PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF RETINAL DEHYDROGENASE TYPE-II

Authors
LAMB AL WANG XS NAPOLI JL NEWCOMER ME
Citation
Al. Lamb et al., PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF RETINAL DEHYDROGENASE TYPE-II, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 639-642
Citations number
19
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
54
Year of publication
1998
Part
4
Pages
639 - 642
Database
ISI
SICI code
0907-4449(1998)54:<639:PCAPDS>2.0.ZU;2-4
Abstract
One enzyme which catalyzes the last step of the formation of the hormo ne retinoic acid from vitamin A (retinol) is retinal dehydrogenase typ e II (RalDH2). RalDH2, expressed in the Escherichia coli BL21(DE3) str ain, was purified and crystallized using ammonium sulfate as a precipi tant. These crystals belong to the space group P2(1)2(1)2(1) (a = 108, b = 150, c = 168 Angstrom, alpha = beta = gamma = 90 degrees).