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• W2085296412 startingPage "68" @default.
• W2085296412 abstract "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." @default.
• W2085296412 created "2016-06-24" @default.
• W2085296412 creator A5011725422 @default.
• W2085296412 creator A5030377405 @default.
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• W2085296412 date "2013-12-24" @default.
• W2085296412 modified "2023-09-27" @default.
• W2085296412 title "Purification, crystallization and preliminary X-ray diffraction of the N-terminal calmodulin-like domain of the human mitochondrial ATP-Mg/P_icarrier SCaMC1" @default.
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• W2085296412 doi "https://doi.org/10.1107/s2053230x1303241x" @default.
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