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The purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes

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dc.contributor.authorJackson, Colin
dc.contributor.authorCarr, Paul D
dc.contributor.authorKim, Hye-Kyung
dc.contributor.authorLiu, Jian-Wei
dc.contributor.authorOllis, David
dc.date.accessioned2015-12-13T23:03:50Z
dc.date.issued2006
dc.date.updated2015-12-12T07:51:49Z
dc.description.abstractThe metallo-glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) has been cloned, expressed in Escherichia coli and purified. Initial screening of crystallization conditions for this enzyme resulted in the identification of needles from one condition in a sodium malonate grid screen. Removal of the metals from the enzyme and subsequent optimization of these conditions led to crystals that diffracted to 2.9 Å and belonged to space group P2 13, with unit-cell parameter a = 164.1 Å. Self-rotation function analysis and VM calculations indicated that the asymmetric unit contains two copies of the monomeric enzyme, corresponding to a solvent content of 79%. It is intended to determine the structure of this protein utilizing SAD phasing from transition metals or molecular replacement.
dc.identifier.issn1744-3091
dc.identifier.urihttp://hdl.handle.net/1885/85099
dc.publisherBlackwell Publishing Ltd
dc.sourceActa Crystallographica Section F: Structural Biology and Crystallization Communications
dc.subjectKeywords: bacterial protein; glycerophosphodiester phosphodiesterase; phosphodiesterase; recombinant protein; article; chemical structure; chemistry; crystallization; Enterobacter aerogenes; enzymology; Escherichia coli; isolation and purification; molecular clonin
dc.titleThe purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes
dc.typeJournal article
local.bibliographicCitation.issue7
local.bibliographicCitation.lastpage661
local.bibliographicCitation.startpage659
local.contributor.affiliationJackson, Colin, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationCarr, Paul D, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationKim, Hye-Kyung, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationLiu, Jian-Wei, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationOllis, David, College of Physical and Mathematical Sciences, ANU
local.contributor.authoruidJackson, Colin, u4040768
local.contributor.authoruidCarr, Paul D, u9206448
local.contributor.authoruidKim, Hye-Kyung, u4025060
local.contributor.authoruidLiu, Jian-Wei, u9604315
local.contributor.authoruidOllis, David, u9200080
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor030499 - Medicinal and Biomolecular Chemistry not elsewhere classified
local.identifier.absfor100103 - Agricultural Molecular Engineering of Nucleic Acids and Proteins
local.identifier.absfor100104 - Genetically Modified Animals
local.identifier.ariespublicationMigratedxPub13307
local.identifier.citationvolume62
local.identifier.doi10.1107/S1744309106020021
local.identifier.scopusID2-s2.0-33745684862
local.type.statusPublished Version

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