Crystallization and preliminary X‐ray diffraction analysis of the N‐terminal domain of Mrs2, a magnesium ion transporter from yeast inner mitochondrial membrane
Mrs2 transporters are distantly related to the major bacterial Mg2+ transporter CorA and to Alr1, which is found in the plasma membranes of lower eukaryotes. Common features of all Mrs2 proteins are the presence of an N‐terminal soluble domain followed by two adjacent transmembrane helices (TM1 and TM2) near the C‐terminus and of the highly conserved F/Y‐G‐M‐N sequence motif at the end of TM1. The inner mitochondrial domain of the Mrs2 from Saccharomyces cerevisae was overexpressed, purified and crystallized in two different crystal forms corresponding to an orthorhombic and a hexagonal space group. The crystals diffracted X‐rays to 1.83 and 4.16 Å resolution, respectively. Matthews volume calculations suggested the presence of one molecule per asymmetric unit in the orthorhombic crystal form and of five or six molecules per asymmetric unit in the hexagonal crystal form. The phase problem was solved for the orthorhombic form by a single‐wavelength anomalous dispersion experiment exploiting the sulfur anomalous signal.
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