Open AccessPurification, crystallization and preliminary X‐ray diffraction studies of retinal dehydrogenase type II
Author(s) -
Lamb Audrey L.,
Wang Xianshu,
Napoli Joseph L.,
Newcomer Marcia E.
Publication year - 1998
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444997014121
Subject(s) - ammonium sulfate , retinoic acid , dehydrogenase , retinal , crystallization , escherichia coli , enzyme , strain (injury) , chemistry , biochemistry , crystallography , biology , chromatography , anatomy , organic chemistry , gene
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 P 2 1 2 1 2 1 ( a = 108, b = 150, c = 168 Å, α = β = γ = 90°).
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