Linked Life Data

19851005

Source:http://linkedlifedata.com/resource/pubmed/id/19851005

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 10
pubmed:dateCreated
2009-10-23
pubmed:abstractText
The Neisseria meningitidis outer membrane protein PorB was expressed in Escherichia coli and purified from inclusion bodies by denaturation in urea followed by refolding in buffered LDAO on a size-exclusion column. PorB has been crystallized in three different crystal forms: C222, R32 and P6(3). The C222 crystal form may contain either one or two PorB monomers in the asymmetric unit, while both the R32 and P6(3) crystal forms contained one PorB monomer in the asymmetric unit. Of the three, the P6(3) crystal form had the best diffraction quality, yielding data extending to 2.3 A resolution.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
996-1000
pubmed:dateRevised
2011-4-7
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Expression, purification and preliminary X-ray analysis of the Neisseria meningitidis outer membrane protein PorB.
pubmed:affiliation
Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232-6600, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural