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Purification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type II

dc.contributor.authorLamb, Audrey L.
dc.contributor.authorWang, Xianshu
dc.contributor.authorNapoli, Joseph L.
dc.contributor.authorNewcomer, Marcia E.
dc.date.accessioned2015-04-24T17:24:00Z
dc.date.available2015-04-24T17:24:00Z
dc.date.issued1998-07
dc.identifier.citationLamb, Audrey L., Xianshu Wang, Joseph L. Napoli, and Marcia E. Newcomer. "Purification, Crystallization and Preliminary X-ray Diffraction Studies of Retinal Dehydrogenase Type II." Acta Crystallographica Section D Biological Crystallography 54.4 (1998): 639-42. http://dx.doi.org/10.1107/S0907444997014121.en_US
dc.identifier.urihttp://hdl.handle.net/1808/17524
dc.descriptionThis is the publisher's version. Copyright 1998 by the International Union of Crystallography.en_US
dc.description.abstractOne enzyme which catalyzes the last step of the formation of the hormone retinoic acid from vitamin A (retinol) is retinal dehydrogenase type II (RalDH2). RalDH2, expressed in the Escherichia coli BL21(DE3) strain, was purified and crystallized using ammonium sulfate as a precipitant. These crystals belong to the space group P212121 (a = 108, b = 150, c = 168 Å, [alpha] = [beta] = [gamma] = 90°).en_US
dc.publisherInternational Union of Crystallographyen_US
dc.titlePurification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type IIen_US
dc.typeArticle
kusw.kuauthorLamb, Audrey Lee
kusw.kudepartmentDepartment of Molecular Biosciencesen_US
dc.identifier.doi10.1107/S0907444997014121
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item does not meet KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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