Crystallization and preliminary crystallographic analysis of the Magnetospirillum magneticum AMB-1 and M. gryphiswaldense MSR-1 magnetosome-associated proteins MamA.
MamA is a unique magnetosome-associated protein that is predicted to contain six sequential tetratricopeptide-repeat (TPR) motifs. The TPR structural motif serves as a template for protein-protein interactions and mediates the assembly of multi-protein complexes. Here, the crystallization and preliminary X-ray analysis of recombinant and purified Magnetospirillum magneticum and M. gryphiswaldense MamA are reported for the first time. M. gryphiswaldense MamADelta41 crystallized in the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 58.88, c = 144.09 A. M. magneticum MamADelta41 crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 44.75, b = 76.19, c = 105.05 A. X-ray diffraction data were collected to resolutions of 2.0 and 1.95 A, respectively.
Zeytuni
Natalie
N
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.
Zarivach
Raz
R
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D055944:Magnetosomes / Q000737:chemistry*; D042201:Magnetospirillum / Q000737:chemistry*
D001426:Bacterial Proteins