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dc.contributor.authorReed, Timothy M.
dc.contributor.authorHirakawa, Hidehiko
dc.contributor.authorMure, Minae
dc.contributor.authorScott, Emily E.
dc.contributor.authorLimburg, Julian
dc.date.accessioned2014-12-18T14:51:33Z
dc.date.available2014-12-18T14:51:33Z
dc.date.issued2008-09-01
dc.identifier.citationReed, T. M.; Hirakawa, H.; Mure, Minae. "Expression, Purification, Crystallization and Preliminary X-ray Studies of Histamine Dehydroganase from Nocardioides simplex." Acta Crystallographica F, 64(9):785-787. http://www.dx.doi.org/10.1107/S1744309108023336.
dc.identifier.issn1744-3091
dc.identifier.urihttp://hdl.handle.net/1808/16166
dc.descriptionThis is the publisher's version, also available electronically from http://scripts.iucr.org/cgi-bin/paper?S1744309108023336.
dc.description.abstractHistamine dehydrogenase (HADH) from Nocardioides simplex catalyzes the oxidative deamination of histamine to produce imidazole acetaldehyde and an ammonium ion. HADH is functionally related to trimethylamine dehydrogenase (TMADH), but HADH has strict substrate specificity towards histamine. HADH is a homodimer, with each 76 kDa subunit containing two redox cofactors: a [4Fe-4S] cluster and an unusual covalently bound flavin mononucleotide, 6-S-cysteinyl-FMN. In order to understand the substrate specificity of HADH, it was sought to determine its structure by X-ray crystallography. This enzyme has been expressed recombinantly in Escherichia coli and successfully crystallized in two forms. Diffraction data were collected to 2.7 Å resolution at the SSRL synchrotron with 99.7% completeness. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 101.14, b = 107.03, c = 153.35 Å.
dc.publisherInternational Union of Crystallography
dc.titleExpression, Purification, Crystallization and Preliminary X-ray Studies of Histamine Dehydroganase from Nocardioides simplex
dc.typeArticle
kusw.kuauthorReed, Timothy M.
kusw.kuauthorHirakawa, Hidehiko
kusw.kuauthorMure, Minae
kusw.kuauthorLimburg, Julian
kusw.kudepartmentChemistry
dc.identifier.doi10.1107/S1744309108023336
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item does not meet KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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