Abstract
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 P412 12 or P43212, with unit-cell parameters a = b = 58.88, c = 144.09 Å. M. magneticum MamAΔ41 crystallized in the orthorhombic space group P212121, 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.
| Original language | English |
|---|---|
| Pages (from-to) | 824-827 |
| Number of pages | 4 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 66 |
| Issue number | 7 |
| DOIs | |
| State | Published - 15 Jul 2010 |
Keywords
- Magnetospirillum gryphiswaldense MSR-1
- Magnetospirillum magneticum AMB-1
- MamA
- magnetosome-associated proteins
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics