Title
Crystallization of retinol dehydratase from Spodoptera frugiperda: Improvement of crystal quality by modification by ethylmercurythiosalicylate
Document Type
Article
Publication Date
12-1-2000
Abstract
Retinol dehydratase is a sulfotransferase which is presumed to catalyze the dehydration of its substrate via a transient retinyl sulfate intermediate. Crystals (space group P21, unit-cell parameters a = 82.05, b = 66.61, c = 84.90 Å, β = 111.29°) are significantly improved by covalent modification of the protein with ethylmercury.
Publication Source (Journal or Book title)
Acta Crystallographica Section D: Biological Crystallography
First Page
1641
Last Page
1643
Recommended Citation
Pakhomova, S., Luz, J., Kobayashi, M., Mellman, D., Buck, J., & Newcomer, M. (2000). Crystallization of retinol dehydratase from Spodoptera frugiperda: Improvement of crystal quality by modification by ethylmercurythiosalicylate. Acta Crystallographica Section D: Biological Crystallography, 56 (12), 1641-1643. https://doi.org/10.1107/S0907444900012671