Purification, crystallization and preliminary X-ray diffraction of the N-terminal calmodulin-like domain of the human mitochondrial ATP-Mg/Pi carrier SCaMC1.

Qin Yang, Sven Brüschweiler, James J Chou

Acta crystallographica. Section F, Structural biology communications 2014 Jan

filter terms:

SCaMC is an ATP-Mg/Pi carrier protein located at the mitochondrial inner membrane. SCaMC has an unusual N-terminal Ca(2+)-binding domain (NTD) in addition to its characteristic six-helix transmembrane bundle. The NTD of human SCaMC1 (residues 1-193) was expressed and purified in order to study its role in Ca(2+)-regulated ATP-Mg/Pi transport mediated by its transmembrane domain. While Ca(2+)-bound NTD could be crystallized, the apo state resisted extensive crystallization trials. Selenomethionine-labeled Ca(2+)-bound NTD crystals, which belonged to space group P6(2)22 with one molecule per asymmetric unit, diffracted X-rays to 2.9 Å resolution.

Citation

Qin Yang, Sven Brüschweiler, James J Chou. Purification, crystallization and preliminary X-ray diffraction of the N-terminal calmodulin-like domain of the human mitochondrial ATP-Mg/Pi carrier SCaMC1. Acta crystallographica. Section F, Structural biology communications. 2014 Jan;70(Pt 1):68-71