Open AccessCrystallization and preliminary crystallographic analysis of the Magnetospirillum magneticum AMB‐1 and M. gryphiswaldense MSR‐1 magnetosome‐associated proteins MamA
Author(s) -
Zeytuni Natalie,
Zarivach Raz
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110018300
Subject(s) - magnetosome , crystallization , crystallography , tetragonal crystal system , orthorhombic crystal system , chemistry , biology , bacteria , crystal structure , paleontology , organic chemistry
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 MamAΔ41 crystallized in the tetragonal space group P 4 1 2 1 2 or P 4 3 2 1 2, with unit‐cell parameters a = b = 58.88, c = 144.09 Å. M. magneticum MamAΔ41 crystallized in the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 44.75, b = 76.19, c = 105.05 Å. X‐ray diffraction data were collected to resolutions of 2.0 and 1.95 Å, respectively.