Crystallization of retinol dehydratase from Spodoptera frugiperda: improvement of crystal quality by modification by ethylmercury-thiosalicylate

Authors
Pakhomova, S Luz, JG Kobayashi, M Mellman, D Buck, J Newcomer, ME
Citation
S. Pakhomova et al., Crystallization of retinol dehydratase from Spodoptera frugiperda: improvement of crystal quality by modification by ethylmercury-thiosalicylate, ACT CRYST D, 56, 2000, pp. 1641-1643
Citations number
8
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
12
Pages
1641 - 1643
Database
ISI
SICI code
0907-4449(200012)56:<1641:CORDFS>2.0.ZU;2-A
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 P2(1), unit-cell parameters a = 82.05, b = 66.61, c = 84.90 Angstrom, beta = 111.29 degrees) are significantly improved by cova lent modification of the protein with ethylmercury.