Purification, crystallization and preliminary X‐ray diffraction of the N‐terminal calmodulin‐like domain of the human mitochondrial ATP‐Mg/Pi carrier SCaMC1. Issue 1 (1st January 2014)

• Record Type: Journal Article
• Authors: Yang, Qin; Brüschweiler, Sven; Chou, James J.
• Is Part Of: Acta crystallographica. Volume 70:Issue 1(2014:Jan.)
• Page Start: 68
• Page End: 71
• Publication Date: 2014-01-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X1303241X
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>SCaMC is an ATP‐Mg/P_i carrier protein located at the mitochondrial inner membrane. SCaMC has an unusual N‐terminal Ca²⁺‐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 Ca²⁺‐regulated ATP‐Mg/P_i transport mediated by its transmembrane domain. While Ca²⁺‐bound NTD could be crystallized, the apo state resisted extensive crystallization trials. Selenomethionine‐labeled Ca²⁺‐bound NTD crystals, which belonged to space group <italic>P</italic>6₂22 with one molecule per asymmetric unit, diffracted X‐rays to 2.9 Å resolution.</p> </abstract>