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      Crystallization and preliminary crystallographic analysis of the C-terminal domain of MamM, a magnetosome-associated protein from Magnetospirillum gryphiswaldense MSR-1.

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          Abstract

          MamM is a unique magnetosome-associated protein that shares substantial homology with cation diffusion facilitator (CDF) proteins, a group of heavy-metal-ion efflux transporters that participate in metal-ion homeostasis in all domains of life. Magnetotactic bacteria utilize CDF proteins in iron-oxide biomineralization and in magnetosome formation. Here, the crystallization and preliminary X-ray analysis of recombinant Magnetospirillum gryphiswaldense MamM is reported. The C-terminal domain of MamM was crystallized in the orthorhombic space group C222(1), with unit-cell parameters a = 37.1, b = 94.0, c = 53.3 Å. X-ray diffraction data were collected to a resolution of 2.0 Å.

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          Author and article information

          Journal
          Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
          Acta crystallographica. Section F, Structural biology and crystallization communications
          1744-3091
          1744-3091
          Aug 1 2012
          : 68
          : Pt 8
          Affiliations
          [1 ] Department of Life Sciences and National Institute for Biotechnology in the Negev, Ben Gurion University of the Negev, PO Box 653, Beer-Sheva 84105, Israel.
          Article
          S1744309112025638
          10.1107/S1744309112025638
          3412775
          22869124
          d8def76f-2366-48be-b9d9-3318396fdde1
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