Linked Life Data

9287223

Source:http://linkedlifedata.com/resource/pubmed/id/9287223

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5332
pubmed:dateCreated
1997-9-29
pubmed:databankReference
pubmed:abstractText
Lipidic cubic phases provide a continuous three-dimensional bilayer matrix that facilitates nucleation and growth of bacteriorhodopsin microcrystals. The crystals diffract x-rays isotropically to 2.0 angstroms. The structure of this light-driven proton pump was solved at a resolution of 2.5 angstroms by molecular replacement, using previous results from electron crystallographic studies as a model. The earlier structure was generally confirmed, but several differences were found, including loop conformations and side chain residues. Eight water molecules are now identified experimentally in the proton pathway. These findings reveal the constituents of the proton translocation pathway in the ground state.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1676-81
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases.
pubmed:affiliation
Institut de Biologie Structurale/CEA-CNRS/Université Joseph Fourier, 41 Avenue des Martyrs, F-38027 Grenoble Cedex 1, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't