Open AccessCrystallization of domains involved in self‐assembly of the S‐layer protein SbsC
Author(s) -
Đordić Anđela,
Egelseer Eva M.,
Tesarz Manfred,
Sleytr Uwe B.,
Keller Walter,
PavkovKeller Tea
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112042650
Subject(s) - crystallization , monolayer , self assembly , crystallography , recombinant dna , layer (electronics) , protein crystallization , s layer , resolution (logic) , materials science , diffraction , chemistry , nanotechnology , biochemistry , physics , gene , organic chemistry , computer science , optics , artificial intelligence
The Gram‐positive bacterium Geobacillus stearothermophilus ATCC 12980 is completely covered with a two‐dimensional crystalline monolayer composed of the S‐layer protein SbsC. In order to complete the structure of the full‐length protein, additional soluble constructs containing the crucial domains for self‐assembly have been successfully cloned, expressed and purified. Crystals obtained from three different recombinant constructs yielded diffraction to 3.4, 2.8 and 1.5 Å resolution. Native data have been collected.