Source:http://linkedlifedata.com/resource/pubmed/id/19851018
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 10
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pubmed:dateCreated |
2009-10-23
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1744-3091
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1042-7
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pubmed:dateRevised |
2011-10-3
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pubmed:meshHeading |
pubmed-meshheading:19851018-Bacterial Proteins,
pubmed-meshheading:19851018-Crystallization,
pubmed-meshheading:19851018-Crystallography, X-Ray,
pubmed-meshheading:19851018-Geobacillus stearothermophilus,
pubmed-meshheading:19851018-Membrane Glycoproteins,
pubmed-meshheading:19851018-Peptide Fragments,
pubmed-meshheading:19851018-Protein Structure, Tertiary
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pubmed:year |
2009
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pubmed:articleTitle |
Towards the structure of the C-terminal part of the S-layer protein SbsC.
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pubmed:affiliation |
Karl-Franzens University, Institute of Molecular Biosciences, Graz, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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