Purification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type II
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Issue Date
1998-07Author
Lamb, Audrey L.
Wang, Xianshu
Napoli, Joseph L.
Newcomer, Marcia E.
Publisher
International Union of Crystallography
Type
Article
Article Version
Scholarly/refereed, publisher version
Metadata
Show full item recordAbstract
One 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°).
Description
This is the publisher's version. Copyright 1998 by the International Union of Crystallography.
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Citation
Lamb, 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.
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