Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Kroutil, M; Pavkov, T; Birner-Gruenberger, R; Tesarz, M; Sleytr, UB; Egelseer, EM; Keller, W.
Towards the structure of the C-terminal part of the S-layer protein SbsC
ACTA CRYSTALLOGR F-STRUCT BIO. 2009; 65: 1042-1047.
Doi: 10.1107/S1744309109035386
[OPEN ACCESS]
Web of Science
FullText
FullText_MUG
- Co-Autor*innen der Med Uni Graz
- Birner-Grünberger Ruth
- Altmetrics:
- Dimensions Citations:
- Plum Analytics:
- Scite (citation analytics):
- Abstract:
- The S-layer protein SbsC from Geobacillus stearothermophilus ATCC 12980 is the most prevalent single protein produced by the bacterium and covers the complete bacterial surface in the form of a two-dimensional crystalline monolayer. In order to elucidate the structural features of the assembly domains, several N-terminally truncated fragments of SbsC have been crystallized. Crystals obtained from recombinant fragments showed anisotropic diffraction to a maximum of 3.5 angstrom resolution using synchrotron radiation. The best diffracting crystals were obtained from rSbsC((755-1099)), an unintentional in situ proteolytic degradation product of rSbsC((447-1099)). Crystals were obtained in two different space groups, P2(1) and P4(1)2(1)2, and diffracted to 2.6 and 3 angstrom resolution, respectively. Native and heavy-atom derivative data have been collected. The structure of the C-terminal part will yield atomic resolution information for the domains that are crucial for the assembly of the two-dimensional lattice.