title: Crystallization and preliminary crystallographic analysis of the C-terminal domain of MamM, a magnetosome-associated protein from Magnetospirillum gryphiswaldense MSR-1.
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.
authors.affiliation: 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.
authors.forename: Natalie
authors.initials: N
authors.lastname: Zeytuni
authors.forename: Tal
authors.initials: T
authors.lastname: Offer
authors.forename: Geula
authors.initials: G
authors.lastname: Davidov
authors.forename: Raz
authors.initials: R
authors.lastname: Zarivach
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D055944:Magnetosomes / Q000737:chemistry*; D042201:Magnetospirillum / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins