Linked Life Data

21636924

Source:http://linkedlifedata.com/resource/pubmed/id/21636924

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 6
pubmed:dateCreated
2011-6-3
pubmed:abstractText
The binding between two universally conserved translation initiation factors, eIF5B and eIF1A, is important in the initiation step of eukaryotic protein synthesis on the ribosome. Through this interaction, eIF1A assists in recruiting eIF5B to the initiating 40S subunit; eIF5B then encourages the joining of the 60S subunit to form an initiating 80S ribosome. Here, the expression, purification, crystallization and preliminary X-ray analyses of eIF5B?N and the eIF5B?N-eIF1A?N complex from Saccharomyces cerevisiae are reported. The crystal of eIF5B?N diffracted to 2.45?Å resolution and belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 130.0, c = 71.7?Å. The asymmetric unit was estimated to contain one molecule. The initial phase was obtained by Se-SAD. The crystal of the eIF5B?N-eIF1A?N complex diffracted to 3.3?Å resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 101.9, b = 120.9, c = 132.8?Å. The asymmetric unit was estimated to contain two complex molecules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
730-3
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Crystallization and preliminary X-ray crystallographic analysis of eIF5B?N and the eIF5B?N-eIF1A?N complex.
pubmed:affiliation
Graduate School of Life Sciences, Hokkaido University, Sapporo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't