crystallization , mutant , crystallography , peg ratio , recombinant dna , calcium , microbiology and biotechnology , chemistry , biology , biochemistry , organic chemistry , finance , economics , gene
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 ( Am CBL1) 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 P 2 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.