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 P21212, 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.
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