Linked Life Data

3042463

Source:http://linkedlifedata.com/resource/pubmed/id/3042463

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-9-20
pubmed:abstractText
Thermitase, the thermostable alkaline protease from Thermoactinomyces vulgaris, has been crystallised in a 1:1 complex with eglin, the inhibitor from the medical leech. Two large crystals were grown, with cell dimensions of a = 49.3 A, b = 67.3 A, c = 90.5 A and space group P2(1)2(1)2(1). The crystals are relatively tightly packed with Vm = 2.1 A3/Da. Three-dimensional data to 1.9 A have been recorded from one of these crystals. The orientation and position of the complex in the unit cell have been established using the subtilisin Carlsberg-eglin structure as a model. The structure of the complex is being refined by restrained least-squares. The present crystallographic R factor (= sigma parallel Fo - Fc parallel/sigma/Fo parallel) is 26% at 2.5 A resolution.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
236
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Crystal structure of a complex between thermitase from Thermoactinomyces vulgaris and the leech inhibitor eglin.
pubmed:affiliation
European Molecular Biology Laboratory, c/o DESY, Hamburg, FRG.
pubmed:publicationType
Journal Article, Comparative Study