Purification, Crystallization and Preliminary X-ray Diffraction of the N-terminal Calmodulin-like Domain of the Human Mitochondrial ATP-Mg/Pi Carrier SCaMC1

Overview

Journal Acta Crystallogr F Struct Biol Commun

Specialty Chemistry

Date 2014 Jan 15

PMID 24419621

Citations 3

Authors

Qin Yang

Sven Bruschweiler

James J Chou

Affiliations

Soon will be listed here.

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.

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