Crystallographic analysis of AcrB

Cite This

Files in this item

Checksum: MD5:895df92de7258c94e390b2053f28f77a

POS, Klaas Martinus, André SCHIEFNER, Markus A. SEEGER, Kay DIEDERICHS, 2004. Crystallographic analysis of AcrB. In: FEBS Letters. 564(3), pp. 333-339. ISSN 0014-5793. Available under: doi: 10.1016/S0014-5793(04)00272-8

@article{Pos2004Cryst-8129, title={Crystallographic analysis of AcrB}, year={2004}, doi={10.1016/S0014-5793(04)00272-8}, number={3}, volume={564}, issn={0014-5793}, journal={FEBS Letters}, pages={333--339}, author={Pos, Klaas Martinus and Schiefner, André and Seeger, Markus A. and Diederichs, Kay} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:contributor>Schiefner, André</dc:contributor> <dc:language>eng</dc:language> <dcterms:isPartOf rdf:resource=""/> <dc:contributor>Seeger, Markus A.</dc:contributor> <dc:date rdf:datatype="">2011-03-24T17:40:50Z</dc:date> <dc:creator>Diederichs, Kay</dc:creator> <dc:creator>Pos, Klaas Martinus</dc:creator> <dcterms:bibliographicCitation>First publ. in: FEBS Letters 564 (2004), pp. 333-339</dcterms:bibliographicCitation> <dcterms:hasPart rdf:resource=""/> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <bibo:uri rdf:resource=""/> <dc:creator>Seeger, Markus A.</dc:creator> <dc:contributor>Diederichs, Kay</dc:contributor> <dspace:hasBitstream rdf:resource=""/> <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights> <dc:contributor>Pos, Klaas Martinus</dc:contributor> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dspace:isPartOfCollection rdf:resource=""/> <dcterms:abstract xml:lang="eng">A His-tagged derivative of the multidrug efflux pump AcrB could be crystallized in three different space groups (R3, R32 and P321). Experimental MAD-phasing maps from R32 AcrBHis crystals were obtained to a resolution of 3.5 Å. Datasets of native and substrate soaked AcrBHis crystals were collected at the Swiss Light Source X06SA beamline up to a resolution of 2.7 A+ and re¢nement of these data provided good quality electron density maps,which allowed us to complement the published AcrB structure (PDB code 1iwg). Introduction of amino acids 860-865 and 868 lacking in the 1iwg structure and deletion of a highly disordered region (amino acids 669-678) improved Rfree and average B factors in the 2.7 Å model. We could not identify signi¢cant densities indicating speci¢c antibiotic binding sites in the AcrB R32 space group datasets under the soaking conditions tested.</dcterms:abstract> <dcterms:available rdf:datatype="">2011-03-24T17:40:50Z</dcterms:available> <dc:creator>Schiefner, André</dc:creator> <dcterms:title>Crystallographic analysis of AcrB</dcterms:title> <dc:format>application/pdf</dc:format> <dcterms:rights rdf:resource=""/> <dcterms:issued>2004</dcterms:issued> </rdf:Description> </rdf:RDF>

Downloads since Oct 1, 2014 (Information about access statistics)

65_febs2004.pdf 439

This item appears in the following Collection(s)

Attribution-NonCommercial-NoDerivs 2.0 Generic Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 2.0 Generic

Search KOPS


My Account