Open AccessTowards the structure of the C‐terminal part of the S‐layer protein SbsC
Author(s) -
Kroutil Markus,
Pavkov Tea,
BirnerGruenberger Ruth,
Tesarz Manfred,
Sleytr Uwe B.,
Egelseer Eva M.,
Keller Walter
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109035386
Subject(s) - crystallography , s layer , diffraction , crystal structure , monolayer , x ray crystallography , resolution (logic) , protein crystallization , synchrotron radiation , lattice (music) , materials science , chemistry , physics , crystallization , optics , nanotechnology , biochemistry , artificial intelligence , computer science , acoustics , gene , organic chemistry
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 Å 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, P 2 1 and P 4 1 2 1 2, and diffracted to 2.6 and 3 Å 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.