Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 10
pubmed:dateCreated
2009-10-23
pubmed:abstractText
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 A 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 A 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1042-7
pubmed:dateRevised
2011-10-3
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Towards the structure of the C-terminal part of the S-layer protein SbsC.
pubmed:affiliation
Karl-Franzens University, Institute of Molecular Biosciences, Graz, Austria.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't