Linked Life Data

1793542

Source:http://linkedlifedata.com/resource/pubmed/id/1793542

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1992-4-6
pubmed:abstractText
The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 A and beta = 110.0 degrees and are in the space group P2(1). Three-dimensional data to 2.0 A have been recorded on film from a single crystal. The orientation and position of the complex in the unit cell have been established using the refined coordinates of subtilisin Carlsberg and of eglin-C as independent models. The structure of the complex has been refined by restrained least-squares minimization. The crystallographic R factor (= sigma[magnitude of Fo - magnitude of Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water molecules. The structure is discussed in terms of its physicochemical properties in solution and its relation to other Bacillus subtilisins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0108-7681
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
47 ( Pt 5)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
707-30
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C.
pubmed:affiliation
European Molecular Biology Laboratory (EMBL), Hamburg, Germany.
pubmed:publicationType
Journal Article, Comparative Study