Linked Life Data

15299521

Source:http://linkedlifedata.com/resource/pubmed/id/15299521

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
2004-8-9
pubmed:abstractText
The structure of the serine protease trypsin from the North Atlantic salmon (Salmo salar) has been solved by molecular replacement and refined by restrained least-squares methods to a conventional R factor of 16.4% using diffractometer data in the 6.0-1.82 A resolution range (14 443 reflections greater than 3sigma). The model comprises 1793 protein atoms and 180 solvent molecules which were given unit occupancies, and the average temperature factors for protein atoms and solvent oxygen atoms are 15.2 and 36.8 A(2), respectively. The estimated error in atomic positions is about 0.2 A. The structure of salmon trypsin was solved and refined with only a small part of the amino-acid sequence known. However, a gene sequence of salmon trypsin has later become available. Some discrepancies between this sequence and the sequence obtained from the present X-ray crystal study indicate that the mentioned sequences may correspond to isoenzymes. The structure of salmon trypsin is similar to other trypsins of known structure.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
May
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
318-30
pubmed:dateRevised
2007-7-24
pubmed:year
1993
pubmed:articleTitle
Structure determination and refinement of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar) at 1.82 A resolution.
pubmed:affiliation
Protein Crystallography Group, Institute of Mathematical and Physical Sciences, University of Tromsø, Norway.
pubmed:publicationType
Journal Article